CN110023474A - 酶用于洗涤的用途、洗涤方法和器皿洗涤组合物 - Google Patents
酶用于洗涤的用途、洗涤方法和器皿洗涤组合物 Download PDFInfo
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- CN110023474A CN110023474A CN201780057836.7A CN201780057836A CN110023474A CN 110023474 A CN110023474 A CN 110023474A CN 201780057836 A CN201780057836 A CN 201780057836A CN 110023474 A CN110023474 A CN 110023474A
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Classifications
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- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
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- C11D3/38—Products with no well-defined composition, e.g. natural products
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- C11D3/38618—Protease or amylase in liquid compositions only
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Abstract
本发明涉及淀粉酶和/或蛋白酶用于去除和/或减少表面上的污垢的用途，一种用于去除和/或减少表面上的污垢的方法，和一种器皿洗涤组合物。
Description
技术领域
本发明涉及淀粉酶和/或蛋白酶用于去除和/或减少表面上的污垢的用途，一种用于去除和/或减少表面上的污垢的方法，和一种器皿洗涤组合物。
对序列表的引用
本申请包含计算机可读形式的序列表，将其通过引用结合在此。
序列表综述
SEQ ID NO:1是α-淀粉酶(AA560)的氨基酸序列
SEQ ID NO:2是α-淀粉酶(SP722)的氨基酸序列
SEQ ID NO:3是α-淀粉酶(Termamyl)的氨基酸序列
SEQ ID NO:4是融合α-淀粉酶的氨基酸序列
SEQ ID NO:5是蛋白酶(克劳氏芽孢杆菌)的氨基酸序列
SEQ ID NO:6是蛋白酶(地衣芽孢杆菌)的氨基酸序列
SEQ ID NO:7是蛋白酶(耐盐芽孢杆菌)的氨基酸序列
SEQ ID NO:8是蛋白酶(解淀粉芽孢杆菌，BNP’)的氨基酸序列
SEQ ID NO:9-17是枯草杆菌蛋白酶抑制剂的氨基酸序列。
SEQ ID NO:18是地衣多糖酶(licheninase)(粘琼脂芽孢杆菌(Bacillusagaradhaerens))的氨基酸序列
SEQ ID NO:19是地衣多糖酶(芽孢杆菌属物种-62449)的氨基酸序列
SEQ ID NO:20是地衣多糖酶(芽孢杆菌属物种-62449)的氨基酸序列
SEQ ID NO:21是地衣多糖酶(秋叶氏芽孢杆菌)的氨基酸序列
SEQ ID NO:22是地衣多糖酶(莫哈韦芽孢杆菌(Bacillus mojavensis))的氨基酸序列
SEQ ID NO:23是SEQ ID NO:18的地衣多糖酶的His-标记的重组成熟氨基酸序列
SEQ ID NO:24是变体蛋白酶的氨基酸序列。
附图说明
图1示出了具有和不具有淀粉酶和/或蛋白酶的温和pH的器皿洗涤洗涤剂组合物的洗涤性能。
图2示出了温和pH的器皿洗涤洗涤剂组合物和可商购的器皿洗涤洗涤剂组合物的洗涤性能。
背景技术
工业的和机构的器皿洗涤是在工业的、商业的或机构的情况中所应用的器皿洗涤工艺，以在尽可能短的时间段内提供洁净卫生的器皿。为了实现这种结果，器皿洗涤器通常在洗涤过程期间施用高温和强机械的和强化学的作用。
在大部分器皿洗涤应用中，由于容量约束，限制了可用于洗涤的时间。一般，洗涤循环在10秒与5分钟之间。为了克服这些时间约束并且交付洁净卫生的器皿，器皿洗涤器通常向该器皿施用高水平的机械作用。这通常使用通过喷嘴分布的高压水来完成的，并且将其在器皿洗涤器中再循环。在一些情况下，可以将研磨元件引入该系统(例如，聚合物珠)中，以提高水对弄脏器皿的机械作用。尽管在器皿洗涤过程中施用高度机械作用，但仍依赖强化学作用来交付所需水平的清洁度，并且如果需要的话，交付所需水平的卫生。器皿洗涤化学品特征在于一般为高碱性的并且包含其他元素来提高清洁性能，来确保令人满意的结果，并且来保护器皿洗涤机免于潜在腐蚀性的碱性化学品。
用于工业的和机构的器皿洗涤的器皿洗涤洗涤剂组合物包括设计用于从器皿上去除污渍和污垢的苛刻化学品。作为实例，工业器皿洗涤组合物包含最高达50％的氢氧化钠，导致组合物的pH高于10.5并且pH最高达13.5。高pH的洗涤剂造成安全问题，因为许多操作人员没有经过适当地培训。因此，使用这些器皿洗涤洗涤剂的操作员暴露于腐蚀性化学品，这意味着当他们操作器皿洗涤器时需要额外的预防措施。此外，组合物中的苛刻化学品对周围事物和环境造成问题。
发明内容
本发明涉及淀粉酶和/或蛋白酶用于去除和/或减少表面上的污垢的用途，其中将所述表面暴露于所述淀粉酶和/或蛋白酶持续10至240秒的时间段。
还要求保护一种用于去除和/或减少表面上的污垢的方法，其中清洁循环包括以下步骤：
i.洗涤步骤，其中将所述表面暴露于包含以下项的洗涤液
a.淀粉酶和/或蛋白酶和任选的洗涤剂组分，或
b.根据本发明的器皿洗涤洗涤剂组合物，
ii.任选地排出部分所述洗涤液，
iii.任选地漂洗所述表面，
iv.任选地干燥所述表面；
其中将所述表面暴露于所述洗涤液持续在10至240秒范围内的时间段。
本发明还涉及一种包含淀粉酶和/或蛋白酶和一种或多种洗涤剂组分的器皿洗涤洗涤剂组合物，所述组合物具有在7-10.5范围内的pH。
定义
清洁水：术语“清洁水”是指在先前的清洁循环中未用作洗涤液的水。
清洁循环：术语“清洁循环”在本文中定义为清洁操作，其中通过使洗涤液循环并将洗涤液喷到器皿上而使器皿与洗涤液接触一段时间以便清洁器皿。将器皿任选地漂洗和干燥。
洗涤剂组分：术语“洗涤剂组分”是指可以包含在器皿洗涤洗涤剂组合物中的成分。此类组分可以促进清洁过程。洗涤剂组分的实例是表面活性剂、助洗剂、螯合剂(chelator)或螯合试剂(chelating agent)、漂白体系或漂白组分、聚合物、增泡剂、抑泡剂、染料、香料、晦暗抑制剂、光学增亮剂、杀细菌剂、杀真菌剂、污垢悬浮剂、防腐蚀剂、酶抑制剂或稳定剂、酶活化剂、一种或多种转移酶、水解酶、氧化还原酶、上蓝剂和荧光染料、抗氧化剂、以及增溶剂。
器皿洗涤洗涤剂组合物：术语“器皿洗涤洗涤剂组合物”是指可用于从待清洁的表面(例如器皿的表面或器皿洗涤机内部存在的表面)去除和/或减少不希望的化合物的组合物。
器皿洗涤洗涤剂组合物可以是旨在用于减少和/或去除盘、餐桌用餐具、罐、锅、刀叉的污垢的任何组合物和用于减少和/或去除洗碗机内表面的污垢的组合物的所有形式。本发明不限于任何特定类型的器皿洗涤洗涤剂组合物。这些术语包括为所希望的特定类型的清洁组合物选择的任何洗涤剂组分和产品形式(例如，液体、凝胶、粉末、棒、颗粒、糊剂或喷雾组合物)。洗涤剂组合物可含有除了组合物中包含的淀粉酶和/或蛋白酶外的酶，例如一种或多种另外的酶，例如蛋白酶、淀粉酶、脂肪酶、角质酶、纤维素酶、内切葡聚糖酶、木葡聚糖酶、果胶酶、果胶裂解酶、黄原胶酶、过氧化物酶、卤代过氧合酶、过氧化氢酶和甘露聚糖酶，或其任何混合物；和洗涤剂组分。
器皿洗涤机：术语“器皿洗涤机”是指可用于工业的或机构的器皿洗涤的任何种类的洗涤机。该术语包括但不限于门器皿洗涤机、罩器皿洗涤机、传送带器皿洗涤机、台下器皿洗涤机(undercounter warewashing machine)、玻璃洗涤器、飞机器皿洗涤机(flightwarewashing machine)、罐和锅器皿洗涤机和器具洗涤器。
器皿：术语“器皿”旨在是指任何形式的餐具、厨房用具、成套餐具或餐桌用餐具，例如但不限于锅、盘、饮水玻璃杯、杯子、刀、叉、匙、瓷器等。该器皿可以是由任何适合的材料(例如金属、玻璃、橡胶、塑料、PVC、丙烯酸材料、陶瓷、瓷器或瓷料)制成。
改善的洗涤性能：术语“改善的洗涤性能”在本文中定义为相对于不含酶或不含酶的共混物的类似洗涤剂的洗涤性能显示出增加的洗涤性能的酶或酶的共混物，例如通过提高的污垢去除或提高的污垢减少。
洗涤性能：术语“洗涤性能”用作酶在例如清洁循环期间去除或减少待清洁表面上存在的污垢的能力。
变体：术语“变体”意指在一个或多个(例如，若干个)位置处包含改变(即，取代、插入和/或缺失)的与亲本酶具有相同活性的多肽。取代意指用不同的氨基酸替代占用某一位置的氨基酸；缺失意指去除占用某一位置的氨基酸；并且插入意指邻接并且紧随占用某一位置的氨基酸之后添加氨基酸。
洗涤液：术语“洗涤液”旨在意指用于硬表面清洁或用于餐具洗涤的水和洗涤剂的溶液或混合物(任选地包括酶)。
如在此使用的术语“水硬度”或“硬度”(degree of hardness)或“dH”或“°dH”是指德国硬度(German degrees of hardness)。一度被定义为10毫克氧化钙/升水。
变体命名惯例
出于本发明的目的，SEQ ID NO:1、2、3、4、5、6、7、8、9、10、11、12、13、14、15、16、17、18、19或20中披露的多肽可以用于确定另一种多肽中对应的氨基酸残基。将另一种多肽的氨基酸序列与SEQ ID NO:1、2、3、4、5、6、7、8、9、10、11、12、13、14、15、16、17、18、19或20中披露的多肽(这取决于它是α-淀粉酶、蛋白酶、枯草杆菌蛋白酶抑制剂还是地衣多糖酶)进行比对，并且基于该比对，使用如在EMBOSS软件包(EMBOSS:The European MolecularBiology Open Software Suite[EMBOSS：欧洲分子生物学开放软件套件]，Rice等人，2000，Trends Genet.[遗传学趋势]，16:276-277)(优选5.0.0版本或更新版本)的尼德尔(Needle)程序中所实施的尼德曼-翁施算法(Needleman-Wunsch algorithm)(Needleman和Wunsch，1970，J.Mol.Biol.[分子生物学杂志]48:443-453)确定对应于在SEQ ID NO:1、2、3、4、5、6、7、8、9、10、11、12、13、14、15、16、17、18、19或20中披露的多肽中的任何氨基酸残基的氨基酸位置编号。使用的参数是缺口开放罚分10、缺口扩展罚分0.5以及EBLOSUM62(BLOSUM62的EMBOSS版本)取代矩阵。
可以通过使用若干种计算机程序，使用其相应的默认参数比对多个多肽序列来确定在另一种酶中的对应氨基酸残基的鉴定，所述计算机程序包括但不限于MUSCLE(通过对数期望值的多种序列比较；版本3.5或更新版本；Edgar,2004,Nucleic Acids Research[核酸研究]32:1792-1797)、MAFFT(版本6.857或更新版本；Katoh和Kuma,2002,Nucleic AcidsResearch[核酸研究]30:3059-3066；Katoh等人,2005,Nucleic Acids Research[核酸研究]33:511-518；Katoh和Toh,2007,Bioinformatics[生物信息学]23:372-374；Katoh等人,2009,Methods in Molecular Biology[分子生物学方法]537:39-64；Katoh和Toh,2010，Bioinformatics[生物信息学]26:1899-1900)以及采用ClustalW的EMBOSS EMMA(1.83或更新版本；Thompson等人,1994,Nucleic Acids Research[核酸研究]22:4673-4680)。
当其他酶与SEQ ID NO:1、2、3、4、5、6、7、8、9、10、11、12、13、14、15、16、17、18、19或20的多肽相背离使得传统的基于序列的比较方法不能检测其相互关系时(Lindahl和Elofsson,2000,J.Mol.Biol.[分子生物学杂志]295:613-615)，可以使用其他成对序列比较算法。在基于序列的搜索中较高的敏感度可使用搜索程序来获得，这些搜索程序采用多肽家族的概率表现(谱)来搜索数据库。例如，PSI-BLAST程序通过迭代数据库搜索过程来产生多个谱，并且能够检测远距离同源物(Atschul等人，1997，NucleicAcids Res.[核酸研究]25:3389-3402)。如果多肽的家族或超家族具有在蛋白结构数据库中的一个或多个代表，甚至可以实现更高的敏感度。程序例如GenTHREADER(Jones,1999,J.Mol.Biol.[分子生物学杂志]287:797-815；McGuffin和Jones,2003,Bioinformatics[生物信息学]19:874-881)利用来自多种来源(PSI-BLAST、二级结构预测、结构比对谱、以及溶剂化势)的信息作为预测查询序列的结构折叠的神经网络的输入。类似地，Gough等人,2000,J.Mol.Biol.[分子生物学杂志]313:903-919的方法可以用于比对未知结构的序列与存在于SCOP数据库中的超家族模型。这些比对进而可以用于产生多肽的同源性模型，并且使用出于该目的而开发的多种工具可以评估此类模型的准确度。
对于已知结构的蛋白质，若干工具和资源可用于检索并产生结构比对。例如，蛋白的SCOP超家族已在结构上进行比对，并且那些比对是可访问的并且可下载的。可以使用多种算法如距离比对矩阵(Holm和Sander,1998,Proteins[蛋白质]33:88-96)或组合延伸(Shindyalov和Bourne,1998,Protein Engineering[蛋白质工程]11:739-747)比对两种或更多种蛋白质结构，并且这些算法的实施可以另外用于查询具有感兴趣结构的结构数据库，以便发现可能的结构同源物(例如，Holm和Park,2000,Bioinformatics[生物信息学]16:566-567)。
当必须鉴定相应的氨基酸位置时确定使用哪种比对工具是在技术人员的知识范围内。因此，考虑了在本发明的上下文中可以使用本领域技术人员发现适合的任何可用的比对工具。
在描述在此所述的酶变体中，以下所述的命名法适于方便参考。采用公认的IUPAC单字母或三字母氨基酸缩写。氨基酸位置表示为H1、G109等。
在此所述的变体与亲本多肽相比包含一个或多个修饰。因此，变体可以包含保守修饰，具体而言，此类保守修饰可以是保守取代。保守取代的实例是在下组之内：碱性氨基酸(精氨酸、赖氨酸及组氨酸)、酸性氨基酸(谷氨酸和天冬氨酸)、极性氨基酸(谷氨酰胺和天冬酰胺)、疏水性氨基酸(亮氨酸、异亮氨酸和缬氨酸)、芳香族氨基酸(苯丙氨酸、色氨酸和酪氨酸)及小氨基酸(甘氨酸、丙氨酸、丝氨酸、苏氨酸和甲硫氨酸)。一般不会改变比活性的氨基酸取代是本领域已知的并且例如由H.Neurath和R.L.Hill,1979,于The Proteins[蛋白质]，学术出版社(Academic Press)，纽约中描述。常见的取代包括：Ala/Ser、Val/Ile、Asp/Glu、Asn/Gln、Thr/Ser、Ala/Gly、Ala/Thr、Ser/Asn、Ala/Val、Ser/Gly、Tyr/Phe、Ala/Pro、Lys/Arg、Asp/Asn、Glu/Gln、Leu/Ile、Leu/Val、Ala/Glu以及Asp/Gly。
可替代地，这些氨基酸改变具有这样一种性质：改变多肽的物理化学特性。例如，氨基酸改变可以改进多肽的热稳定性、改变底物特异性、改变最适pH等。
取代：对于氨基酸取代，使用以下命名法：原始氨基酸、位置、取代的氨基酸。因此，在位置G109处的甘氨酸被丙氨酸取代表示为“Gly109Ala”或“G109A”。多个突变由加号(“+”)或由逗号(“,”)分开，例如“Gly109Ala+Leu173Pro”或“G109A,L173P”表示在位置109和173处的甘氨酸(G)和亮氨酸(L)分别被丙氨酸(A)和脯氨酸(P)取代。如果在给定位置中可以取代多于一种氨基酸，那么将这些氨基酸以分隔号(例如/)列出或分开。因此，如果根据本发明的Ala和Pro两者都可以被取代，代替占据位置109的氨基酸，这被表示为X109A/P，其中本实例中的X表明不同酶可以是亲本，例如像具有SEQ ID NO:1的α-淀粉酶或与其具有至少75％同一性的α-淀粉酶。因此，在一些情况下，将这些变体表示为109A/P或X109A/P，表明将被取代的氨基酸取决于亲本酶而变化。
缺失：对于氨基酸缺失，使用以下命名法：原有氨基酸、位置、*。因此，将在位置181处的精氨酸的缺失表示为“Arg181*”或“R181*”。多个缺失由加号(“+”)或逗号分开，例如“Arg181*+Gly182*”或“R181*+G182*”或“R181*,G182*”。
插入：另外的氨基酸残基的插入，例如像在G#1之后插入赖氨酸可表示为：Gly#1GlyLys或G#1GK。可替代地，另外的氨基酸残基的插入，如在G109之后插入赖氨酸可表示为：*109aL。当插入多于一个的氨基酸残基，例如像在109之后插入Lys和Ala时，这种插入可表示为：Gly109GlyLysAla或G109GKA。在此类情况下，还可以通过将小写字母添加到在所插入的一个或多个氨基酸残基之前的氨基酸残基位置编号处来对所插入的一个或多个氨基酸残基进行编号，在该实例中：*109aK*109bA。
总而言之，取代、缺失和插入在本文中可以被称为“修饰”。因此，应当理解的是，除非上下文另有说明在此描述的任何变体包括修饰，例如取代、缺失和/或插入。
多个修饰：包含多个修饰的变体由加号(“+”)、分隔号(“/”)或由逗号(“，”)分开，例如，“Gly109Pro+Lys391Ala”或“G109P,K391A”表示在位置109处的甘氨酸和在位置391处的赖氨酸分别如上所述被脯氨酸和丙氨酸取代。
不同修饰：在可以在一个位置上引入不同的修饰的情况下，这些不同的修饰由分隔号(“/”)或由逗号(“，”)分开，例如“Gly109Pro,Lys”或“G109P,K”表示在位置109处的甘氨酸被脯氨酸或赖氨酸取代。因此，“Gly109Pro,Lys+Lys391Ala”指示了以下变体：“Gly109Pro+Lys391Ala”、“Gly109Lys+Lys391Ala”或“G109P,K+K391A”。
具体实施方式
工业的和机构的器皿洗涤是在工业的、商业的或机构的情况中所应用的工艺，以在尽可能短的时间段内提供洁净卫生的器皿。为了实现这种结果，器皿洗涤器通常在洗涤过程中施用高温和强机械的和强化学的作用。
诸位发明人已经发现了更环保的方式来进行器皿洗涤而不使用苛刻的化学品。新用途和方法涉及在器皿洗涤过程中使用淀粉酶和/或蛋白酶。当酶用于从待洗涤的表面去除和/或减少污垢时，可以降低器皿洗涤洗涤剂组合物的pH。使用较不苛刻的化学品对环境和执行洗涤过程的操作员的安全性具有影响。
诸位发明人已经发现，在器皿洗涤过程中使用淀粉酶和/或蛋白酶来去除和/或减少表面上的污垢实际上是可能的。在工业厨房中例如在餐馆中在很短的时间内，例如几分钟或甚至不到一分钟内进行器皿洗涤是至关重要的。在本发明的一个实施例中，将表面暴露于淀粉酶和/或蛋白酶持续10至240秒的时间段。此外，本发明涉及一种用于去除和/或减少表面上的污垢的方法，其中清洁循环包括以下步骤：
i.洗涤步骤，其中将所述表面暴露于包含以下项的洗涤液
a.淀粉酶和/或蛋白酶和任选的洗涤剂组分，或
b.根据本发明的器皿洗涤洗涤剂组合物，
ii.任选地排出部分所述洗涤液，
iii.任选地漂洗所述表面，
iv.任选地干燥所述表面；
其中将所述表面暴露于所述洗涤液持续在10至240秒范围内的时间段。
所述表面可以暴露于所述淀粉酶和/或蛋白酶持续10至220秒的时间段，例如在10至200秒的范围内、在10至180秒的范围内、在10至160秒的范围内、在10至140秒的范围内、在10至120秒的范围内、在10至100秒的范围内、在10至80秒的范围内、在10至70秒的范围内、在10至66秒的范围内、在20至66秒的范围内、在25至66秒的范围内、在28至66秒的范围内、在28至60秒的范围内、在28至55秒的范围内、在28至50秒的范围内或在28至45秒的范围内。
本发明人已经证明，单独使用的淀粉酶或蛋白酶显示出改善的洗涤性能，并且当将酶一起使用时，酶表现出协同效应。
在本发明方法中使用淀粉酶和/或蛋白酶的另一个优点是酶防止污垢在表面上的再沉积。在一个实施例中，蛋白酶用于本发明的方法中并防止污垢在待清洁表面上的再沉积。在本发明的另一个实施例中，淀粉酶用于本发明的方法中并防止污垢在待清洁表面上的再沉积。在本发明的第三个实施例中，蛋白酶连同淀粉酶一起用于本发明的方法中并防止污垢在待清洁表面上的再沉积。
在本发明的一个实施例中，清洁循环包括漂洗步骤和/或干燥步骤。在一个实施例中，清洁水任选地与漂洗助剂一起用于漂洗步骤。该漂洗助剂可包括二甲苯磺酸钠、异丙醇、胺聚二醇缩合物、醇烷氧基化物、羟基乙酸、醇烷氧基化物、聚氧丙烯-聚氧乙烯、柠檬酸、脲、丙烯酸、烷氧基化醇、2-丙烯酸调聚物、钠盐、三芳基甲烷和具有环氧乙烷的甲基-环氧乙烷聚合物。
在一个实施例中，该方法包括在步骤a之前的浸泡步骤。
在操作器皿洗涤过程中，将器皿洗涤机的内表面暴露于包含潜在高水平有机污垢的水中，并且随着时间推移，污垢膜或沉积物会在器皿洗涤机的内表面上形成。在正常每日清洁操作过程中，这种膜可能潜在是不易去除的。在器皿洗涤过程(其中污垢膜存在于机器的内表面上)中，经常会看到性能降低、化学剂量需求增加、恶臭以及机器内生物膜的形成。
清洁循环可包括排出步骤，其中部分洗涤液被排出。在一个实施例中，来自漂洗步骤c的清洁水替换所排出的洗涤液。5％-15％的洗涤液可以被清洁水替换，例如7.5％的洗涤液被清洁水替换。洗涤液可以在随后的清洁循环中重复使用。洗涤液的pH可以在7.5-10.5的范围内、例如在7.5-10的范围内、在7.5-9.5的范围内、在7.5-9.0的范围内、在7.5-8.5的范围内、在7.5-8.2的范围内、或在7.8-8.2的范围内。洗涤液的温度可以在50℃-95℃的范围内、例如在50℃-90℃的范围内、在50℃-85℃的范围内、在50℃-80℃的范围内、在50℃-75℃的范围内、在50℃-70℃的范围内、在50℃-65℃的范围内、55℃-62℃或在58℃-62℃的范围内。
表面可经历清洁循环1次、2次、3次、4次或甚至5次。
在本发明的一个实施例中，洗涤液包含一种或多种选自下组的洗涤剂组分，该组由以下组成：表面活性剂、助洗剂、螯合剂或螯合试剂、漂白体系或漂白组分、聚合物、增泡剂、抑泡剂、染料、香料、晦暗抑制剂、光学增亮剂、杀细菌剂、杀真菌剂、污垢悬浮剂、抗腐蚀剂、酶稳定剂、酶抑制剂或活化剂、一种或多种转移酶、水解酶、氧化还原酶、上蓝剂和荧光染料、抗氧化剂、以及增溶剂。洗涤剂组分可以单独加入洗涤液中或作为包含洗涤剂组分和淀粉酶和/或蛋白酶的器皿洗涤洗涤剂组合物。根据本发明的器皿洗涤组合物包含淀粉酶和/或蛋白酶和一种或多种洗涤剂组分，该组合物具有在7-10.5范围内的pH。该组合物可包含至少5％wt.的螯合剂和/或少于2％的表面活性剂。在本发明的一个实施例中，该组合物不包含表面活性剂。该组合物是用于工业或机构用途的器皿洗涤组合物并且可以具有在7.5-10.5的范围内、例如在7.5-10的范围内、在7.5-9.5的范围内、在7.5-9.0的范围内、在7.5-8.5的范围内、在7.5-8.2的范围内、或在7.8-8.2的范围内的pH。因此，该组合物的pH低于其他器皿洗涤洗涤剂组合物并且因此可以使用而没有操作者或环境安全问题。
器皿洗涤洗涤剂组合物的浓度在0.5-5g/升洗涤液的范围内，例如在1-4g/升洗涤液的范围内，例如1.5-3g/升洗涤液的范围内。在优选的实施例中，浓度为2g/升洗涤液。
考虑到宽范围的器皿洗涤器的潜在应用，存在各种各样的可用系统。这些包括单洗涤台下系统(类似于家用洗碗机)、连帽单次使用系统、用于连续操作的更大或严重弄脏的设备和大型输送机或飞行机的系统。器皿洗涤器通常包含洗涤水的储槽或储罐。此储槽的目的是通过允许在一段时间或洗涤内重复使用和再循环水来减少水和器皿洗涤化学品消耗。这节省了水和用于加热水的能量。
本发明可以在各种器皿洗涤机中进行，包括工业器皿洗涤机。
用于去除和/或减少表面上的污垢的方法可以在器皿洗涤机中进行，该器皿洗涤机选自下组，该组由以下组成：门器皿洗涤机、罩器皿洗涤机、传送带器皿洗涤机、台下器皿洗涤机、玻璃洗涤器、飞机器皿洗涤机、罐和锅器皿洗涤机和器具洗涤器。在本发明的一个实施例中，待清洁的表面是器皿洗涤机的内表面或器皿的表面。
该组合物可以处于以下形式：条，块，均匀的片剂，具有两层或更多层的片剂，具有一个或多个室的袋，规则的或压缩的粉末，颗粒，膏，凝胶，或者规则的、压缩的或浓缩的液体。
固体器皿洗涤洗涤剂组合物包括有效量的清洁剂和碱源(用于提供污垢去除)，用于粘合组合物的固化剂和支链脂肪酸分解剂(用于提供固体洗涤剂组合物在水性应用溶液中的改善的溶解)。所述支链脂肪酸分解剂选自下组，该组由以下组成：异壬酸钠、异壬酸、异辛酸钠、异辛酸、新癸酸钠、新癸酸、新戊酸钠、新戊酸、新庚酸钠、新庚酸、3,5,5-三甲基己酸、6-甲基-庚酸、2,2-二甲基辛酸、新戊酸(2,2-二甲基丙酸)、2,2-二甲基戊酸、及其盐、或其混合物。
在一个实施例中，所述组合物是当在68℃下暴露于4000mL水溶液时具有至少15g/分钟的溶解速率的块或片剂。
在一个实施例中，所述组合物是液体器皿洗涤组合物。
洗涤液和器皿洗涤组合物可包含选自下组的另外的酶，该组由以下组成：另外的蛋白酶、脂肪酶、角质酶、另外的淀粉酶、糖酶、纤维素酶、果胶酶、甘露聚糖酶、阿拉伯糖酶、半乳聚糖酶、木聚糖酶、氧化酶、地衣多糖酶、漆酶和/或过氧化物酶。洗涤液可以供应有来自单独容器的酶和洗涤剂组分，并且另外淀粉酶和蛋白酶以及任选的另外的酶可以从单独的容器供应。
器皿洗涤组合物可包含一种或多种蛋白酶抑制剂，或者一种或多种蛋白酶抑制剂可包含在洗涤液中。这些蛋白酶抑制剂中的至少一种是肽醛、其亚硫酸氢盐加合物或半缩醛加合物。典型地加入一种或多种蛋白酶抑制剂以改善器皿洗涤组合物的稳定性，特别是用于液体组合物，并且以这种方式改善组合物的保存期限，因此可以在使用之前储存更长的时间段并且在器皿洗涤过程中仍然提供相同的性能。
在一个实施例中，所述蛋白酶抑制剂是式P-(A)y-L-(B)x-B0-H的肽醛或其亚硫酸氢盐加合物或半缩醛加合物，其中：
i.H是氢；
ii.B0是具有式-NH-CH(R)-C(＝O)-的L-或D-构型的单一氨基酸残基；
iii.(B)x的x是1、2或3，并且B独立地是经由(B)x氨基酸的C端连接到B0上的单一氨基酸
iv.L不存在或L独立地是式-C(＝O)-、-C(＝O)-C(＝O)-、-C(＝S)-、-C(＝S)-C(＝S)-或-C(＝S)-C(＝O)-的连接基团；
v.(A)y的y是0、1或2，并且A独立地是经由(A)y氨基酸的N端连接到L上的单一氨基酸残基，其前提是如果L不存在，那么A不存在；
vi.P选自下组，该组由以下组成：氢和N端保护基团，其前提是如果L不存在，那么P是N端保护基团；
vii.R独立地选自下组，该组由以下组成：任选地被一个或多个相同或不同的取代基R’取代的C1-6烷基、C6-10芳基或C7-10芳烷基；
viii.R’独立地选自下组，该组由以下组成：卤素、-OH、-OR”、-SH、-SR”、-NH2、-NHR”、-NR”2、-CO2H、-CONH2、-CONHR”、-CONR”2、-NHC(＝N)NH2；并且
ix.R”是C1-6烷基基团。
在另一个实施例中，蛋白酶抑制剂是式P-(A)y-L-(B)x-N(H)-CHR-CH(OH)-SO3M的肽醛的亚硫酸氢盐加合物，其中
i.M是氢或碱金属；
ii.(B)x的x是1、2或3，并且B独立地是经由(B)x氨基酸的C端连接到B0上的单一氨基酸
iii.L不存在或L独立地是式-C(＝O)-、-C(＝O)-C(＝O)-、-C(＝S)-、-C(＝S)-C(＝S)-或-C(＝S)-C(＝O)-的连接基团；
iv.(A)y的y是0、1或2，并且A独立地是经由(A)y氨基酸的N端连接到L上的单一氨基酸残基，其前提是如果L不存在，那么A不存在；
v.P选自下组，该组由以下组成：氢和N端保护基团，其前提是如果L不存在，那么P是N端保护基团；
vi.R独立地选自下组，该组由以下组成：任选地被一个或多个相同或不同的取代基R’取代的C1-6烷基、C6-10芳基或C7-10芳烷基；
vii.R’独立地选自下组，该组由以下组成：卤素、-OH、-OR”、-SH、-SR”、-NH2、-NHR”、-NR”2、-CO2H、-CONH2、-CONHR”、-CONR”2、-NHC(＝N)NH2；并且
viii.R”是C1-6烷基基团。
下文进一步详细描述了肽抑制剂。
用于去除和/或减少表面上的污垢的淀粉酶可以是α-淀粉酶。α-淀粉酶可包含在洗涤液中或器皿洗涤洗涤剂组合物中。
在本发明的一个实施例中，所述淀粉酶与SEQ ID NO:1、2、3或4的序列具有至少70％，例如至少75％、例如至少80％、例如至少85％、例如至少90％、例如至少95％、例如至少98％、例如至少99％、例如100％的序列同一性。
在本发明的一个实施例中，在器皿洗涤过程中将地衣多糖酶与淀粉酶和/或蛋白酶一起使用。地衣多糖酶可以是SEQ ID NO.18、SEQ ID NO.19、SEQ ID NO.20、SEQ IDNO.21、SEQ ID NO.22的地衣多糖酶或该酶的His-标记的变体。在本发明的一个实施例中，地衣多糖酶是氨基酸序列NO.23的酶。对酶进行的地衣多糖酶活性测试可以如欧洲专利申请号15198277.4的实例1所述进行确定。可以如同一专利申请的实例2中所述对地衣多糖酶进行克隆、表达和纯化。
在一个实施例中，所述淀粉酶是α-淀粉酶变体，其在与以下位置对应的一个或多个位置处包含修饰：SEQ ID NO:1的D183*+G184*+R118K+N195F+R320K+R458K或M9L+R118K+G149A+G182T+G186A+D183*+G184*+N195F+M202L+T257I+Y295F+N299Y+R320K+M323T+A339S+E345R+R458K；SEQ ID NO:2的D183*+G184*或W140Y+D183*+G184*+N195F+V206Y+Y243F+E260G+G304R+G476K；SEQ ID NO:3的H156Y+A181T+N190F+A209V+Q264S，其中所述α-淀粉酶变体分别与SEQ ID NO:1、2或3具有至少75％但小于100％的序列同一性，并且其中所述α-淀粉酶变体具有α-淀粉酶活性。
在一个实施例中，该淀粉酶是α-淀粉酶变体，其在与以下位置对应的一个或多个位置处包含修饰：SEQ ID NO:4的H1、N54、V56、K72、G109、F113、R116、T134、W140、W159、W167、Q169、Q172、L173、A174、R181、G182、D183、G184、W189、E194、N195、V206、G255、N260、F262、A265、W284、F289、S304、G305、W347、K391、Q395、W439、W469、R444、F473、G476和G477，其中所述α-淀粉酶变体与SEQ ID NO:4具有至少75％但小于100％的序列同一性并且其中所述α-淀粉酶变体具有α-淀粉酶活性。
在一个实施例中，所述一个或多个位置处的修饰选自下组，该组由以下组成：H1*、H1A、N54S、V56T、K72R、G109A、F113Q、R116Q、R116H、T134E、W140Y、W140F、W140H、W159Y、W159F、W159H、W167Y、W167H、W167F、Q169E、Q172K、Q172G、Q172N、L173P、A174*、A174S、R181*、G182*、D183*、G184*、G184T、W189Y、W189F、W189H、W189E、W189D、W189Q、W189N、E194D、E194N、E194S、N195F、V206L、V206F、V206Y、G255A、N260G、N260P、N260A、N260G、N260P、N260A、A265G、W284G、W284H、F289H、S304K、S304R、S304Q、S304E、G305K、G305R、G305Q、G305E、W347Y、W347F、W347H、K391A、Q395P、W439N、W439Q、W439T、R444Q、W469T、W469N、F473R、G476R、G476Q、G476E、G476K G477K、G477R、G477Q、以及G477E，其中这些位置对应于SEQ IDNO:4的位置。
在一个实施例中，该α-淀粉酶变体在与SEQ ID NO:4的R181+G182；R181+D183；R181+G184；G182+D183；G182+G184或D183+G184对应的位置处包含缺失。
在一个实施例中，该α-淀粉酶变体选自下组，该组由以下组成：
SEQ ID NO:4的多肽的H1*+N54S+V56T+G109A+Q169E+Q172K+A174*+G182*+D183*+N195F+V206L+K391A+G476K；
H1*+N54S+V56T+G109A+R116H+A174S+G182*+D183*+N195F+V206L+K391A+G476K；
H1*+N54S+V56T+K72R+G109A+F113Q+R116Q+W167F+Q172G+A174S+G182*+D183*+G184T+N195F+V206L+K391A+P473R+G476K；
H1*+N54S+V56T+G109A+F113Q+R116Q+Q172N+A174S+G182*+D183*+N195F+V206L+A265G+K391A+P473R+G476K；
H1*+N54S+V56T+K72R+G109A+F113Q+W167F+Q172R+A174S+G182*+D183*+N195F+V206L+K391A+G476K；
H1*+N54S+V56T+K72R+G109A+R116H+T134E+W167F+Q172G+L173V+A174S+G182*+D183*+N195F+V206L+G255A+K391A+G476K；
H1*+N54S+V56T+K72R+G109A+R116H+T134E+W167F+Q172G+L173V+A174S+G182*+D183*+N195F+V206L+G255A+K391A+Q395P+T444Q+P473R+G476K；
H1*+N54S+V56T+G109A+T134E+A174S+G182*+D183*+N195F+V206L+K391A+G476K；
H1*+N54S+V56T+K72R+G109A+A174S+G182*+D183*+N195F+V206L+G255A+K391A+G476K；
H1*+N54S+V56T+K72R+G109A+F113Q+R116Q+W167F+Q172G+A174S+G184T+N195F+V206L+K391A+P473R+G476K，以及H1*+N54S+V56T+G109A+W167F+Q172E+L173P+A174K+G182*+D183*+N195F+V206L+K391A+G476K，并且其中所述α-淀粉酶变体与SEQ ID NO:4的多肽共享至少80％，例如至少85％、例如至少90％、例如至少93％、例如至少94％、例如至少95％、例如至少96％、例如至少97％、例如至少98％但小于100％的序列同一性，并且其中所述α-淀粉酶变体具有α-淀粉酶活性。
在一个实施例中，蛋白酶选自下组，该组由以下组成：
i.与SEQ ID NO:5、6、7和8的序列具有至少70％，例如至少75％、例如至少80％、例如至少85％、例如至少90％、例如至少95％、例如至少98％、例如至少99％、例如100％的序列同一性的蛋白酶；
ii.在与SEQ ID NO:5的位置9、15、36、61、68、76、99、106、120、167、170、194、195、205、218、235、245或261对应的一个或多个位置处包含取代的蛋白酶变体，其中所述蛋白酶变体与SEQ ID NO:5具有至少75％但小于100％的序列同一性。
无论何处描述蛋白酶变体，位置是指BPN'编号(SEQ ID NO:8)。
在一个实施例中，该蛋白酶选自下组，该组由以下组成：SEQ ID NO:5的M222S、*36D+N76D+N120D+G195E+K235L、Y167A+R170S+A194P、S99SE、V68A+S106A、S9R+A15T+V68A+N218D+Q245R、S9R+A15T+G61E+V68A+A194P+V205I+Q245R+N261D和S99AD，其中所述蛋白酶变体与SEQ ID NO:5具有至少75％但小于100％的序列同一性，并且其中所述蛋白酶变体具有蛋白酶活性。在本发明的一个实施例中，该蛋白酶是SEQ ID NO:24的蛋白酶变体。
蛋白酶抑制剂
蛋白酶抑制剂可以是使蛋白酶稳定或抑制蛋白酶以使得洗衣皂条中的蛋白酶或其他一种或多种酶不降解的任何化合物。蛋白酶抑制剂的实例是抑肽酶、贝他定(bestatin)、钙蛋白酶抑制剂I和II、胰凝乳蛋白酶抑制剂、亮肽素、抑肽素、苯甲基磺酰氟(PMSF)、硼酸、硼酸盐、硼砂、硼酸、苯基硼酸(如4-甲酰基苯基硼酸(4-FPBA))、肽醛或其亚硫酸氢盐加合物或半缩醛加合物以及肽三氟甲基酮。可以存在一种或多种蛋白酶抑制剂，如5、4、3、2或1种抑制剂，其中至少一种是肽醛、其亚硫酸氢盐加合物或半缩醛加合物。
肽醛抑制剂
肽醛可以具有式P-(A)y-L-(B)x-B0-H，或其亚硫酸氢盐加合物或半缩醛加合物，其中：
i.H是氢；
ii.B0是具有式-NH-CH(R)-C(＝O)-的L-或D-构型的单一氨基酸残基；
iii.(B)x的x是1、2或3，并且B独立地是经由B氨基酸的C端连接到B0上的单一氨基酸
iv.L不存在或L独立地是式-C(＝O)-、-C(＝O)-C(＝O)-、-C(＝S)-、-C(＝S)-C(＝S)-或-C(＝S)-C(＝O)-的连接基团；
v.(A)y的y是0、1或2，并且A独立地是经由A氨基酸的N端连接到L上的单一氨基酸残基，其前提是如果L不存在，那么A不存在；
vi.P选自下组，该组由以下组成：氢和N端保护基团，其前提是如果L不存在，那么P是N端保护基团；
vii.R独立地选自下组，该组由以下组成：任选地被一个或多个相同或不同的取代基R’取代的C1-6烷基、C6-10芳基或C7-10芳烷基；
viii.R’独立地选自下组，该组由以下组成：卤素、-OH、-OR”、-SH、-SR”、-NH2、-NHR”、-NR”2、-CO2H、-CONH2、-CONHR”、-CONR”2、-NHC(＝N)NH2；并且
ix.R”是C1-6烷基基团。
x可以是1、2或3并且因此B对应地可以是1、2或3个氨基酸残基。因此，B可以表示B1、B2-B1或B3-B2-B1，其中B3、B2和B1各自表示一个氨基酸残基。y可以是0、1或2并且因此A可以不存在，或是对应地具有式A1或A2-A1的1个或2个氨基酸残基，其中A2和A1各自表示一个氨基酸残基。
B0可以是具有L或D构型的单一氨基酸残基，它经由氨基酸的C端被连接到H上，其中R是C1-6烷基、C6-10芳基或C7-10芳烷基侧链，如甲基、乙基、丙基、异丙基、丁基、异丁基、苯基或苄基，并且其中R可以任选地被一个或多个相同或不同的取代基R'取代。具体实例是D-或L-形式的精氨酸(Arg)、3,4-二羟基苯丙氨酸、异亮氨酸(Ile)、亮氨酸(Leu)、甲硫氨酸(Met)、正亮氨酸(Nle)、正缬氨酸(Nva)、苯丙氨酸(Phe)、间酪氨酸、对酪氨酸(Tyr)以及缬氨酸(Val)。具体实施例是当B0是亮氨酸、甲硫氨酸、苯丙氨酸、对酪氨酸以及缬氨酸时。
经由B1氨基酸的C端连接到B0上的B1可以是脂肪族、疏水性和/或中性氨基酸。B1的实例是丙氨酸(Ala)、半胱氨酸(Cys)、甘氨酸(GIy)、异亮氨酸(Ile)、亮氨酸(Leu)、正亮氨酸(Nle)、正缬氨酸(Nva)、脯氨酸(Pro)、丝氨酸(Ser)、苏氨酸(Thr)以及缬氨酸(VaI)。B1的具体实例是丙氨酸、甘氨酸、异亮氨酸、亮氨酸以及缬氨酸。具体实施例是当B1是丙氨酸、甘氨酸或缬氨酸时。
如果存在，经由B2氨基酸的C端连接到B1上的B2可以是脂肪族、疏水性、中性和/或极性氨基酸。B2的实例是丙氨酸(Ala)、精氨酸(Arg)、卷须霉啶(capreomycidine，Cpd)、半胱氨酸(Cys)、甘氨酸(GIy)、异亮氨酸(Ile)、亮氨酸(Leu)、正亮氨酸(Nle)、正缬氨酸(Nva)、苯丙氨酸(Phe)、脯氨酸(Pro)、丝氨酸(Ser)、苏氨酸(Thr)以及缬氨酸(VaI)。B2的具体实例是丙氨酸、精氨酸、卷须霉啶、甘氨酸、异亮氨酸、亮氨酸、苯丙氨酸以及缬氨酸。具体实施例是当B2是精氨酸、甘氨酸、亮氨酸、苯丙氨酸或缬氨酸时。
经由B3氨基酸的C端连接到B2上的B3(如果存在)可以是大型、脂肪族、芳香族、疏水性和/或中性氨基酸。B3的实例是异亮氨酸(Ile)、亮氨酸(Leu)、正亮氨酸(Nle)、正缬氨酸(Nva)、苯丙氨酸(Phe)、苯基甘氨酸、酪氨酸(Tyr)、色氨酸(Trp)以及缬氨酸(VaI)。B3的具体实例是亮氨酸、苯丙氨酸、酪氨酸以及色氨酸。
连接基团L可以不存在或选自下组，该组由以下组成：-C(＝O)-、-C(＝O)-C(＝O)-、-C(＝S)-、-C(＝S)-C(＝S)-或-C(＝S)-C(＝O)-。本发明的具体实施例是当L不存在或L是羰基基团-C(＝O)-时。
经由氨基酸的N端连接到L上的A1(如果存在)可以是脂肪族、芳香族、疏水性、中性和/或极性氨基酸。A1的实例是丙氨酸(Ala)、精氨酸(Arg)、卷须霉啶(Cpd)、甘氨酸(GIy)、异亮氨酸(Ile)、亮氨酸(Leu)、正亮氨酸(Nle)、正缬氨酸(Nva)、苯丙氨酸(Phe)、苏氨酸(Thr)、酪氨酸(Tyr)、色氨酸(Trp)以及缬氨酸(VaI)。A1的具体实例是丙氨酸、精氨酸、甘氨酸、亮氨酸、苯丙氨酸、酪氨酸、色氨酸以及缬氨酸。具体实施例是当B2是亮氨酸、苯丙氨酸、酪氨酸或色氨酸时。
经由氨基酸的N端连接到A1上的A2残基(如果存在)可以是大型、脂肪族、芳香族、疏水性和/或中性氨基酸。A2的实例是精氨酸(Arg)、异亮氨酸(Ile)、亮氨酸(Leu)、正亮氨酸(Nle)、正缬氨酸(Nva)、苯丙氨酸(Phe)、苯基甘氨酸、酪氨酸(Tyr)、色氨酸(Trp)以及缬氨酸(VaI)。A2的具体实例是苯丙氨酸和酪氨酸。
N端保护基团P(如果存在)可以选自甲酰基、乙酰基(Ac)、苄酰基(Bz)、三氟乙酰基、甲氧基丁二酰基、芳香族和脂肪族氨基甲酸乙酯保护基团，如芴基甲氧羰基(Fmoc)、甲氧羰基、(氟甲氧基)羰基、苄氧羰基(Cbz)、叔丁氧羰基(Boc)以及金刚烷氧羰基；对甲氧基苄基羰基(Moz)、苄基(Bn)、对甲氧基苄基(PMB)、对甲氧基苯基(PMP)、甲氧基乙酰基、甲基氨基羰基、甲基磺酰基、乙基磺酰基、苄基磺酰基、甲基磷酰胺基(MeOP(OH)(＝O))以及苄基磷酰胺基(PhCH2OP(OH)(＝O))。
肽醛的通式还可以写成：P-A2-A1-L-B3-B2B1-B0-H，其中P、A2、A1、L、B3、B2、B1以及B0如上文所定义。
在具有保护基团的三肽醛(即x＝2，L不存在并且A不存在)的情况下，P优选地是乙酰基、甲氧基羰基、苄氧基羰基、甲基氨基羰基、甲基磺酰基、苄基磺酰基以及苄基磷酰胺基。在具有保护基团的四肽醛(即x＝3，L不存在并且A不存在)的情况下，P优选地是乙酰基、甲氧基羰基、甲基磺酰基、乙基磺酰基以及甲基磷酰胺基。
适合的肽醛描述于WO 94/04651、WO 95/25791、WO 98/13458、WO 98/13459、WO98/13460、WO 98/13461、WO 98/13462、WO 07/141736、WO 07/145963、WO 09/118375、WO10/055052以及WO 11/036153中。
更具体地说，肽醛可以是
Cbz-Arg-Ala-Tyr-H(L-丙氨酰胺,N2-[(苯基甲氧基)羰基]-L-精氨酰基-N-[(1S)-1-甲酰基-2-(4-羟基苯基)乙基]-)，
Ac-Gly-Ala-Tyr-H(L-丙氨酰胺,N-乙酰基甘氨酰基-N-[(1S)-1-甲酰基-2-(4-羟基苯基)乙基]-)，
Cbz-Gly-Ala-Tyr-H(L-丙氨酰胺,N-[(苯基甲氧基)羰基]甘氨酰基-N-[(1S)-1-甲酰基-2-(4-羟基苯基)乙基]-)，
Cbz-Gly-Ala-Leu-H(L-丙氨酰胺,N-[(苯基甲氧基)羰基]甘氨酰基-N-[(1S)-1-甲酰基-3-甲基丁基]-)，
Cbz-Val-Ala-Leu-H(L-丙氨酰胺,N-[(苯基甲氧基)羰基]-L-缬氨酰基-N-[(1S)-1-甲酰基-3-甲基丁基]-)，
Cbz-Gly-Ala-Phe-H(L-丙氨酰胺,N-[(苯基甲氧基)羰基]甘氨酰基-N-[(1S)-1-甲酰基-2-苯乙基]-)，
Cbz-Gly-Ala-Val-H(L-丙氨酰胺,N-[(苯基甲氧基)羰基]甘氨酰基-N-[(1S)-1-甲酰基-2-甲基丙基]-)，
Cbz-Gly-Gly-Tyr-H(甘氨酰胺,N-[(苯基甲氧基)羰基]甘氨酰基-N-[(1S)-1-甲酰基-2-(4-羟基苯基)乙基]-)，
Cbz-Gly-Gly-Phe-H(甘氨酰胺,N-[(苯基甲氧基)羰基]甘氨酰基-N-[(1S)-1-甲酰基-2-苯乙基]-)，
Cbz-Arg-Val-Tyr-H(L-缬氨酰胺,N2-[(苯基甲氧基)羰基]-L-精氨酰基-N-[(1S)-1-甲酰基-2-(4-羟基苯基)乙基]-)，
Cbz-Leu-Val-Tyr-H(L-缬氨酰胺,N-[(苯基甲氧基)羰基]-L-亮氨酰基-N-[(1S)-1-甲酰基-2-(4-羟基苯基)乙基]-)
Ac-Leu-Gly-Ala-Tyr-H(L-丙氨酰胺,N-乙酰基-L-亮氨酰基甘氨酰基-N-[(1S)-1-甲酰基-2-(4-羟基苯基)乙基]-)，
Ac-Phe-Gly-Ala-Tyr-H(L-丙氨酰胺,N-乙酰基-L-苯丙氨酰基甘氨酰基-N-[(1S)-1-甲酰基-2-(4-羟基苯基)乙基]-)，
Ac-Tyr-Gly-Ala-Tyr-H(L-丙氨酰胺,N-乙酰基-L-酪氨酰基甘氨酰基-N-[(1S)-1-甲酰基-2-(4-羟基苯基)乙基]-)，
Ac-Phe-Gly-Ala-Leu-H(L-丙氨酰胺,N-乙酰基-L-苯丙氨酰基甘氨酰基-N-[(1S)-1-甲酰基-3-甲基丁基]-)，
Ac-Phe-Gly-Ala-Phe-H(L-丙氨酰胺,N-乙酰基-L-苯丙氨酰基甘氨酰基-N-[(1S)-1-甲酰基-2-苯乙基]-)，
Ac-Phe-Gly-Val-Tyr-H(L-缬氨酰胺,N-乙酰基-L-苯丙氨酰基甘氨酰基-N-[(1S)-1-甲酰基-2-(4-羟基苯基)乙基]-)，
Ac-Phe-Gly-Ala-Met-H(L-丙氨酰胺,N-乙酰基-L-苯丙氨酰基甘氨酰基-N-[(1S)-1-甲酰基-3-(甲硫基)丙基]-)，
Ac-Trp-Leu-Val-Tyr-H(L-缬氨酰胺,N-乙酰基-L-色氨酰基-L-亮氨酰基-N-[(1S)-1-甲酰基-2-(4-羟基苯基)乙基]-)，
MeO-CO-Val-Ala-Leu-H(L-丙氨酰胺,N-(甲氧羰基)-L-缬氨酰基-N-[(1S)-1-甲酰基-3-甲基丁基]-)，
MeNHCO-Val-Ala-Leu-H(L-丙氨酰胺,N-(氨基甲基羰基)-L-缬氨酰基-N-[(1S)-1-甲酰基-3-甲基丁基]-)，
MeO-CO-Phe-Gly-Ala-Leu-H(L-丙氨酰胺,N-(甲氧羰基)-L-苯丙氨酰基甘氨酰基-N-[(1S)-1-甲酰基-3-甲基丁基]-)，
MeO-CO-Phe-Gly-Ala-Phe-H(L-丙氨酰胺,N-(甲氧羰基)-L-苯丙氨酰基甘氨酰基-N-[(1S)-1-甲酰基-2-苯乙基]-)，
MeSO2-Phe-Gly-Ala-Leu-H(L-丙氨酰胺,N-(甲磺酰基)-L-苯丙氨酰基甘氨酰基-N-[(1S)-1-甲酰基-3-甲基丁基]-)，
MeSO2-Val-Ala-Leu-H(L-丙氨酰胺,N-(甲磺酰基)-L-缬氨酰基-N-[(1S)-1-甲酰基-3-甲基丁基]-)，
PhCH2O-P(OH)(O)-Val-Ala-Leu-H(L-丙氨酰胺,N-[羟基(苯基甲氧基)氧膦基]-L-缬氨酰基-N-[(1S)-1-甲酰基-3-甲基丁基]-)，
EtSO2-Phe-Gly-Ala-Leu-H(L-丙氨酰胺,N-(乙磺酰基)-L-苯丙氨酰基甘氨酰基-N-[(1S)-1-甲酰基-3-甲基丁基]-)，
PhCH2SO2-Val-Ala-Leu-H(L-丙氨酰胺,N-[(苯甲基)磺酰基]-L-缬氨酰基-N-[(1S)-1-甲酰基-3-甲基丁基]-)，
PhCH2O-P(OH)(O)-Leu-Ala-Leu-H(L-丙氨酰胺,N-[羟基(苯基甲氧基)氧膦基]-L-亮氨酰基-N-[(1S)-1-甲酰基-3-甲基丁基]-)，
PhCH2O-P(OH)(O)-Phe-Ala-Leu-H(L-丙氨酰胺,N-[羟基(苯基甲氧基)氧膦基]-L-苯并酰胺基-N-[(1S)-1-甲酰基-3-甲基丁基]-)，或
MeO-P(OH)(O)-Leu-Gly-Ala-Leu-H；(L-丙氨酰胺,N-(羟基甲氧基氧膦基)-L-亮氨酰基甘氨酰基-N-[(1S)-1-甲酰基-3-甲基丁基]-)。
优选实例是Cbz-Gly-Ala-Tyr-H。
这类肽醛的另外的实例包括
α-MAPI(3,5,8,11-四氮杂十三酸,6-[3-[(氨基亚氨基甲基)氨基]丙基]-12-甲酰基-9-(1-甲基乙基)-4,7,10-三氧代-13-苯基-2-(苯甲基)-,(2S,6S,9S,12S)-
L-缬氨酰胺,N2-[[(1-羧基-2-苯基乙基)氨基]羰基]-L-精氨酰基-N-(1-甲酰基-2-苯乙基)-,[1(S),2(S)]-；L-缬氨酰胺,N2-[[[(1S)-1-羧基-2-苯乙基]氨基]羰基]-L-精氨酰基-N-[(1S)-1-甲酰基-2-苯基乙基]-(9CI)；SP-胰凝乳蛋白酶抑制剂B)，
β-MAPI(L-缬氨酰胺,N2-[[[(1S)-1-羧基-2-苯乙基]氨基]羰基]-L-精氨酰基-N-[(1R)-1-甲酰基-2-苯乙基]-L-缬氨酰胺,N2-[[(1-羧基-2-苯乙基)氨基]羰基]-L-精氨酰基-N-(1-甲酰基-2-苯乙基)-,[1(S),2(R)]-)，
Phe-C(＝O)-Arg-Val-Tyr-H(L-缬氨酰胺,N2-[[[(1S)-1-羧基-2-苯乙基]氨基]羰基]-L-精氨酰基-N-[(1S)-1-甲酰基-2-(4-羟基苯基)乙基]-(9CI))，
Phe-C(＝O)-Gly-Gly-Tyr-H(3,5,8,11-四氮杂十三酸,12-甲酰基-13-(4-羟基苯基)-4,7,10-三氧代-2-(苯甲基),(2S,12S)-)，
Phe-C(＝O)-Gly-Ala-Phe-H(3,5,8,11-四氮杂十三酸,12-甲酰基-9-甲基-4,7,10-三氧代-13-苯基-2-(苯甲基)-,(2S,9S,12S)-)，
Phe-C(＝O)-Gly-Ala-Tyr-H(3,5,8,11-四氮杂十三酸,12-甲酰基-13-(4-羟基苯基)-9-甲基-4,7,10-三氧代-2-(苯甲基)-,(2S,9S,12S)-)，
Phe-C(＝O)-Gly-Ala-Leu-H(3,5,8,11-四氮杂十五酸,12-甲酰基-9,14-二甲基-4,7,10-三氧代-2-(苯甲基)-,(2S,9S,12S)-)，
Phe-C(＝O)-Gly-Ala-Nva-H(3,5,8,11-四氮杂十五酸,12-甲酰基-9-甲基-4,7,10-三氧代-2-(苯甲基)-,(2S,9S,12S)-)，
Phe-C(＝O)-Gly-Ala-Nle-H(3,5,8,11-四氮杂十六酸,12-甲酰基-9-甲基-4,7,10-三氧代-2-(苯甲基)-,(2S,9S,12S)-)，
Tyr-C(＝O)-Arg-Val-Tyr-H(L-缬氨酰胺,N2-[[[(1S)-1-羧基-2-(4-羟基苯基)乙基]氨基]羰基]-L-精氨酰基-N-[(1S)-1-甲酰基-2-(4-羟基苯基)乙基]-(9CI))
Tyr-C(＝O)-Gly-Ala-Tyr-H(3,5,8,11-四氮杂十三酸,12-甲酰基-13-(4-羟基苯基)-2-[(4-羟基苯基)甲基]-9-甲基-4,7,10-三氧代-,(2S,9S,12S)-)
Phe-C(＝S)-Arg-Val-Phe-H(3,5,8,11-四氮杂十三酸,6-[3-[(氨基亚氨基甲基)氨基]丙基]-12-甲酰基-9-(1-甲基乙基)-7,10-二氧代-13-苯基-2-(苯甲基)-4-硫代-,(2S,6S,9S,12S)-)，
Phe-C(＝S)-Arg-Val-Tyr-H(3,5,8,11-四氮杂十三酸,6-[3-[(氨基亚氨基甲基)氨基]丙基]-12-甲酰基-13-(4-羟基苯基)-9-(1-甲基乙基)-7,10-二氧代-2-(苯甲基)-4-硫代-,(2S,6S,9S,12S)-)，
Phe-C(＝S)-Gly-Ala-Tyr-H(3,5,8,11-四氮杂十三酸,12-甲酰基-13-(4-羟基苯基)-9-甲基-7,10-二氧代-2-(苯甲基)-4-硫代-,(2S,9S,12S)-)，
抗痛素(L-缬氨酰胺,N2-[[(1-羧基-2-苯乙基)氨基]羰基]-L-精氨酰基-N-[4-[(氨基亚氨基甲基)氨基]-1-甲酰基丁基]-)，
GE20372A(L-缬氨酰胺,N2-[[[(1S)-1-羧基-2-(4-羟基苯基)乙基]氨基]羰基]-L-精氨酰基-N-[(1S)-1-甲酰基-2-苯乙基]-
L-缬氨酰胺,N2-[[[1-羧基-2-(4-羟基苯基)乙基]氨基]羰基]-L-精氨酰基-N-(1-甲酰基-2-苯乙基)-,[1(S),2(S)]-)，
GE20372B(L-缬氨酰胺,N2-[[[(1S)-1-羧基-2-(4-羟基苯基)乙基]氨基]羰基]-L-精氨酰基-N-[(1R)-1-甲酰基-2-苯乙基]-
L-缬氨酰胺,N2-[[[1-羧基-2-(4-羟基苯基)乙基]氨基]羰基]-L-精氨酰基-N-(1-甲酰基-2-苯乙基)-,[1(S),2(R)]-)，
胰凝乳蛋白酶抑制剂A(L-亮氨酰胺,(2S)-2-[(4S)-2-氨基-3,4,5,6-四氢-4-嘧啶基]-N-[[[(1S)-1-羧基-2-苯乙基]氨基]羰基]甘氨酰基-N-(1-甲酰基-2-苯乙基)-
L-亮氨酰胺,(2S)-2-[(4S)-2-氨基-1,4,5,6-四氢-4-嘧啶基]-N-[[[(1S)-1-羧基-2-苯乙基]氨基]羰基]甘氨酰基-N-(1-甲酰基-2-苯乙基)-(9CI)；L-亮氨酰胺,L-2-(2-氨基-1,4,5,6-四氢-4-嘧啶基)-N-[[(1-羧基-2-苯乙基)氨基]羰基]甘氨酰基-N-(1-甲酰基-2-苯乙基)-，立体异构体)，
胰凝乳蛋白酶抑制剂B(L-缬氨酰胺,(2S)-2-[(4S)-2-氨基-3,4,5,6-四氢-4-嘧啶基]-N-[[[(1S)-1-羧基-2-苯乙基]氨基]羰基]甘氨酰基-N-(1-甲酰基-2-苯乙基)-
L-缬氨酰胺,(2S)-2-[(4S)-2-氨基-1,4,5,6-四氢-4-嘧啶基]-N-[[[(1S)-1-羧基-2-苯乙基]氨基]羰基]甘氨酰基-N-(1-甲酰基-2-苯乙基)-(9CI)；L-缬氨酰胺,L-2-(2-氨基-1,4,5,6-四氢-4-嘧啶基)-N-[[(1-羧基-2-苯乙基)氨基]羰基]甘氨酰基-N-(1-甲酰基-2-苯乙基)-，立体异构体)，以及
胰凝乳蛋白酶抑制剂C(L-异亮氨酰胺,(2S)-2-[(4S)-2-氨基-3,4,5,6-四氢-4-嘧啶基]-N-[[[(1S)-1-羧基-2-苯乙基]氨基]羰基]甘氨酰基-N-(1-甲酰基-2-苯乙基)-
L-异亮氨酰胺,(2S)-2-[(4S)-2-氨基-1,4,5,6-四氢-4-嘧啶基]-N-[[[(1S)-1-羧基-2-苯乙基]氨基]羰基]甘氨酰基-N-(1-甲酰基-2-苯乙基)-(9CI)；L-异亮氨酰胺,L-2-(2-氨基-1,4,5,6-四氢-4-嘧啶基)-N-[[(1-羧基-2-苯乙基)氨基]羰基]甘氨酰基-N-(1-甲酰基-2-苯乙基)-，立体异构体)。
肽醛加合物
代替肽醛，蛋白酶抑制剂可以是肽醛的加合物。该加合物可以是具有式P-(A)y-L-(B)x-N(H)-CHR-CH(OH)-SO3M的亚硫酸氢盐加合物，其中P、A、y、L、B、x以及R如上文所定义，并且M是H或碱金属、优选地Na或K。可替代地，该加合物可以是具有式P-(A)y-L-(B)x-N(H)-CHR-CH(OH)-OR的半缩醛，其中P、A、y、L、B、x以及R如上文所定义。优选实施例是亚硫酸氢盐加合物，其中P＝Cbz，B2＝Gly；B1＝Ala；B0＝Tyr(因此R＝PhCH2，R’＝OH)，x＝2，y＝0，L＝A＝不存在并且M＝Na(Cbz-Gly-Ala-N(H)-CH(CH2-p-C6H4OH)-CH(OH)-SO3Na，L-丙氨酰胺,N-[(苯基甲氧基)羰基]甘氨酰基-N-[2-羟基-1-[(4-羟基苯基)甲基]-2-磺乙基]-,钠盐(1:1))。
肽醛的亚硫酸氢盐加合物的通式还可以写成P-A2-A1-L-B3-B2-B1-N(H)-CHR-CH(OH)-SO3M，其中P、A2、A1、L、B3、B2、B1、R和M如上文所定义。
可替代地，肽醛的加合物可以是Cbz-Gly-Ala-N(H)-CH(CH2-p-C6H4OH)-CH(OH)-SO3Na((2S)-[(N-{N-[((苄氧基))羰基]甘氨酰基}-L-丙氨酰基)氨基]-1-羟基-3-(4-羟基苯基)丙烷-1-磺酸钠)或Cbz-Gly-Ala-N(H)-CH(CH2Ph)-CH(OH)-SO3Na((2S)-[(N-{N-[((苄氧基))羰基]甘氨酰基}-L-丙氨酰基)氨基]-1-羟基-3-(苯基)丙烷-1-磺酸钠)或“MeO-CO_Val-Ala-N(H)-CH(CH2CH(CH3)2)-CH(OH)-SO3Na((2S)-[(N-{N-[((苄氧基))羰基]甘氨酰基}-L-丙氨酰基)氨基]-1-羟基-3-(2-丙基)丙烷-1-磺酸钠)。
其他优选的肽醛亚硫酸氢盐是
Cbz-Arg-Ala-NHCH(CH2C6H4OH)C(OH)(SO3M)-H，其中M＝Na，
Ac-Gly-Ala-NHCH(CH2C6H4OH)C(OH)(SO3M)-H，其中M＝Na，
Cbz-Gly-Ala-NHCH(CH2C6H4OH)C(OH)(SO3M)-H，其中M＝Na(L-丙氨酰胺,N-[(苯基甲氧基)羰基]甘氨酰基-N-[2-羟基-1-[(4-羟基苯基)甲基]-2-磺乙基]-,钠盐(1:1))，
Cbz-Gly-Ala-NHCH(CH2CH(CH3)2))C(OH)(SO3M)-H，其中M＝Na，
Cbz-Val-Ala-NHCH(CH2CH(CH3)2))C(OH)(SO3M)-H，其中M＝Na，
Cbz-Gly-Ala-NHCH(CH2Ph)C(OH)(SO3M)-H，其中M＝Na，
Cbz-Gly-Ala-NHCH(CH(CH3)2)C(OH)(SO3M)-H，其中M＝Na，
Cbz-Gly-Gly-NHCH(CH2C6H4OH)C(OH)(SO3M)-H，其中M＝Na，
Cbz-Gly-Gly-NHCH(CH2Ph)C(OH)(SO3M)-H，其中M＝Na，
Cbz-Arg-Val-NHCH(CH2C6H4OH)C(OH)(SO3M)-H，其中M＝Na，
Cbz-Leu-Val-NHCH(CH2C6H4OH)C(OH)(SO3M)-H，其中M＝Na，
Ac-Leu-Gly-Ala-NHCH(CH2C6H4OH)C(OH)(SO3M)-H，其中M＝Na，
Ac-Phe-Gly-Ala-NHCH(CH2C6H4OH)C(OH)(SO3M)-H，其中M＝Na，
Ac-Tyr-Gly-Ala-NHCH(CH2C6H4OH)C(OH)(SO3M)-H，其中M＝Na，
Ac-Phe-Gly-Ala-NHCH(CH2CH(CH3)2))C(OH)(SO3M)-H，其中M＝Na，
Ac-Phe-Gly-Ala-NHCH(CH2Ph)C(OH)(SO3M)-H，其中M＝Na，
Ac-Phe-Gly-Val-NHCH(CH2C6H4OH)C(OH)(SO3M)-H，其中M＝Na，
Ac-Phe-Gly-Ala-NHCH(CH2CH2SCH3)(SO3M)-H，其中M＝Na，
Ac-Trp-Leu-Val-NHCH(CH2C6H4OH)C(OH)(SO3M)-H，其中M＝Na，
MeO-CO-Val-Ala-NHCH(CH2CH(CH3)2))C(OH)(SO3M)-H，其中M＝Na，
MeNCO-Val-Ala-NHCH(CH2CH(CH3)2))C(OH)(SO3M)-H，其中M＝Na，
MeO-CO-Phe-Gly-Ala-NHCH(CH2CH(CH3)2))C(OH)(SO3M)-H，其中M＝Na，
MeO-CO-Phe-Gly-Ala-NHCH(CH2Ph)C(OH)(SO3M)-H，其中M＝Na，
MeSO2-Phe-Gly-Ala-NHCH(CH2CH(CH3)2))C(OH)(SO3M)-H，其中M＝Na，
MeSO2-Val-Ala-NHCH(CH2CH(CH3)2))C(OH)(SO3M)-H，其中M＝Na，
PhCH2O(OH)(O)P-Val-Ala-NHCH(CH2CH(CH3)2))C(OH)(SO3M)-H，其中M＝Na，
EtSO2-Phe-Gly-Ala-NHCH(CH2CH(CH3)2))C(OH)(SO3M)-H，其中M＝Na，
PhCH2SO2-Val-Ala-NHCH(CH2CH(CH3)2))C(OH)(SO3M)-H，其中M＝Na，
PhCH2O(OH)(O)P-Leu-Ala-NHCH(CH2CH(CH3)2))C(OH)(SO3M)-H，其中M＝Na，
PhCH2O(OH)(O)P-Phe-Ala-NHCH(CH2CH(CH3)2))C(OH)(SO3M)-H，其中M＝Na，
MeO(OH)(O)P-Leu-Gly-Ala-NHCH(CH2CH(CH3)2))C(OH)(SO3M)-H，其中M＝Na，
Phe-脲-Arg-Val-NHCH(CH2C6H4OH)C(OH)(SO3M)-H，其中M＝Na。
盐
该条中所用的盐是一价阳离子与有机阴离子的盐。该一价阳离子可以是例如Na+、K+或NH4 +。该有机阴离子可以是例如甲酸根、乙酸根、柠檬酸根或乳酸根。由此，一价阳离子与有机阴离子的盐可以是例如甲酸钠、甲酸钾、甲酸铵、乙酸钠、乙酸钾、乙酸铵、乳酸钠、乳酸钾、乳酸铵、单柠檬酸钠、二柠檬酸钠、三柠檬酸钠、柠檬酸钠钾、柠檬酸钾、柠檬酸铵等。具体实施例是甲酸钠。
本发明的酶
在本发明的一个实施例中，可以将本发明的多肽以对应于以下的量添加至器皿洗涤洗涤剂组合物中：每升的洗涤液0.001mg-200mg的蛋白，例如0.005mg-100mg的蛋白，优选0.01mg-50mg的蛋白，更优选0.05mg-20mg的蛋白，甚至更优选0.1mg-10mg的蛋白。
可以使用常规稳定剂使本发明的器皿洗涤洗涤剂组合物中的一种或多种酶稳定化，这些稳定剂例如为多元醇(如丙二醇或甘油)、糖或糖醇、乳酸、硼酸、或硼酸衍生物(例如，芳族硼酸酯)、或苯基硼酸衍生物(如4-甲酰苯基硼酸)，并且该组合物可以如上所述进行配制。在优选的实施例中，使用蛋白酶抑制剂稳定一种或多种酶。
表面活性剂
该洗涤剂组合物包含一种或多种表面活性剂，其中至少一种表面活性剂是阴离子的。其他表面活性剂可以是阴离子的和/或非离子的和/或半极性的和/或两性离子的、或其混合物。在一个具体实施例中，洗涤剂组合物包含一种或多种非离子型表面活性剂和一种或多种阴离子表面活性剂的混合物。这种或这些表面活性剂典型地以按重量计从约0.0％至10％的水平存在，如约0.1％至约5％、或约0％至约3％、或约0％至约2％。基于所希望的清洁应用来选择该一种或多种表面活性剂，并且该一种或多种表面活性剂可以包括本领域中已知的任何常规表面活性剂。
当包括在其中时，该洗涤剂通常将包含按重量计从约1％至约40％的阴离子表面活性剂，如从约5％至约30％，包括从约5％至约15％，或从约15％至约20％，或从约20％至约25％的阴离子表面活性剂。阴离子表面活性剂的非限制性实例包括硫酸盐和磺酸盐，具体地，直链烷基苯磺酸盐(LAS)、LAS的异构体、支链烷基苯磺酸盐(BABS)、苯基链烷磺酸盐、α-烯烃磺酸盐(AOS)、烯烃磺酸盐、链烯烃磺酸盐、链烷-2,3-二基双(硫酸盐)、羟基链烷磺酸盐以及二磺酸盐、烷基硫酸盐(AS)(如十二烷基硫酸钠(SDS))、脂肪醇硫酸盐(FAS)、伯醇硫酸盐(PAS)、醇醚硫酸盐(AES或AEOS或FES，也被称为醇乙氧基硫酸盐或脂肪醇醚硫酸盐)、仲链烷磺酸盐(SAS)、石蜡磺酸盐(PS)、酯磺酸盐、磺化的脂肪酸甘油酯、α-磺基脂肪酸甲酯(α-SFMe或SES)(包括甲酯磺酸盐(MES))、烷基琥珀酸或烯基琥珀酸、十二烯基/十四烯基琥珀酸(DTSA)、氨基酸的脂肪酸衍生物、磺基琥珀酸的二酯和单酯或脂肪酸盐(皂)、及其组合。
当包括在其中时，该洗涤剂通常将含有按重量计从约0.2％至约40％的非离子表面活性剂，例如从约0.5％至约30％，特别是从约1％至约20％、从约3％至约10％，如从约3％至约5％、从约8％至约12％或从约10％至约12％。非离子表面活性剂的非限制性实例包括醇乙氧基化物(AE或AEO)、醇丙氧基化物、丙氧基化的脂肪醇(PFA)、烷氧基化的脂肪酸烷基酯(例如乙氧基化的和/或丙氧基化的脂肪酸烷基酯)、烷基酚乙氧基化物(APE)、壬基酚乙氧基化物(NPE)、烷基多糖苷(APG)、烷氧基化胺、脂肪酸单乙醇酰胺(FAM)、脂肪酸二乙醇酰胺(FADA)、乙氧基化的脂肪酸单乙醇酰胺(EFAM)、丙氧基化的脂肪酸单乙醇酰胺(PFAM)、多羟基烷基脂肪酸酰胺、或葡糖胺的N-酰基N-烷基衍生物(葡糖酰胺(GA)、或脂肪酸葡糖酰胺(FAGA))、以及可以商品名SPAN和TWEEN获得的产品、及其组合。
当包括在其中时，洗涤剂通常将含有按重量计从约0％至约40％的半极性表面活性剂。半极化表面活性剂的非限制性实例包括胺氧化物(AO)，如烷基二甲胺氧化物、N-(椰油基烷基)-N,N-二甲胺氧化物和N-(牛油-烷基)-N,N-双(2-羟乙基)胺氧化物，及其组合。
当包括在其中时，洗涤剂通常将含有按重量计从约0％至约40％的两性离子表面活性剂。两性离子表面活性剂的非限制性实例包括甜菜碱，如烷基二甲基甜菜碱、磺基甜菜碱、及其组合。
助洗剂和共助洗剂
该洗涤剂组合物可以包含按重量计约0％-65％(如约5％至约50％)的洗涤剂助洗剂或共助洗剂、或其混合物。助洗剂和/或共助洗剂可以具体是形成具有Ca和Mg的水溶性络合物的螫合剂。可以使用本领域中已知用于在洗涤剂中使用的任何助洗剂和/或共助洗剂。助洗剂的非限制性实例包括沸石、二磷酸盐(焦磷酸盐)、三磷酸盐例如三磷酸钠(STP或STPP)、碳酸盐例如碳酸钠、可溶性硅酸盐例如偏硅酸钠、层状硅酸盐(例如，来自赫斯特公司(Hoechst)的SKS-6)、乙醇胺例如2-氨基乙-1-醇(MEA)、二乙醇胺(DEA，也称为2,2’-亚氨基二乙-1-醇)、三乙醇胺(TEA，也称为2,2’,2”-次氮基三乙-1-醇)、以及(羧甲基)菊粉(CMI)、及其组合。
该洗涤剂组合物还可以包含按重量计0％-50％，如约5％至约30％的洗涤剂共助洗剂。洗涤剂组合物可以包含单独或与助洗剂组合的共助洗剂，例如沸石助洗剂。共助洗剂的非限制性实例包括聚丙烯酸酯均聚物或其共聚物，如聚(丙烯酸)(PAA)或共聚(丙烯酸/马来酸)(PAA/PMA)。另外的非限制性实例包括柠檬酸盐；螯合剂，例如氨基羧酸盐、氨基多羧酸盐和膦酸盐；以及烷基琥珀酸或烯基琥珀酸。另外的具体实例包括2,2’,2”-次氨基三乙酸(NTA)、乙二胺四乙酸(EDTA)、二亚乙基三胺五乙酸(DTPA)、亚氨基二琥珀酸(IDS)、乙二胺-N,N’-二琥珀酸(EDDS)、甲基甘氨酸二乙酸(MGDA)、谷氨酸-N,N-二乙酸(GLDA)、1-羟基乙烷-1,1-二膦酸(HEDP)、乙二胺四(亚甲基膦酸)(EDTMPA)、二亚乙基三胺五(亚甲基膦酸)(DTMPA或DTPMPA)、N-(2-羟乙基)亚氨基二乙酸(EDG)、天冬氨酸-N-单乙酸(ASMA)、天冬氨酸-N,N-二乙酸(ASDA)、天冬氨酸-N-单丙酸(ASMP)、亚氨基二琥珀酸(iminodisuccinicacid)(IDA)、N-(2-磺甲基)-天冬氨酸(SMAS)、N-(2-磺乙基)-天冬氨酸(SEAS)、N-(2-磺甲基)-谷氨酸(SMGL)、N-(2-磺乙基)-谷氨酸(SEGL)、N-甲基亚氨基二乙酸(MIDA)、α-丙氨酸-N,N-二乙酸(α-ALDA)、丝氨酸-N,N-二乙酸(SEDA)、异丝氨酸-N,N-二乙酸(ISDA)、苯丙氨酸-N,N-二乙酸(PHDA)、邻氨基苯甲酸-N,N-二乙酸(ANDA)、磺胺酸-N,N-二乙酸(SLDA)、牛磺酸-N,N-二乙酸(TUDA)以及磺甲基-N,N-二乙酸(SMDA)、N-(2-羟乙基)-亚乙基二胺-N,N’,N”-三乙酸盐(HEDTA)、二乙醇甘氨酸(DEG)、二亚乙基三胺五(亚甲基膦酸)(DTPMP)、氨基三(亚甲基膦酸)(ATMP)、及其组合和盐。另外的示例性助洗剂和/或共助洗剂描述于例如WO 09/102854、US 5977053中
沸石
优选的一类沸石被表征为“中间体”硅酸盐/铝酸盐沸石。这些中间体沸石特征为小于约10的SiOx/AlOz摩尔比。优选地，Si02/A102的摩尔比范围从约2至约10。这些中间体沸石可以具有优于“高”沸石的优点。这些中间体沸石对胺类型气味具有更高亲和力，它们对于气味吸收更有效，因为它们具有更大的表面积，并且它们比高沸石更耐水分并且在水中保持更多的它们的气味吸收能力。适用于本文使用的多种多样的中间体沸石是可商购的，如 CP301-68、300-63、 CP300-35、以及 CP300-56，可从PQ公司获得，以及可从Conteka公司获得的沸石的系列。
以商品名和销售的，可从联合碳化物公司(Union CarbideCorporation)和UOP获得的沸石材料也是优选的。此类材料相比于用于控制含硫气味(例如硫醇(thiol)、硫醇(mercaptan))的中间体沸石是优选的。
当沸石用作有待喷洒至表面上的组合物中的气味控制剂时，该沸石材料优选地具有小于约10微米的粒度，并且以按该组合物重量计小于约1％的水平存在于组合物中。
漂白体系
洗涤剂可以含有按重量计0％-30％，例如约1％至约20％的漂白体系。可以使用本领域中已知用于洗涤剂中的任何漂白体系。合适的漂白体系组分包括漂白催化剂、光漂白剂、漂白活化剂、过氧化氢源如过碳酸钠、过硼酸钠和过氧化氢―脲(1:1)、预成型过酸及其混合物。合适的预成型过酸包括但不限于过氧羧酸及盐、二过氧二羧酸、过亚氨酸(perimidic acid)及盐、过氧单硫酸及盐(例如过硫酸氢钾(Oxone(R))及其混合物。漂白系统的非限制性实例包括与过酸形成漂白活化剂组合的基于过氧化物的漂白体系，其可以包含例如无机盐，包括碱金属盐例如过硼酸盐的钠盐(通常为单水合物或四水合物)、过碳酸盐、过硫酸盐、过磷酸盐、过硅酸盐。术语漂白活化剂在本文意指与过氧化氢反应以经由过水解形成过酸的化合物。以此方式形成的过酸构成活化的漂白剂。本文有待使用的适合的漂白活化剂包括属于酯、酰胺、酰亚胺或酸酐类别的那些。适合的实例是四乙酰乙二胺(TAED)、4-[(3,5,5-三甲基己酰基)氧基]苯-1-磺酸钠(ISONOBS)、4-(十二酰基氧基)苯-1-磺酸盐(LOBS)、4-(癸酰基氧基)苯-1-磺酸盐、4-(癸酰基氧基)苯甲酸盐(DOBS或DOBA)、4-(壬酰氧基)苯-1-磺酸盐(NOBS)和/或披露于WO98/17767中的那些。感兴趣的漂白活化剂的具体家族披露于EP 624154中并且该家族中特别优选的是乙酰柠檬酸三乙酯(ATC)。ATC或短链甘油三酸酯(像三醋汀)具有以下优点，它是环境友好的。此外，乙酰柠檬酸三乙酯和三醋汀在储存时在产品中具有良好的水解稳定性，并且是有效的漂白活化剂。最后，ATC是多功能的，因为在过水解反应中释放的柠檬酸盐可以作为助洗剂起作用。可替代地，漂白系统可以包括例如酰胺、酰亚胺、或砜型的过氧酸。漂白体系还可以包含过酸，如6-(苯二甲酰亚氨基)过氧己酸(PAP)。漂白系统还可以包括漂白催化剂。在一些实施例中，漂白组分可以是选自下组的有机催化剂，该组由以下各项组成：具有下式的有机催化剂：
(iii)及其混合物；
其中每个R1独立地是含有从9至24个碳的支链烷基基团或含有从11至24个碳的直链烷基基团，优选地每个R1独立地是含有从9至18个碳的支链烷基基团或含有从11至18个碳的直链烷基基团，更优选地每个R1独立地选自下组，该组由以下组成：2-丙基庚基、2-丁基辛基、2-戊基壬基、2-己基癸基、十二烷基、十四烷基、十六烷基、十八烷基、异壬基、异癸基、异十三烷基以及异十五烷基。其他示例性漂白体系描述于例如WO 2007/087258、WO2007/087244、WO 2007/087259、EP 1867708(维生素K)以及WO 2007/087242中。适合的光漂白剂可以例如是磺化的酞菁锌或酞菁铝。
优选地，除了漂白催化剂、特别是有机漂白催化剂以外，漂白组分还包含过酸源。过酸源可以选自(a)预形成的过酸；(b)过碳酸盐、过硼酸盐或过硫酸盐(过氧化氢源)，优选与漂白活化剂组合；和(c)过水解酶以及酯，用于在处理步骤中在水的存在下原位形成过酸。
聚合物
该洗涤剂可以含有按重量计0％-10％(例如0.5％-5％、2％-5％、0.5％-2％或0.2％-1％)的聚合物。可以利用本领域中已知的用于在洗涤剂中使用的任何聚合物。该聚合物可以作为如上文提到的共助洗剂起作用，或可以提供抗再沉积、纤维保护、污垢释放、染料转移抑制、油污清洁和/或抑泡特性。一些聚合物可以具有多于一种的以上提到的特性和/或多于一种的以下提到的基序(motif)。示例性聚合物包括(羧甲基)纤维素(CMC)、聚(乙烯醇)(PVA)、聚(乙烯吡咯烷酮)(PVP)、聚(乙二醇)或聚(环氧乙烷)(PEG)、乙氧基化的聚(亚乙基亚胺)、羧甲基菊粉(CMI)、和聚羧酸酯(如PAA、PAA/PMA、聚-天冬氨酸、和甲基丙烯酸月桂酯/丙烯酸共聚物)、疏水修饰的CMC(HM-CMC)和硅酮、对苯二甲酸和低聚乙二醇的共聚物、聚(对苯二甲酸乙二酯)和聚(氧乙烯对苯二甲酸酯)的共聚物(PET-POET)、PVP、聚(乙烯基咪唑)(PVI)、聚(乙烯吡啶-N-氧化物)(PVPO或PVPNO)以及聚乙烯吡咯烷酮-乙烯基咪唑(PVPVI)。另外的示例性聚合物包括磺化的聚羧酸酯、聚环氧乙烷和聚环氧丙烷(PEO-PPO)以及乙氧基硫酸二季铵盐。其他示例性聚合物披露于例如WO 2006/130575中。也考虑了以上提到的聚合物的盐。
调色剂
本发明的洗涤剂组合物还可以包括调色剂，例如染料或颜料，当配制在洗涤剂组合物中时，当所述表面与洗涤液接触时调色剂可以沉积到表面上，该洗涤液包含所述洗涤剂组合物，并且因此通过可见光的吸收/反射改变所述表面的色彩。荧光增白剂发射至少一些可见光。相比之下，因为它们吸收至少一部分可见光光谱，所以调色剂改变表面的色彩。适合的调色剂包括染料和染料-粘土结合物，并且还可以包括颜料。适合的染料包括小分子染料和聚合物染料。适合的小分子染料包括选自下组的小分子染料，该组由落入颜色索引(Colour Index)(C.I.)分类的以下染料组成：直接蓝、直接红、直接紫、酸性蓝、酸性红、酸性紫、碱性蓝、碱性紫和碱性红、或其混合物，例如于WO 2005/03274、WO 2005/03275、WO2005/03276和EP 1876226中所描述的(将其通过引用而特此结合)。洗涤剂组合物优选地包含从约0.00003wt％至约0.2wt％、从约0.00008wt％至约0.05wt％、或甚至从约0.0001wt％至约0.04wt％的调色剂。该组合物可以包含从0.0001wt％至0.2wt％的调色剂，当该组合物处于单位剂量袋的形式时，这可以是尤其优选的。合适的调色剂还披露于例如WO 2007/087257和WO 2007/087243中。
酶
器皿洗涤洗涤剂组合物和/或洗涤液可以包含一种或多种另外的酶如另外的蛋白酶、脂肪酶、角质酶、另外的淀粉酶、糖酶、纤维素酶、果胶酶、甘露聚糖酶、阿拉伯糖酶、半乳聚糖酶、木聚糖酶、氧化酶例如漆酶、和/或过氧化物酶。
一般而言，所选的一种或多种酶的特性应与所选的洗涤剂兼容(即，最适pH、与其他酶和非酶成分的兼容性等)，并且该一种或多种酶应以有效量存在。
纤维素酶
适合的纤维素酶包括细菌来源或真菌来源的那些。包括化学修饰的突变体或蛋白质工程化的突变体。适合的纤维素酶包括来自芽孢杆菌属、假单胞菌属、腐质霉属、镰孢属、梭孢壳属、支顶孢属的纤维素酶，例如披露于US 4,435,307、US 5,648,263、US 5,691,178、US 5,776,757以及WO 89/09259中的由特异腐质霉、嗜热毁丝霉和尖孢镰孢产生的真菌纤维素酶。
特别适合的纤维素酶是具有颜色护理益处的碱性或中性纤维素酶。此类纤维素酶的实例是在EP 0 495 257、EP 0 531 372、WO 96/11262、WO 96/29397、WO 98/08940中描述的纤维素酶。其他实例是例如描述于WO 94/07998、EP 0 531 315、US 5,457,046、US 5,686,593、US 5,763,254、WO 95/24471、WO 98/12307以及WO 99/001544中的那些纤维素酶变体。
其他纤维素酶是具有以下序列的内切-β-1,4-葡聚糖酶，该序列与WO 2002/099091的SEQ ID NO:2的位置1至位置773的氨基酸序列具有至少97％同一性，或家族44木葡聚糖酶，该木葡聚糖酶具有以下序列，该序列与WO 2001/062903的SEQ ID NO:2的位置40-559具有至少60％同一性。
可商购的纤维素酶包括CelluzymeTM和CarezymeTM(诺维信公司(Novozymes A/S))、Carezyme PremiumTM(诺维信公司)、CellucleanTM(诺维信公司)、CellucleanClassicTM(诺维信公司)、CellusoftTM(诺维信公司)、WhitezymeTM(诺维信公司)、ClazinaseTM和Puradax HATM(杰能科国际公司(Genencor International Inc.))以及KAC-500(B)TM(花王株式会社(Kao Corporation))。
甘露聚糖酶
适合的甘露聚糖酶包括细菌或真菌来源的那些。包括化学或基因修饰的突变体。该甘露聚糖酶可以是家族5或26的碱性甘露聚糖酶。它可以是一种来自芽孢杆菌属或腐质霉属的野生型，特别是粘琼脂芽孢杆菌、地衣芽孢杆菌、嗜碱芽孢杆菌、克劳氏芽孢杆菌或特异腐质霉。适合的甘露聚糖酶描述在WO 1999/064619中。可商购的甘露聚糖酶是Mannaway(诺维信公司)。
纤维素酶
适合的纤维素酶包括细菌或真菌来源的完整纤维素酶或单组分内切葡聚糖酶。包括化学或基因修饰的突变体。该纤维素酶可以，例如，是通常就称为内切葡聚糖酶的单-组分的内切-1,4-β-葡聚糖酶的单-组分或混合物。适合的纤维素酶包括真菌纤维素酶，该真菌纤维素酶来自特异腐质霉(US 4,435,307)或来自木霉属，例如里氏木霉或绿色木霉。纤维素酶的实例在EP 0 495 257进行了描述。其他适合的纤维素酶来自梭孢壳菌属，例如如在WO 96/29397中描述的土生梭孢壳霉或如在WO 91/17244中描述的尖孢镰孢，或者来自如在WO 02/099091和JP 2000210081中所描述的芽孢杆菌属。其他实例是纤维素酶变体，例如描述于WO 94/07998、EP 0 531 315、US 5,457,046、US 5,686,593、US 5,763,254、WO 95/24471、WO 98/12307中的那些可商购的纤维素酶包括 和(诺维信公司)、Puradax HA、和Puradax EG(可从杰能科公司(Genencor)获得)。
蛋白酶
适合的蛋白酶包括细菌、真菌、植物、病毒或动物来源的那些，例如植物或微生物来源。优选微生物来源。包括化学修饰的突变体或蛋白质工程化的突变体。它可以是碱性蛋白酶，例如丝氨酸蛋白酶或金属蛋白酶。丝氨酸蛋白酶可以例如是S1家族(如胰蛋白酶)或S8家族(如枯草杆菌蛋白酶)。金属蛋白酶可以例如是来自例如M4家族的嗜热菌蛋白酶或其他金属蛋白酶，如来自M5、M7或M8家族的那些。
术语“枯草杆菌酶”是指根据Siezen等人，Protein Engng.[蛋白质工程]4(1991)719-737和Siezen等人，Protein Science[蛋白质科学]6(1997)501-523的丝氨酸蛋白酶亚组。丝氨酸蛋白酶是通过在活性位点具有与底物形成共价加合物的丝氨酸来表征的蛋白酶的亚组。枯草杆菌酶可以被划分为6个亚类，即，枯草杆菌蛋白酶家族、嗜热蛋白酶家族、蛋白酶K家族、羊毛硫氨酸抗生素肽酶家族、Kexin家族和Pyrolysin家族。
枯草杆菌酶的实例是来源于芽孢杆菌属的那些，例如描述于US 7262042和WO 09/021867中的迟缓芽孢杆菌、嗜碱芽孢杆菌、枯草芽孢杆菌、解淀粉芽孢杆菌、短小芽孢杆菌和吉氏芽孢杆菌；和描述于WO 89/06279中的枯草杆菌蛋白酶lentus、枯草杆菌蛋白酶Novo、枯草杆菌蛋白酶Carlsberg、地衣芽孢杆菌、枯草杆菌蛋白酶BPN’、枯草杆菌蛋白酶309、枯草杆菌蛋白酶147和枯草杆菌蛋白酶168以及描述于(WO 93/18140)中的蛋白酶PD138。其他有用的蛋白酶可以是描述于WO 92/175177、WO 01/016285、WO 02/026024以及WO 02/016547中的那些。胰蛋白酶样蛋白酶的实例是胰蛋白酶(例如猪或牛来源的)和镰孢属蛋白酶(描述于WO89/06270、WO94/25583和WO 05/040372中)，以及来源于纤维单胞菌(Cellumonas)的胰凝乳蛋白酶(描述于WO05/052161和WO05/052146中)。
另外优选的蛋白酶是来自迟缓芽孢杆菌DSM 5483的碱性蛋白酶(如描述于例如WO95/23221中)、及其变体(描述于WO 92/21760、WO 95/23221、EP 1921147以及EP 1921148中)。
金属蛋白酶的实例是如描述于WO 07/044993(杰能科国际公司(Genencor Int.))中的中性金属蛋白酶，例如来源于解淀粉芽孢杆菌的那些。
有用的蛋白酶的实例是描述于以下中的变体：WO 92/19729、WO 96/034946、WO98/20115、WO 98/20116、WO 99/011768、WO 01/44452、WO 03/006602、WO 04/03186、WO 04/041979、WO 07/006305、WO 11/036263、WO 11/036264，尤其是在以下位置中的一个或多个处具有取代的变体：3、4、9、15、24、27、42、55、59、60、66、74、85、96、97、98、99、100、101、102、104、116、118、121、126、127、128、154、156、157、158、161、164、176、179、182、185、188、189、193、198、199、200、203、206、211、212、216、218、226、229、230、239、246、255、256、268和269，其中所述位置对应于WO 2016/001449的SEQ ID NO 1中示出的迟缓芽孢杆菌蛋白酶的位置。更优选地，枯草杆菌酶变体可以包含以下突变：S3T、V4I、S9R、S9E、A15T、S24G、S24R、K27R、N42R、S55P、G59E、G59D、N60D、N60E、V66A、N74D、N85S、N85R、、G96S、G96A、S97G、S97D、S97A、S97SD、S99E、S99D、S99G、S99M、S99N、S99R、S99H、S101A、V102I、V102Y、V102N、S104A、G116V、G116R、H118D、H118N、N120S、S126L、P127Q、S128A、S154D、A156E、G157D、G157P、S158E、Y161A、R164S、Q176E、N179E、S182E、Q185N、A188P、G189E、V193M、N198D、V199I、Y203W、S206G、L211Q、L211D、N212D、N212S、M216S、A226V、K229L、Q230H、Q239R、N246K、N255W、N255D、N255E、L256E、L256D、T268A、R269H。这些蛋白酶变体优选地是在WO 2016/001449的SEQ ID NO 1中所示的迟缓芽孢杆菌蛋白酶的变体、或在WO 2016/001449的SEQ ID NO 2中所示的解淀粉芽孢杆菌蛋白酶(BPN’)的变体。这些蛋白酶变体与WO 2016/001449的SEQ ID NO 1或SEQ ID NO2优选地具有至少80％序列同一性。
在以下一个或多个位置处包括取代的蛋白酶变体，该位置对应于WO 2004/067737的SEQ ID NO:1的位置171、173、175、179、或180，其中所述蛋白酶变体与WO 2004/067737的SEQ ID NO:1具有至少75％但小于100％的序列同一性。
适合的可商购蛋白酶包括以下列商标名出售的那些：DuralaseTm、DurazymTm、 Ultra、 Ultra、 Ultra、 Ultra、Blaze 100T、Blaze125T、Blaze 150T、和(诺维信公司)，在以下商标名下出售的那些：PurafectPurafect ExcellenzP1000TM、Excellenz P1250TM、Preferenz P100TM、Purafect PreferenzP110TM、Effectenz P1000TM、EffectenzP1050TM、Purafect Effectenz P2000TM、 和(丹斯尼克公司(Danisco)/杜邦公司(DuPont))、AxapemTM(吉斯特布罗卡德斯公司(Gist-BrocasesN.V.))、BLAP(在US5352604的图29中示出的序列)及其变体(汉高公司(Henkel AG))和来自花王株式会社(Kao)的KAP(嗜碱芽孢杆菌枯草杆菌蛋白酶)。
脂肪酶和角质酶：
适合的脂肪酶和角质酶包括细菌或真菌来源的那些。包括化学修饰的或蛋白质工程化的突变体酶。实例包括来自嗜热真菌属的脂肪酶，例如如描述于EP 258068和EP305216中的来自疏绵状嗜热丝孢菌(早先命名为疏棉状腐质霉)；来自腐质霉属的角质酶，例如特异腐质霉(WO 96/13580)；来自假单胞菌属的菌株的脂肪酶(这些中的一些现在改名为伯克霍尔氏菌属)，例如产碱假单胞菌或类产碱假单胞菌(EP 218272)、洋葱假单胞菌(EP331376)、假单胞菌属菌株SD705(WO 95/06720&WO 96/27002)、威斯康星假单胞菌(P.wisconsinensis)(WO 96/12012)；GDSL-型链霉菌属脂肪酶(WO 10/065455)；来自稻瘟病菌的角质酶(WO 10/107560)；来自门多萨假单胞菌的角质酶(US 5,389,536)；来自褐色嗜热裂孢菌(Thermobifida fusca)的脂肪酶(WO 11/084412)；嗜热脂肪土芽孢杆菌脂肪酶(WO 11/084417)；来自枯草芽孢杆菌的脂肪酶(WO 11/084599)；以及来自灰色链霉菌(WO11/150157)和始旋链霉菌(S.pristinaespiralis)的脂肪酶(WO 12/137147)。
其他实例是脂肪酶变体，例如描述于EP 407225、WO 92/05249、WO 94/01541、WO94/25578、WO 95/14783、WO 95/30744、WO 95/35381、WO 95/22615、WO 96/00292、WO 97/04079、WO 97/07202、WO 00/34450、WO 00/60063、WO 01/92502、WO 07/87508以及WO 09/109500中的那些。
优选的商业化脂肪酶产品包括LipolaseTM、LipexTM；LipolexTM和LipocleanTM(诺维信公司)，Lumafast(来自杰能科公司(Genencor))以及Lipomax(来自吉斯特布罗卡德斯公司(Gist-Brocades))。
还其他实例是有时称为酰基转移酶或过水解酶的脂肪酶，例如与南极假丝酵母(Candida antarctica)脂肪酶A具有同源性的酰基转移酶(WO 10/111143)、来自耻垢分枝杆菌(Mycobacterium smegmatis)的酰基转移酶(WO 05/56782)、来自CE 7家族的过水解酶(WO 09/67279)以及耻垢分枝杆菌过水解酶的变体(特别是来自亨斯迈纺织品染化有限公司(Huntsman Textile Effects Pte Ltd)的商业产品Gentle Power Bleach中所用的S54V变体)(WO 10/100028)。
淀粉酶：
可以用于本发明中的适合的淀粉酶可以是α-淀粉酶或葡糖淀粉酶并且可以具有细菌或真菌来源。包括化学修饰的突变体或蛋白质工程化的突变体。淀粉酶包括例如从芽孢杆菌属，例如地衣芽孢杆菌的特定菌株(更详细地描述于GB 1,296,839中)获得的α-淀粉酶。
适合的淀粉酶包括具有WO 95/10603中的SEQ ID NO:2的淀粉酶或其与SEQ IDNO:3具有90％序列同一性的变体。优选变体描述于WO 94/02597、WO 94/18314、WO 97/43424以及WO 99/019467的SEQ ID NO:4中，例如在以下位置中的一个或多个处具有取代的变体：15、23、105、106、124、128、133、154、156、178、179、181、188、190、197、201、202、207、208、209、211、243、264、304、305、391、408以及444。
不同的适合的淀粉酶包括具有在WO 02/010355中的SEQ ID NO:6的淀粉酶或其与SEQ ID NO:6具有90％序列同一性的变体。SEQ ID NO:6的优选变体是具有在位置181和182处的缺失和在位置193处的取代的那些。
其他适合的淀粉酶是包含示于WO 2006/066594的SEQ ID NO:6中的来源于解淀粉芽孢杆菌的α-淀粉酶的残基1-33和示于WO 2006/066594的SEQ ID NO:4中的地衣芽孢杆菌α-淀粉酶的残基36-483的杂合α-淀粉酶或其具有90％序列同一性的变体。此杂合α-淀粉酶的优选的变体是在以下位置中的一个或多个中具有取代、缺失或插入的那些：G48、T49、G107、H156、A181、N190、M197、I201、A209以及Q264。包含示于WO 2006/066594的SEQ ID NO:6中的来源于解淀粉芽孢杆菌的α-淀粉酶的残基1-33和SEQ ID NO:4的残基36-483的杂合α-淀粉酶的最优选变体是具有以下取代的那些：
M197T
H156Y+A181T+N190F+A209V+Q264S；或
G48A+T49I+G107A+H156Y+A181T+N190F+I201F+A209V+Q264S。
另外适合的淀粉酶是具有WO 99/019467中的SEQ ID NO:6的淀粉酶或其与SEQ IDNO:6具有90％序列同一性的变体。SEQ ID NO:6的优选的变体是在以下位置中的一个或多个处具有取代、缺失或插入的那些：R181、G182、H183、G184、N195、I206、E212、E216以及K269。特别优选的淀粉酶是在位置R181和G182、或位置H183和G184中具有缺失的那些。
可以使用的另外的淀粉酶是具有WO 96/023873的SEQ ID NO:1、SEQ ID NO:3、SEQID NO:2或SEQ ID NO:7的那些或其与SEQ ID NO:1、SEQ ID NO:2、SEQ ID NO:3或SEQ IDNO:7具有90％序列同一性的变体。SEQ ID NO:1、SEQ ID NO:2、SEQ ID NO:3或SEQ ID NO:7的优选的变体是在以下位置中的一个或多个中具有取代、缺失或插入的那些：140、181、182、183、184、195、206、212、243、260、269、304、以及476，使用WO 96/023873的SEQ ID 2用于编号。更优选的变体是在选自181、182、183和184的两个位置(如181和182、182和183、或位置183和184)中具有缺失的那些。SEQ ID NO:1、SEQ ID NO:2或SEQ ID NO:7的最优选的淀粉酶变体是在位置183和184中具有缺失并且在位置140、195、206、243、260、304和476中的一个或多个中具有取代的那些。
其他可以使用的淀粉酶是具有WO 08/153815的SEQ ID NO:2、WO 01/66712的SEQID NO:10的淀粉酶或其与WO 08/153815的SEQ ID NO:2具有90％序列同一性或与WO 01/66712的SEQ ID NO:10具有90％序列同一性的变体。WO 01/66712中的SEQ ID NO:10的优选变体是在以下位置中的一个或多个处具有取代、缺失或插入的那些：176、177、178、179、190、201、207、211以及264。
另外的适合的淀粉酶是具有WO 09/061380的SEQ ID NO:2的淀粉酶或其与SEQ IDNO:2具有90％序列同一性的变体。SEQ ID NO:2的优选的变体是在以下位置中的一个或多个中具有C-末端截短和/或取代、缺失或插入的那些：Q87、Q98、S125、N128、T131、T165、K178、R180、S181、T182、G183、M201、F202、N225、S243、N272、N282、Y305、R309、D319、Q320、Q359、K444以及G475。SEQ ID NO:2的更优选的变体是在以下位置中的一个或多个处具有取代的那些：Q87E,R、Q98R、S125A、N128C、T131I、T165I、K178L、T182G、M201L、F202Y、N225E,R、N272E,R、S243Q,A,E,D、Y305R、R309A、Q320R、Q359E、K444E以及G475K，和/或在位置R180和/或S181或T182和/或G183处具有缺失的那些。SEQ ID NO:2的最优选的淀粉酶变体是具有以下取代的那些：
N128C+K178L+T182G+Y305R+G475K；
N128C+K178L+T182G+F202Y+Y305R+D319T+G475K；
S125A+N128C+K178L+T182G+Y305R+G475K；或
S125A+N128C+T131I+T165I+K178L+T182G+Y305R+G475K，其中这些变体是C-末端截短的并且任选地进一步包含在位置243处的取代和/或在位置180和/或位置181处的缺失。
另外的适合的淀粉酶是具有WO 13184577中的SEQ ID NO:1的淀粉酶或其与SEQID NO:1具有90％序列同一性的变体。SEQ ID NO:1的优选的变体是在以下位置中的一个或多个处具有取代、缺失或插入的那些：K176、R178、G179、T180、G181、E187、N192、M199、I203、S241、R458、T459、D460、G476和G477。SEQ ID NO:1的更优选的变体是在以下位置中的一个或多个处具有取代的那些：K176L、E187P、N192FYH、M199L、I203YF、S241QADN、R458N、T459S、D460T、G476K、以及G477K，和/或在位置R178和/或S179或T180和/或G181中具有缺失的那些。SEQ ID NO:1的最优选的淀粉酶变体是具有以下取代的那些：
E187P+I203Y+G476K
E187P+I203Y+R458N+T459S+D460T+G476K
其中这些变体任选地进一步包含在位置241处的取代和/或在位置178和/或位置179处的缺失。
另外的适合的淀粉酶是具有WO10104675中的SEQ ID NO:1的淀粉酶或其与SEQ IDNO:1具有90％序列同一性的变体。SEQ ID NO:1的优选的变体是在以下位置中的一个或多个处具有取代、缺失或插入的那些：N21、D97、V128、K177、R179、S180、I181、G182、M200、L204、E242、G477和G478。SEQ ID NO:1的更优选的变体是在以下位置中的一个或多个处具有取代的那些：N21D、D97N、V128I、K177L、M200L、L204YF、E242QA、G477K、以及G478K，和/或在位置R179和/或S180或I181和/或G182中具有缺失的那些。SEQ ID NO:1的最优选的淀粉酶变体是具有以下取代的那些：
N21D+D97N+V128I
其中这些变体任选地进一步包含在位置200处的取代和/或在位置180和/或位置181处的缺失。
其他合适的淀粉酶是具有在WO 01/66712中的SEQ ID NO:12的α-淀粉酶或与SEQID NO:12具有至少90％序列同一性的变体。优选的淀粉酶变体是在WO 01/66712中的SEQID NO:12中的以下位置中的一个或多个处具有取代、缺失或插入的那些：R28、R118、N174；R181、G182、D183、G184、G186、W189、N195、M202、Y298、N299、K302、S303、N306、R310、N314；R320、H324、E345、Y396、R400、W439、R444、N445、K446、Q449、R458、N471、N484。特别优选的淀粉酶包括具有D183和G184的缺失并且具有取代R118K、N195F、R320K和R458K的变体，以及另外在一个或多个选自下组的位置处具有取代的变体：M9、G149、G182、G186、M202、T257、Y295、N299、M323、E345以及A339，最优选的是另外在所有这些位置处具有取代的变体。
其他的实例是淀粉酶变体，例如在WO2011/098531、WO2013/001078和WO2013/001087中描述的那些。
可商购的淀粉酶是DuramylTM、TermamylTM、FungamylTM、Stainzyme TM、StainzymePlusTM、NatalaseTM、Liquozyme X和BANTM(来自诺维信公司)、以及RapidaseTM、PurastarTM/EffectenzTM、Powerase、Preferenz S1000、Preferenz S100和Preferenz S110(来自杰能科国际有限公司/杜邦公司(Genencor International Inc./DuPont))。
过氧化物酶/氧化酶
根据本发明的过氧化物酶是由酶分类EC 1.11.1.7囊括的由国际生物化学和分子生物学联盟命名委员会(IUBMB)规定的酶，或来源于其中的展示出过氧化物酶活性的任何片段。
适合的过氧化物酶包括植物、细菌或真菌来源的那些。包括化学修饰的突变体或蛋白质工程化的突变体。有用的过氧化物酶的实例包括来自拟鬼伞属，例如来自灰盖拟鬼伞(C.cinerea)的过氧化物酶(EP 179,486)，及其变体，如在WO 93/24618、WO 95/10602以及WO 98/15257中描述的那些。可商购的过氧化物酶包括GuardzymeTM(诺维信公司(Novozymes A/S))。
根据本发明的过氧化物酶还包括卤代过氧化物酶，例如氯过氧化物酶、溴过氧化物酶以及展示出氯过氧化物酶或溴过氧化物酶活性的化合物。根据其对卤素离子的特异性将卤代过氧化物酶进行分类。氯过氧化物酶(E.C.1.11.1.10)催化从氯离子形成次氯酸盐。
在实施例中，本发明的卤代过氧化物酶是氯过氧化物酶。优选地，该卤代过氧化物酶是钒卤代过氧化物酶，即含钒酸盐的卤代过氧化物酶。在本发明的优选方法中，将含钒酸盐的卤代过氧化物酶与氯离子来源组合。
已从许多不同真菌，特别是从暗色丝孢菌(dematiaceous hyphomycete)真菌组中分离出了卤代过氧化物酶，如卡尔黑霉属(Caldariomyces)(例如，煤卡尔黑霉(C.fumago))、链格孢属、弯孢属(例如，疣枝弯孢(C.verruculosa)和不等弯孢(C.inaequalis))、内脐蠕孢属、细基格孢属以及葡萄孢属。
还已从细菌，如假单胞菌属(例如，吡咯假单胞菌(P.pyrrocinia))和链霉菌属(例如，金色链霉菌(S.aureofaciens))中分离出了卤代过氧化物酶。
在优选实施例中，该卤代过氧化物酶可来源于弯孢属物种，特别是疣枝弯孢(Curvularia verruculosa)和不等弯孢，例如如描述于WO 95/27046中的不等弯孢CBS102.42或描述于WO 97/04102中的疣枝弯孢CBS 147.63或疣枝弯孢CBS 444.70；或来源于如描述于WO 01/79459中的Drechslera hartlebii、如描述于WO 01/79458中的盐沼小树状霉(Dendryphiella salina)、如描述于WO 01/79461中的Phaeotrichoconis crotalarie、或如描述于WO 01/79460中的Geniculosporium属物种。
根据本发明的氧化酶具体包括由酶分类EC 1.10.3.2所包含的任何漆酶或来源于其的展示出漆酶活性的任何片段、或展示出类似活性的化合物，如儿茶酚氧化酶(EC1.10.3.1)、邻氨基苯酚氧化酶(EC 1.10.3.4)或胆红素氧化酶(EC 1.3.3.5)。
优选的漆酶是微生物来源的酶。这些酶可以来源于植物、细菌或真菌(包括丝状真菌和酵母)。
来自真菌的适合实例包括可来源于以下的菌株的漆酶：曲霉属，脉孢菌属(例如，粗糙脉孢菌)，柄孢壳菌属，葡萄孢属，金钱菌属(Collybia)，层孔菌属(Fomes)，香菇属，侧耳属，栓菌属(例如，长绒毛栓菌和变色栓菌)，丝核菌属(例如，立枯丝核菌(R.solani))，拟鬼伞属(例如，灰盖拟鬼伞、毛头拟鬼伞(C.comatus)、弗瑞氏拟鬼伞(C.friesii)及C.plicatilis)，小脆柄菇属(Psathyrella)(例如，白黄小脆柄菇(P.condelleana))，斑褶菇属(例如，蝶形斑褶菇(P.papilionaceus))，毁丝霉属(例如，嗜热毁丝霉)，Schytalidium(例如，S.thermophilum)，多孔菌属(例如，P.pinsitus)，射脉菌属(例如，射脉侧菌(P.radiata))(WO 92/01046)或革盖菌属(例如，毛革盖菌(C.hirsutus))(JP 2238885)。
来自细菌的适合实例包括可来源于芽孢杆菌属的菌株的漆酶。
优选的是来源于拟鬼伞属或毁丝霉属的漆酶；特别是来源于灰盖拟鬼伞的漆酶，如披露于WO 97/08325中；或来源于嗜热毁丝霉，如披露于WO 95/33836中。
共颗粒中酶的配制品
本发明的一种或多种酶可以被配制为颗粒，例如，配制为结合一种或多种酶的共颗粒。然后，每种酶将存在于多种颗粒中，这些颗粒确保酶在洗涤剂中的分布更均匀。这还减少了由于不同的粒度，不同酶的物理隔离。用于生产针对洗涤剂工业的多酶共颗粒的方法披露于IP.com披露内容IPCOM000200739D中。
通过使用共颗粒的酶的配制品的另一个实例披露于WO 2013/188331中，其涉及包含以下项的洗涤剂组合物：(a)多酶共颗粒；(b)少于10wt沸石(无水的基础上)；和(c)少于10wt磷酸盐(无水的基础上)，其中所述酶共颗粒包含从10wt％至98wt％的水分汇组分(sink component)，并且该组合物另外还包含从20wt％至80wt％的洗涤剂水分汇组分。
WO 2013/188331还涉及处理和/或清洁表面(优选地织物表面)的方法，该方法包括以下步骤：(i)使所述表面在含水洗涤液中与如在本文要求保护的并且描述的洗涤剂组合物接触，(ii)漂洗和/或干燥该表面。
该多酶共颗粒可以包含本发明的酶和(a)一种或多种选自下组的酶，该组由以下组成：首次洗涤脂肪酶、清洁纤维素酶、木葡聚糖酶、过水解酶、过氧化物酶、脂加氧酶、漆酶及其混合物；和(b)一种或多种选自下组的酶，该组由以下组成：半纤维素酶、蛋白酶、护理纤维素酶、纤维二糖脱氢酶、木聚糖酶、磷脂酶、酯酶、角质酶、果胶酶、甘露聚糖酶、果胶裂解酶、角蛋白酶、还原酶、氧化酶、酚氧化酶、木质酶、普鲁兰酶、鞣酸酶、戊聚糖酶、地衣聚糖酶、葡聚糖酶、阿拉伯糖苷酶、玻璃酸酶、软骨素酶、淀粉酶、及其混合物。
在以下段落中进一步定义本发明：
1.一种淀粉酶和/或蛋白酶用于去除和/或减少表面上的污垢、和/或用于减少再沉积的用途，其中将所述表面暴露于所述淀粉酶和/或蛋白酶持续10至240秒的时间段。
2.根据段落1所述的用途，其中将所述表面暴露于所述淀粉酶和/或蛋白酶持续10至220秒的时间段，例如在10至200秒的范围内、在10至180秒的范围内、在10至160秒的范围内、在10至140秒的范围内、在10至120秒的范围内、在10至100秒的范围内、在10至80秒的范围内、在10至70秒的范围内、在10至66秒的范围内、在20至66秒的范围内、在25至66秒的范围内、在28至66秒的范围内、在28至60秒的范围内、在28至55秒的范围内、在28至50秒的范围内或在28至45秒的范围内。
3.根据前述段落中任一项所述的用途，其中所述淀粉酶和/或蛋白酶包含在具有在7-10.5范围内的pH的液体中。
4.根据段落4所述的用途，其中所述pH是在7.5-10.5的范围内、例如在7.5-10的范围内、在7.5-9.5的范围内、在7.5-9.0的范围内、在7.5-8.5的范围内、在7.5-8.2的范围内、或在7.8-8.2的范围内。
5.根据前述段落中任一项所述的用途，其中使用淀粉酶。
6.根据段落5所述的用途，其中所述淀粉酶与SEQ ID NO:1、2、3或4的序列具有至少70％，例如至少75％、例如至少80％、例如至少85％、例如至少90％、例如至少95％、例如至少98％、例如至少99％、例如100％的序列同一性。
7.根据段落6所述的用途，其中所述淀粉酶是α-淀粉酶变体，其包含以下修饰：SEQID NO:1的D183*+G184*+R118K+N195F+R320K+R458K或M9L+R118K+G149A+G182T+G186A+D183*+G184*+N195F+M202L+T257I+Y295F+N299Y+R320K+M323T+A339S+E345R+R458K；SEQID NO:2的D183*+G184*或W140Y+D183*+G184*+N195F+V206Y+Y243F+E260G+G304R+G476K；SEQ ID NO:3的H156Y+A181T+N190F+A209V+Q264S，其中所述α-淀粉酶变体分别与SEQ IDNO:1、2或3具有至少75％但小于100％的序列同一性，并且其中所述α-淀粉酶变体具有α-淀粉酶活性。
8.根据段落6所述的用途，其中所述淀粉酶是α-淀粉酶变体，所述变体在与以下位置对应的一个或多个位置处包含修饰：SEQ ID NO:4的H1、N54、V56、K72、G109、F113、R116、T134、W140、W159、W167、Q169、Q172、L173、A174、R181、G182、D183、G184、W189、E194、N195、V206、G255、N260、F262、A265、W284、F289、S304、G305、W347、K391、Q395、W439、W469、R444、F473、G476和G477，其中所述α-淀粉酶变体与SEQ ID NO:4具有至少75％但小于100％的序列同一性并且其中所述α-淀粉酶变体具有α-淀粉酶活性。
9.根据段落6或8所述的用途，其中所述一个或多个位置处的修饰选自下组，该组由以下组成：H1*、H1A、N54S、V56T、K72R、G109A、F113Q、R116Q、R116H、T134E、W140Y、W140F、W140H、W159Y、W159F、W159H、W167Y、W167H、W167F、Q169E、Q172K、Q172G、Q172N、L173P、A174*、A174S、R181*、G182*、D183*、G184*、G184T、W189Y、W189F、W189H、W189E、W189D、W189Q、W189N、E194D、E194N、E194S、N195F、V206L、V206F、V206Y、G255A、N260G、N260P、N260A、N260G、N260P、N260A、A265G、W284G、W284H、F289H、S304K、S304R、S304Q、S304E、G305K、G305R、G305Q、G305E、W347Y、W347F、W347H、K391A、Q395P、W439N、W439Q、W439T、R444Q、W469T、W469N、F473R、G476R、G476Q、G476E、G476K G477K、G477R、G477Q、以及G477E，其中这些位置对应于SEQ ID NO:4的位置。
10.根据段落6或8-9所述的用途，其中所述至少一种α-淀粉酶变体在与SEQ IDNO:4的R181+G182；R181+D183；R181+G184；G182+D183；G182+G184或D183+G184对应的位置处包含缺失。
11.根据段落6或8-10所述的用途，其中所述α-淀粉酶变体选自下组，该组由以下组成：
SEQ ID NO:4的多肽的H1*+N54S+V56T+G109A+Q169E+Q172K+A174*+G182*+D183*+N195F+V206L+K391A+G476K；
H1*+N54S+V56T+G109A+R116H+A174S+G182*+D183*+N195F+V206L+K391A+G476K；
H1*+N54S+V56T+K72R+G109A+F113Q+R116Q+W167F+Q172G+A174S+G182*+D183*+G184T+N195F+V206L+K391A+P473R+G476K；
H1*+N54S+V56T+G109A+F113Q+R116Q+Q172N+A174S+G182*+D183*+N195F+V206L+A265G+K391A+P473R+G476K；
H1*+N54S+V56T+K72R+G109A+F113Q+W167F+Q172R+A174S+G182*+D183*+N195F+V206L+K391A+G476K；
H1*+N54S+V56T+K72R+G109A+R116H+T134E+W167F+Q172G+L173V+A174S+G182*+D183*+N195F+V206L+G255A+K391A+G476K；
H1*+N54S+V56T+K72R+G109A+R116H+T134E+W167F+Q172G+L173V+A174S+G182*+D183*+N195F+V206L+G255A+K391A+Q395P+T444Q+P473R+G476K；
H1*+N54S+V56T+G109A+T134E+A174S+G182*+D183*+N195F+V206L+K391A+G476K；
H1*+N54S+V56T+K72R+G109A+A174S+G182*+D183*+N195F+V206L+G255A+K391A+G476K；
H1*+N54S+V56T+K72R+G109A+F113Q+R116Q+W167F+Q172G+A174S+G184T+N195F+V206L+K391A+P473R+G476K，以及
H1*+N54S+V56T+G109A+W167F+Q172E+L173P+A174K+G182*+D183*+N195F+V206L+K391A+G476K，并且其中所述α-淀粉酶变体与SEQ ID NO:4的多肽共享至少80％，例如至少85％、例如至少90％、例如至少93％、例如至少94％、例如至少95％、例如至少96％、例如至少97％、例如至少98％但小于100％的序列同一性，并且其中所述α-淀粉酶变体具有α-淀粉酶活性。
12.根据前述段落中任一项所述的用途，其中使用蛋白酶。
13.根据段落12所述的用途，其中所述蛋白酶选自下组，该组由以下组成：
i.与SEQ ID NO:5、6、7或8的序列具有至少70％，例如至少75％、例如至少80％、例如至少85％、例如至少90％、例如至少95％、例如至少98％、例如至少99％、例如100％的序列同一性的蛋白酶；
ii.在与SEQ ID NO:3的位置9、15、36、61、68、76、99、106、120、167、170、194、195、205、218、235、245或261对应的一个或多个位置处包含取代的蛋白酶变体，其中所述蛋白酶变体与SEQ ID NO:5具有至少75％但小于100％的序列同一性，
iii.SEQ ID NO:24的蛋白酶。
14.根据段落13所述的用途，其中所述蛋白酶选自下组，该组由以下组成：SEQ IDNO:5的M222S、*36D+N76D+N120D+G195E+K235L、Y167A+R170S+A194P、S99SE、V68A+S106A、S9R+A15T+V68A+N218D+Q245R、S9R+A15T+G61E+V68A+A194P+V205I+Q245R+N261D和S99AD，其中所述蛋白酶变体与SEQ ID NO:5具有至少75％但小于100％的序列同一性，并且其中所述蛋白酶变体具有蛋白酶活性。
15.根据前述段落中任一项所述的用途，其中使用淀粉酶和蛋白酶。
16.根据前述段落中任一项所述的用途，其中使用另外的酶，所述酶选自下组，该组由以下组成：蛋白酶、脂肪酶、角质酶、淀粉酶、糖酶、纤维素酶、果胶酶、甘露聚糖酶、阿拉伯糖酶、半乳聚糖酶、木聚糖酶、氧化酶、地衣多糖酶、漆酶和/或过氧化物酶。
17.根据前述段落中任一项所述的用途，其中所述表面是器皿洗涤机的内表面或器皿的表面。
18.一种器皿洗涤洗涤剂组合物，所述组合物包含淀粉酶和/或蛋白酶和一种或多种洗涤剂组分，所述组合物具有在7-10.5范围内的pH。
19.根据段落18所述的组合物，其中所述洗涤剂组分选自下组，该组由以下组成：表面活性剂、助洗剂、螯合剂或螯合试剂、漂白体系或漂白组分、聚合物、增泡剂、抑泡剂、染料、香料、晦暗抑制剂、光学增亮剂、杀细菌剂、杀真菌剂、污垢悬浮剂、抗腐蚀剂、酶稳定剂、酶抑制剂或活化剂、一种或多种转移酶、水解酶、氧化还原酶、上蓝剂和荧光染料、抗氧化剂、以及增溶剂。
20.根据段落18-19中任一项所述的组合物，其中所述组合物包含至少5％wt.的螯合剂。
21.根据段落18-20中任一项所述的组合物，其中所述组合物包含少于2％的表面活性剂。
22.根据段落18-20中任一项所述的组合物，其中所述组合物不包含表面活性剂。
23.根据段落18-22中任一项所述的组合物，其中所述组合物是用于工业或机构用途的器皿洗涤洗涤剂组合物。
24.根据段落18-23中任一项所述的组合物，其中所述洗涤液的pH是在7-10.5的范围内。
25.根据段落24所述的组合物，其中所述pH是在7.5-10.5的范围内、例如在7.5-10的范围内、在7.5-9.5的范围内、在7.5-9.0的范围内、在7.5-8.5的范围内、在7.5-8.2的范围内、或在7.8-8.2的范围内。
26.根据段落18-25中任一项所述的组合物，其中所述组合物是条，块，均匀的片剂，具有两层或更多层的片剂，具有一个或多个室的袋，规则的或压缩的粉末，颗粒，膏，凝胶，或者规则的、压缩的或浓缩的液体。
27.根据段落18-26中任一项所述的组合物，其中所述组合物包含支链脂肪酸分解剂。
28.根据段落27所述的组合物，其中所述支链脂肪酸分解剂选自以下项的组：异壬酸钠、异壬酸、异辛酸钠、异辛酸、新癸酸钠、新癸酸、新戊酸钠、新戊酸、新庚酸钠、新庚酸、3,5,5-三甲基己酸、6-甲基-庚酸、2,2-二甲基辛酸、新戊酸(2,2-二甲基丙酸)、2,2-二甲基戊酸、及其盐、或其混合物。
29.根据段落18-28中任一项所述的组合物，其中所述组合物是当在68℃下暴露于4000mL水溶液时具有至少15g/分钟的溶解速率的块或片剂。
30.根据段落18-29中任一项所述的组合物，其中所述组合物进一步包含一种或多种蛋白酶抑制剂，所述蛋白酶抑制剂中至少一种是肽醛、其亚硫酸氢盐加合物或半缩醛加合物。
31.根据段落30所述的组合物，其中所述蛋白酶抑制剂是式P-(A)y-L-(B)x-B0-H的肽醛或其亚硫酸氢盐加合物或半缩醛加合物，其中：
i.H是氢；
ii.B0是具有式-NH-CH(R)-C(＝O)-的L-或D-构型的单一氨基酸残基；
iii.(B)x的x是1、2或3，并且B独立地是经由(B)x氨基酸的C端连接到B0上的单一氨基酸
iv.L不存在或L独立地是式-C(＝O)-、-C(＝O)-C(＝O)-、-C(＝S)-、-C(＝S)-C(＝S)-或-C(＝S)-C(＝O)-的连接基团；
v.(A)y的y是0、1或2，并且A独立地是经由(A)y氨基酸的N端连接到L上的单一氨基酸残基，其前提是如果L不存在，那么A不存在；
vi.P选自下组，该组由以下组成：氢和N端保护基团，其前提是如果L不存在，那么P是N端保护基团；
vii.R独立地选自下组，该组由以下组成：任选地被一个或多个相同或不同的取代基R'取代的C1-6烷基、C6-10芳基或C7-10芳烷基；
viii.R’独立地选自下组，该组由以下组成：卤素、-OH、-OR”、-SH、-SR”、-NH2、-NHR”、-NR”2、-CO2H、-CONH2、-CONHR”、-CONR”2、-NHC(＝N)NH2；并且
ix.R”是C1-6烷基基团。
32.根据段落31所述的组合物，其中所述肽醛的亚硫酸氢盐加合物具有式P-(A)y-L-(B)x-N(H)-CHR-CH(OH)-SO3M，其中
i.M是氢或碱金属；
ii.(B)x的x是1、2或3，并且B独立地是经由(B)x氨基酸的C端连接到B0上的单一氨基酸
iii.L不存在或L独立地是式-C(＝O)-、-C(＝O)-C(＝O)-、-C(＝S)-、-C(＝S)-C(＝S)-或-C(＝S)-C(＝O)-的连接基团；
iv.(A)y的y是0、1或2，并且A独立地是经由(A)y氨基酸的N端连接到L上的单一氨基酸残基，其前提是如果L不存在，那么A不存在；
v.P选自下组，该组由以下各项组成：氢和一种N端保护基团，其条件是如果L不存在，那么P是一种N端保护基团；
vi.R独立地选自下组，该组由以下组成：任选地被一个或多个相同或不同的取代基R’取代的C1-6烷基、C6-10芳基或C7-10芳烷基；
vii.R’独立地选自下组，该组由以下组成：卤素、-OH、-OR”、-SH、-SR”、-NH2、-NHR”、-NR”2、-CO2H、-CONH2、-CONHR”、-CONR”2、-NHC(＝N)NH2；并且
viii.R”是C1-6烷基基团。
33.根据段落18-32中任一项所述的组合物，其中所述组合物包含淀粉酶
34.根据段落33所述的组合物，其中所述淀粉酶是α-淀粉酶。
35.根据段落34所述的组合物，其中所述淀粉酶与SEQ ID NO:1、2、3或4的序列具有至少70％，例如至少75％、例如至少80％、例如至少85％、例如至少90％、例如至少95％、例如至少98％、例如至少99％、例如100％的序列同一性。
36.根据段落35所述的组合物，其中所述淀粉酶是α-淀粉酶变体，其在与以下位置对应的一个或多个位置处包含修饰：SEQ ID NO:1的D183*+G184*+R118K+N195F+R320K+R458K或M9L+R118K+G149A+G182T+G186A+D183*+G184*+N195F+M202L+T257I+Y295F+N299Y+R320K+M323T+A339S+E345R+R458K；SEQ ID NO:2的D183*+G184*或W140Y+D183*+G184*+N195F+V206Y+Y243F+E260G+G304R+G476K；SEQ ID NO:3的H156Y+A181T+N190F+A209V+Q264S，其中所述α-淀粉酶变体分别与SEQ ID NO:1、2或3具有至少75％但小于100％的序列同一性，并且其中所述α-淀粉酶变体具有α-淀粉酶活性。
37.根据段落35所述的组合物，其中所述淀粉酶是α-淀粉酶变体，其在与以下位置对应的一个或多个位置处包含修饰：SEQ ID NO:4的H1、N54、V56、K72、G109、F113、R116、T134、W140、W159、W167、Q169、Q172、L173、A174、R181、G182、D183、G184、W189、E194、N195、V206、G255、N260、F262、A265、W284、F289、S304、G305、W347、K391、Q395、W439、W469、R444、F473、G476和G477，其中所述α-淀粉酶变体与SEQ ID NO:4具有至少75％但小于100％的序列同一性并且其中所述α-淀粉酶变体具有α-淀粉酶活性。
38.根据段落35和37中任一项所述的组合物，其中所述一个或多个位置处的修饰选自下组，该组由以下组成：H1*、H1A、N54S、V56T、K72R、G109A、F113Q、R116Q、R116H、T134E、W140Y、W140F、W140H、W159Y、W159F、W159H、W167Y、W167H、W167F、Q169E、Q172K、Q172G、Q172N、L173P、A174*、A174S、R181*、G182*、D183*、G184*、G184T、W189Y、W189F、W189H、W189E、W189D、W189Q、W189N、E194D、E194N、E194S、N195F、V206L、V206F、V206Y、G255A、N260G、N260P、N260A、N260G、N260P、N260A、A265G、W284G、W284H、F289H、S304K、S304R、S304Q、S304E、G305K、G305R、G305Q、G305E、W347Y、W347F、W347H、K391A、Q395P、W439N、W439Q、W439T、R444Q、W469T、W469N、F473R、G476R、G476Q、G476E、G476K G477K、G477R、G477Q、以及G477E，其中这些位置对应于SEQ ID NO:4的位置。
39.根据段落35和37-38中任一项所述的组合物，其中所述至少一种α-淀粉酶变体在与SEQ ID NO:4的R181+G182；R181+D183；R181+G184；G182+D183；G182+G184或D183+G184对应的位置处包含缺失。
40.根据段落35和37-39中任一项所述的组合物，其中(i)中的所述α-淀粉酶变体选自下组，该组由以下组成：
SEQ ID NO:4的多肽的H1*+N54S+V56T+G109A+Q169E+Q172K+A174*+G182*+D183*+N195F+V206L+K391A+G476K；
H1*+N54S+V56T+G109A+R116H+A174S+G182*+D183*+N195F+V206L+K391A+G476K；
H1*+N54S+V56T+K72R+G109A+F113Q+R116Q+W167F+Q172G+A174S+G182*+D183*+G184T+N195F+V206L+K391A+P473R+G476K；
H1*+N54S+V56T+G109A+F113Q+R116Q+Q172N+A174S+G182*+D183*+N195F+V206L+A265G+K391A+P473R+G476K；
H1*+N54S+V56T+K72R+G109A+F113Q+W167F+Q172R+A174S+G182*+D183*+N195F+V206L+K391A+G476K；
H1*+N54S+V56T+K72R+G109A+R116H+T134E+W167F+Q172G+L173V+A174S+G182*+D183*+N195F+V206L+G255A+K391A+G476K；
H1*+N54S+V56T+K72R+G109A+R116H+T134E+W167F+Q172G+L173V+A174S+G182*+D183*+N195F+V206L+G255A+K391A+Q395P+T444Q+P473R+G476K；
H1*+N54S+V56T+G109A+T134E+A174S+G182*+D183*+N195F+V206L+K391A+G476K；
H1*+N54S+V56T+K72R+G109A+A174S+G182*+D183*+N195F+V206L+G255A+K391A+G476K；
H1*+N54S+V56T+K72R+G109A+F113Q+R116Q+W167F+Q172G+A174S+G184T+N195F+V206L+K391A+P473R+G476K，以及
H1*+N54S+V56T+G109A+W167F+Q172E+L173P+A174K+G182*+D183*+N195F+V206L+K391A+G476K，并且其中所述α-淀粉酶变体与SEQ ID NO:4的多肽共享至少80％，例如至少85％、例如至少90％、例如至少93％、例如至少94％、例如至少95％、例如至少96％、例如至少97％、例如至少98％但小于100％的序列同一性，并且其中所述α-淀粉酶变体具有α-淀粉酶活性。
41.根据段落18-40中任一项所述的组合物，其中所述组合物包含蛋白酶。
42.根据段落41所述的组合物，其中所述蛋白酶选自下组，该组由以下组成：
i.与SEQ ID NO:5、6、7或8的序列具有至少70％，例如至少75％、例如至少80％、例如至少85％、例如至少90％、例如至少95％、例如至少98％、例如至少99％、例如100％的序列同一性的蛋白酶；
ii.在与SEQ ID NO:3的位置9、15、36、61、68、76、99、106、120、167、170、194、195、205、218、235、245或261对应的一个或多个位置处包含取代的蛋白酶变体，其中所述蛋白酶变体与SEQ ID NO:5具有至少75％但小于100％的序列同一性，
iii.SEQ ID NO:24的蛋白酶。
43.根据段落42所述的组合物，其中所述蛋白酶选自下组，该组由以下组成：SEQID NO:5的M222S、*36D+N76D+N120D+G195E+K235L、Y167A+R170S+A194P、S99SE、V68A+S106A、S9R+A15T+V68A+N218D+Q245R、S9R+A15T+G61E+V68A+A194P+V205I+Q245R+N261D和S99AD，其中所述蛋白酶变体与SEQ ID NO:5具有至少75％但小于100％的序列同一性，并且其中所述蛋白酶变体具有蛋白酶活性。
44.根据段落18-43中任一项所述的组合物，进一步包含选自下组的另外的酶，该组由以下组成：另外的蛋白酶、脂肪酶、角质酶、另外的淀粉酶、糖酶、纤维素酶、果胶酶、甘露聚糖酶、阿拉伯糖酶、半乳聚糖酶、木聚糖酶、氧化酶、地衣多糖酶、漆酶和/或过氧化物酶。
45.根据段落44所述的组合物，其中所述地衣多糖酶是与选自下组的序列的成熟多肽具有至少89％序列同一性的多肽，该组由以下组成：SEQID NO:18、SEQ ID NO:19、SEQID NO:20、SEQ ID NO:21或SEQ ID NO:22。
46.根据段落45所述的组合物，其中所述地衣多糖酶是SEQ ID NO:18、SEQ ID NO:19、SEQ ID NO:20、SEQ ID NO:21或SEQ ID NO:22的His-标记的重组成熟多肽。
47.根据段落44所述的组合物，其中所述地衣多糖酶是SEQ ID NO:23。
48.一种用于去除和/或减少表面上的污垢的方法，其中清洁循环包括以下步骤：
i.洗涤步骤，其中将所述表面暴露于包含以下项的洗涤液
a.淀粉酶和/或蛋白酶和任选的洗涤剂组分，或
b.根据段落18-47所述的器皿洗涤洗涤剂组合物，
ii.任选地排出部分所述洗涤液，
iii.任选地漂洗所述表面，
iv.任选地干燥所述表面；
其中将所述表面暴露于所述洗涤液持续在10至240秒范围内的时间段。
49.根据段落48所述的方法，其中清洁循环包括漂洗步骤。
50.根据段落48-49中任一项所述的方法，其中清洁循环包括干燥步骤。
51.根据段落48-50中任一项所述的方法，其中清洁循环包括漂洗和干燥步骤。
52.根据段落48-51中任一项所述的方法，其中清洁水任选地与漂洗助剂一起用于所述漂洗步骤。
53.根据段落48-52中任一项所述的方法，其中所述方法包括在步骤a之前的浸泡步骤。
54.根据段落48-53中任一项所述的方法，其中所述方法包括排出步骤，其中排出部分所述洗涤液。
55.根据段落54所述的方法，其中来自漂洗步骤c的清洁水替换所排出的洗涤液。
56.根据段落54-55所述的方法，其中5％-15％的所述洗涤液被清洁水替换。
57.根据段落56所述的方法，其中7.5％的所述洗涤液被清洁水替换。
58.根据段落48-57中任一项所述的方法，其中所述洗涤液在随后的清洁循环中重复使用。
59.根据段落48-58中任一项所述的方法，其中所述表面经历所述清洁循环1次。
60.根据段落48-59中任一项所述的方法，其中所述表面经历所述清洁循环2次、3次、4次或5次。
61.根据段落48-60中任一项所述的方法，其中所述洗涤液包含根据段落18-47中任一项所述的组合物。
62.根据段落48-61中任一项所述的方法，其中所述洗涤液供应有来自单独容器的酶和洗涤剂组分。
63.根据段落62所述的方法，其中洗涤液供应有来自单独容器的淀粉酶和/或蛋白酶以及任选地另外的酶。
64.根据段落48-63中任一项所述的方法，其中将所述表面暴露于所述淀粉酶和/或蛋白酶持续10至220秒的时间段，例如在10至200秒的范围内、在10至180秒的范围内、在10至160秒的范围内、在10至140秒的范围内、在10至120秒的范围内、在10至100秒的范围内、在10至80秒的范围内、在10至70秒的范围内、在10至66秒的范围内、在20至66秒的范围内、在25至66秒的范围内、在28至66秒的范围内、在28至60秒的范围内、在28至55秒的范围内、在28至50秒的范围内或在28至45秒的范围内。
65.根据段落48-64中任一项所述的方法，其中所述洗涤液的pH是在7-10.5的范围内。
66.根据段落65所述的方法，其中所述pH是在7.5-10.5的范围内、例如在7.5-10的范围内、在7.5-9.5的范围内、在7.5-9.0的范围内、在7.5-8.5的范围内、在7.5-8.2的范围内、或在7.8-8.2的范围内。
67.根据段落48-66中任一项所述的方法，其中所述洗涤液的温度是在50℃-95℃的范围内。
68.根据段落67所述的方法，其中所述温度是在50℃-90℃的范围内、在50℃-85℃的范围内、在50℃-80℃的范围内、在50℃-75℃的范围内、在50℃-70℃的范围内、在50℃-65℃的范围内、55℃-62℃、例如在58℃-62℃的范围内。
69.根据段落48-68中任一项所述的方法，其中所述方法在器皿洗涤机中进行，所述器皿洗涤机选自下组，该组由以下组成：门器皿洗涤机、罩器皿洗涤机、传送带器皿洗涤机、台下器皿洗涤机、玻璃洗涤器、飞机器皿洗涤机、罐和锅器皿洗涤机和器具洗涤器。
70.根据段落48-69中任一项所述的方法，其中所述表面是器皿洗涤机的内表面或器皿的表面。
71.根据段落48-70中任一项所述的方法，其中所述洗涤剂组合物的浓度是在0.5-5g/升洗涤液的范围内。
72.根据段落71所述的方法，其中所述浓度是在1-4g/升洗涤液的范围内，例如在1.5-3g/升洗涤液的范围内。
73.根据段落72所述的方法，其中所述浓度是2g/升洗涤液。
实例
器皿洗涤洗涤剂组合物
器皿洗涤洗涤剂组合物
| 组分 | 组成(wt.％) |
| 蒸馏水 | 30-70 |
| 碳酸钠(pH调节剂) | 2-10 |
| 碳酸氢钠(pH调节剂) | 2-10 |
| 1,2-丙二醇(溶剂) | 10-20 |
| 二甲苯磺酸钠40％(增溶剂) | 5-20 |
| Dissolvine GL38(螯合剂) | 2-10 |
| Bio-Soft N91-2.5(非离子表面活性剂) | 1-5 |
漂洗助剂组合物
测定
测定I
将物品浸入碘溶液(0.025M)中持续约30秒。碘与物品上的污垢结合并且从而使得物品上的污垢肉眼可见。由受过训练的测试人员以从1至10的标度评估在相同条件下清洁或测试的物品。1分配给在其上大多数污垢可见(最脏)的物品，并且10分配给在其上较少污垢不可见(最干净)的物品。
测定II-α-淀粉酶活性测定-pNP-G7测定
可以通过使用G7-pNP底物的方法确定α-淀粉酶活性。为4,6-亚乙基(G7)-对硝基苯基(G1)-α,D-麦芽七糖苷的缩写的G7-pNP是可以被内切淀粉酶如α-淀粉酶切割的嵌段寡糖。切割之后，试剂盒中所包括的α-葡糖苷酶进一步消化水解的底物以释放游离PNP分子，该分子具有黄颜色并且因而可以通过可见分光光度法在λ＝405nm(400nm至420nm)测量。包含G7-pNP底物和α-葡糖苷酶的试剂盒由Roche/Hitachi制造(目录号11876473)。
试剂：
来自这个试剂盒的G7-pNP底物包含22mM 4,6-亚乙基-G7-pNP和52.4mM HEPES(2-[4-(2-羟基乙基)-1-哌嗪基]-乙磺酸)，pH 7.0。
α-葡糖苷酶试剂包含52.4mM HEPES、87mM NaCl、12.6mM MgCl2、0.075mM CaCl2、>4kU/L的α-葡糖苷酶。
通过将1mLα-葡糖苷酶试剂与0.2mL G7-pNP底物混合，制成底物工作溶液。此底物工作溶液在使用之前立即制成。
稀释缓冲液：50mM MOPS，0.05％(w/v)Triton X100(聚乙二醇对-(1,1,3,3-四甲基丁基)-苯基醚(C14H22O(C2H4O)n(n＝9-10)))，1mM CaCl2，pH 8.0。
程序：
将待分析的淀粉酶样品稀释于稀释缓冲液中以确保稀释样品中的pH是7。通过将20μl稀释的酶样品转移至96孔微量滴定板中并添加80μl底物工作溶液来进行测定。将溶液混合并在室温预温育1分钟并且在OD 405nm经5分钟每20秒测量吸收。
在给定的一组条件下，时间依赖性吸收曲线的斜率(每分钟的吸光度)与所讨论的α-淀粉酶的比活性(活性/mg酶)成正比。淀粉酶样品应稀释至其中斜率为0.4吸光度单位/分钟以下的水平。
测定III-α-淀粉酶活性测定-Phadebas活性测定
α-淀粉酶活性还可以通过使用Phadebas底物(例如来自瑞典隆德麦戈尔生命科学(Magle Life Sciences,Lund,Sweden))的方法来确定。Phadebas片剂包括互联淀粉聚合物，这些聚合物呈不溶于水的球状微球形式。将蓝色染料共价结合至这些微球。微球中的互联淀粉聚合物以与α-淀粉酶活性成比例的速度降解。当α-淀粉酶降解了淀粉聚合物时，释放的蓝色染料是可溶于水的并且染料浓度可通过在620nm下测量吸光度来确定。蓝色的浓度与样品中的α-淀粉酶活性成比例。
将待分析的α-淀粉酶样品稀释于具有所希望的pH的活性缓冲液中。将两个底物片剂悬浮于5mL活性缓冲液中并且在磁力搅拌器上混合。在混合底物期间，将150μl转移至微量滴定板(MTP)或PCR-MTP。将30μl稀释的淀粉酶样品添加至150μl底物并混合。在37℃温育15分钟。通过添加30μl 1M NaOH并且混合来停止反应。在4000xg离心MTP 5分钟。将100μl转移至新的MTP并且测量620nm的吸光度。
该α-淀粉酶样品应稀释成使得620nm下的吸光度在0与2.2之间，并且在活性测定的线性范围内。
测定IV-α-淀粉酶活性测定-Amylazyme活性测定
α-淀粉酶活性还可以通过使用包括已经与乳糖和硬脂酸镁混合并且压片的AZCL-直链淀粉的淀粉酶底物( Amylazyme Test，由梅格泽姆公司(Megazyme)提供的用于谷类和细菌淀粉酶的测定法)的方法来确定。将蓝色染料共价结合至这些微球。微球中的互联直链淀粉聚合物以与α-淀粉酶活性成比例的速度降解。当α-淀粉酶降解了直链淀粉聚合物时，释放的蓝色染料是可溶于水的并且染料浓度可通过在590nm下测量吸光度来确定。蓝色的浓度与样品中的α-淀粉酶活性成比例。
将待分析的α-淀粉酶样品稀释于具有所希望的pH的活性缓冲液中。将两个底物片剂悬浮于5mL活性缓冲液中并且在磁力搅拌器上混合。在混合底物期间，将150μl转移至微量滴定板(MTP)或PCR-MTP。接下来，将25μl稀释的淀粉酶样品添加到150μl底物中并混合。将混合物在37℃下孵育10分钟。通过添加25μl 1M NaOH并且混合来停止反应。将MTP在4000xg离心5分钟，随后将100μl转移至新的MTP，并在590nm处测量吸光度。
测定V-蛋白酶活性测定：
1)Suc-AAPF-pNA活性测定：
蛋白水解活性可以通过使用Suc-AAPF-PNA底物的方法来确定。Suc-AAPF-PNA是N-琥珀酰基-丙氨酸-丙氨酸-脯氨酸-苯丙氨酸-对硝基苯胺的缩写，并且它是可以被内切蛋白酶切割的一种嵌段肽。在切割后，一个游离PNA分子被释放出来，并且它具有黄颜色并且因此可以通过可见光分光光度法在波长405nm进行测量。该Suc-AAPF-PNA底物由巴亨公司(Bachem)制造(目录号L1400，溶解于DMSO中)。
待分析的蛋白酶样品被稀释在残余活性缓冲液(100mM Tris pH 8.6)中。通过转移60μl的稀释的酶样品至96孔微量滴定板并添加140μl底物工作溶液(0.72mg/ml于100mMTris pH 8.6)中进行该测定。将该溶液在室温混合并且在OD 405nm经5分钟每20秒测量吸收。
在一组给定条件下，时间相关吸收曲线的斜率(每分钟的吸光度)与所讨论的蛋白酶的比活性(活性/mg酶)成正比例。应该将蛋白酶样品稀释至其中斜率为线性的水平。
测定VI-溶解速率测试程序
本发明中使用的测试程序包括三个开发的测试程序。第一个测试程序是溶解速率测试程序。该测试程序测量当将固体加入不同温度下的水中时所述固体的溶解速率。测试程序如下：
1.在热板上在4000ml烧杯中使3500ml软水达到指定温度。
2.将筛网支架添加到烧杯中(筛网支架将样品放置在距离烧杯底部7.5cm处)。
3.记录待测试的固体样品重量。
4.当水达到指定温度时，添加样品并启动秒表。
5.记录当筛网上没有样品剩余时的时间。
除非另外指出，否则下面呈现的所有溶解速率测试结果均根据上述程序在155°F下进行。溶解速率测试程序也可以在处于或高于室温并低于水溶液沸点的其他指定温度下进行。实例指定温度包括例如但不限于130°F和190°F。
标准室温、压力等条件在其他方面是适用的。
实例1
盘上的器皿洗涤试验
燕麦粥污垢是通过将50克燕麦片加入到250ml的UHT(超高温处理的)牛奶(均质化的，1.5％脂肪)和750ml合成水(16.8°dH)中，在连续搅拌下稳定加热并煮沸10分钟而制备的。
使用刷子，将3g热燕麦粥均匀地涂抹在盘内表面上。盘的边缘保持没有。内盘直径为15cm。将弄脏的盘在热橱柜中在80℃下干燥2小时。当盘已经冷却至室温时，洗涤它们。
在以90秒清洁循环操作的霍巴特(Hobart)AUXX连帽式器皿洗涤器中在1个清洁循环期间洗涤用燕麦粥预先弄脏的盘，该清洁循环包括洗涤步骤(66秒(s)，60℃-65℃)，排出2.5l洗涤液(15s)，用2.5l清洁水漂洗(9s，85℃)以及干燥步骤(31s)。洗涤液的水硬度为0°dH。为了模拟真实生活中厨房中的条件，将压载污垢添加到器皿洗涤器的清洁循环中。在开始清洁循环之前，将1g/L洗涤液压载污垢添加到储槽中。
使用(A)不添加酶，(B)添加蛋白酶，(C)添加淀粉酶和(D)添加蛋白酶和淀粉酶二者的器皿洗涤标准洗涤剂组合物(warewash model detergent composition)测试四种不同设置的清洁性能。每种设置测试十个盘。为了消除在每种设置之间转移有机材料的风险，将器皿洗涤器在每个清洁循环后清洗(关闭)并重新启动。在此过程期间，清洁器皿洗涤器的内表面。
洗涤试验中使用的洗涤剂组合物如表1中所定义制造。洗涤剂组合物是pH中性的，即酶友好的，并以2g/L洗涤液加入到器皿洗涤器中。在洗涤试验中，将酶(参见表2)添加到器皿洗涤器中，如所示。
表1：没有酶的器皿洗涤洗涤剂(图中称为NZ洗涤剂)的化学组成
| 组分 | 组成(wt.％) |
| 蒸馏水 | 56.00 |
| 碳酸钠(pH调节剂) | 2.18 |
| 碳酸氢钠(pH调节剂) | 3.62 |
| 1,2-丙二醇(溶剂) | 15.60 |
| 二甲苯磺酸钠40％(增溶剂) | 12.00 |
| Dissolvine GL38(螯合剂) | 8.60 |
| Bio-Soft N91-2.5(非离子表面活性剂) | 2.00 |
表2：洗涤试验中使用的酶
表2的蛋白酶与蛋白酶抑制剂Cbz-Gly-Ala-Tyr-H一起使用。
一旦洗涤盘后，根据测定I由受过训练的测试人员评估洗涤剂的性能。评估结果示于下表3-6和图1中。
图1：由10名受过训练的测试人员组成的测试小组评估所有盘相对于彼此的清洁度(测定I)。该图示出当将表2的淀粉酶和蛋白酶的酶混合物添加到器皿洗涤洗涤剂(表1)中时，存在显著的性能改善。当使用淀粉酶或蛋白酶洗涤盘时，清洁性能不显著。这表明存在高度的淀粉酶/蛋白酶协同作用。
实例2
盘上的器皿洗涤试验
燕麦粥污垢是通过将50克燕麦片加入到250ml的UHT(超高温处理的)牛奶(均质化的，1.5％脂肪)和750ml合成水(16.8°dH)中，在连续搅拌下稳定加热并煮沸10分钟而制备的。
使用刷子，将3g热燕麦粥均匀地涂抹在盘内表面上。盘的边缘保持没有。内盘直径为15cm。将弄脏的盘在热橱柜中在80℃下干燥2小时。当盘已经冷却至室温时，洗涤它们。
在以90秒清洁循环操作的霍巴特(Hobart)AUXX连帽式器皿洗涤器中在1个清洁循环期间洗涤用燕麦粥预先弄脏的盘，该清洁循环包括洗涤步骤(66秒(s)，60℃-65℃)，排出2.5l洗涤液(15s)，用2.5l清洁水漂洗(9s，85℃)以及干燥步骤(31s)。洗涤液的水硬度为0°dH。为了模拟真实生活中厨房中的条件，将压载污垢添加到器皿洗涤器的清洁循环中。在开始清洁循环之前，将1g/L洗涤液压载污垢添加到储槽中。
使用(A)Diversey Suma Ultra Pur-Eco L2(没有酶的商业高pH器皿洗涤洗涤剂)，(B)不同的没有酶的商业高pH器皿洗涤洗涤剂Novadan Bistro741，(C)不添加酶的温和pH的标准洗涤剂组合物和(D)添加蛋白酶和淀粉酶的标准洗涤剂组合物测试四种不同设置的清洁性能。每种设置测试十个盘。为了消除在每种设置之间转移有机材料的风险，将器皿洗涤器在每个清洁循环后清洗(关闭)并重新启动。在此过程期间，清洁器皿洗涤器的内表面。
洗涤试验中使用的洗涤剂组合物如表1中所定义制造。洗涤剂组合物是pH中性的，即酶友好的，并以2g/L洗涤液加入到器皿洗涤器中。在洗涤试验中，将酶(参见表2)添加到器皿洗涤器中，如所示。
器皿洗涤洗涤剂组合物的化学组成、所用的酶和酶的浓度与实例1中的相同并且示于表1和2中。
一旦洗涤盘后，根据测定I由受过训练的测试人员评估洗涤剂的性能。评估结果示于下表7中。由两名受过训练的测试人员组成的测试小组评估所有盘相对于彼此的清洁度(测定I)。图2示出了表10中数据的平均值。可以看出，与没有酶的温和pH洗涤剂(表1)的洗涤性能相比，当将表2的淀粉酶和蛋白酶的酶混合物添加到温和pH洗涤剂(表1)中时，存在洗涤性能的显著改善。下表7也显示出，与常规的高pH商业器皿洗涤洗涤剂相比，当使用温和pH洗涤剂(表1)时的显著的洗涤性能损失。然而，看出，通过向温和pH洗涤剂(表1)中添加蛋白酶和淀粉酶(表2)，可以降低清洁性能差距。
表7：由两名受过训练的测试人员组成的测试小组评估所有盘相对于彼此的清洁度(测定I)。
实例3
盘上的器皿洗涤试验
如实例1第一段所述制备燕麦粥污垢和预先弄脏的盘，其中修改是在燕麦粥煮沸10分钟后，使用手持搅拌器将燕麦粥充分混合约5分钟。
以与实例1第二段所述的相同洗涤程序在霍巴特AUXX连帽式器皿洗涤器中在1个清洁循环期间洗涤预先弄脏的盘。
使用(A)不添加酶，(B)添加淀粉酶和蛋白酶，(C)添加淀粉酶、蛋白酶和地衣多糖酶，(D)仅添加地衣多糖酶，(E)仅添加淀粉酶和(F)添加淀粉酶和地衣多糖酶的商业温和洗涤中pH的器皿洗涤洗涤剂来测试六种不同处理的清洁性能。每种处理测试六个盘。为了消除在每种设置之间转移有机材料的风险，将器皿洗涤器在每个清洁循环后清洗(关闭)并重新启动。在此过程期间，用自来水清洁器皿洗涤器的内表面。
使用的商业器皿洗涤洗涤剂组合物(韦格博士公司，neodisher BioClean)是不含磷酸盐且不含活性氯的液体浓缩物。该配制品被认为是无害的、无腐蚀性且无刺激性的。在本实验中，将洗涤剂组合物以2g/L洗涤液加入器皿洗涤器中，并且施用pH为中性的，即酶友好的。在洗涤试验中，将酶(参见表)添加到器皿洗涤器中，如所示。
表8：洗涤试验中使用的酶
一旦洗涤盘后，根据测定I由受过训练的测试人员评估洗涤剂的性能。评估结果示于下表9中。
受过训练的测试人员评估所有盘相对于彼此的清洁度(测定I)。从表中明显看出，与没有地衣多糖酶的类似处理(表1)相比，当用地衣多糖酶处理盘时存在小的性能改善。这表明通过添加地衣多糖酶的性能益处。
实例4
盘上的器皿洗涤试验
如实例1第一段所述制备燕麦粥污垢和预先弄脏的盘，其中修改是在燕麦粥煮沸10分钟后，使用手持搅拌器将燕麦粥充分混合约5分钟。
以与实例1第二段所述的相同洗涤程序在霍巴特AUXX连帽式器皿洗涤器中在1个清洁循环期间洗涤预先弄脏的盘。
使用(A)来自希悦尔泰华施公司(Sealed Air Diversey)的常规商业高pH器皿洗涤洗涤剂组合物Suma Ultra Pur-Eco L2，(B)来自韦格博士公司的商业温和洗涤中pH的器皿洗涤洗涤剂组合物Neodisher BioClean和(C)来自韦格博士公司的添加了蛋白酶和淀粉酶的Neodisher BioClean来测试三种不同处理的清洁性能。每种处理测试六个盘。为了消除在每种设置之间转移有机材料的风险，将器皿洗涤器在每个清洁循环后清洗(关闭)并重新启动。在此过程期间，清洁器皿洗涤器的内表面。
在实验中，将根据处理的适当的器皿洗涤洗涤剂以2g/L洗涤液加入到器皿洗涤器中。处理(A)的施用pH是高于11，并且对于处理(B)和(C)，施用pH为8.5，即酶友好的。在洗涤试验中，将酶(参见表10)添加到器皿洗涤器中，如所示。
表10：洗涤试验中使用的酶
一旦洗涤盘后，根据测定I由受过训练的测试人员评估洗涤剂的性能。评估结果示于下表11中。
受过训练的测试人员评估所有盘相对于彼此的清洁度(测定I)。显然，与没有蛋白酶和淀粉酶的类似处理相比，当添加蛋白酶和淀粉酶(表1)时，存在显著的性能改善。出人意料地，与常规的高pH器皿洗涤洗涤剂相比，与蛋白酶和淀粉酶组合(表11)的温和pH(8.5)的器皿洗涤洗涤剂的洗涤性能也显著改善。
实例5
盘上的器皿洗涤试验
通过分离新鲜的生有机蛋的蛋黄来制备蛋黄。将该蛋黄在烧杯中搅拌，并使用刷子1g±0.1g均匀地涂抹在盘内表面上。
盘的边缘保持没有。内盘直径为15cm。将弄脏的盘在室温下干燥至少4小时(h)并最多24小时。为了变性，将盘浸入沸腾的软化水中30秒。在将所有弄脏的盘煮沸后不久，将它们在热橱柜中在80℃下干燥30分钟。然后将盘在使用它们之前在室温下储存至少24h。
以与实例1第二段所述的相同洗涤程序在霍巴特AUXX连帽式器皿洗涤器中在1个清洁循环期间洗涤预先弄脏的盘。
使用(A)没有酶和(B)具有蛋白酶的来自希悦尔泰华施公司的常规商业高pH器皿洗涤洗涤剂组合物Suma Ultra Pur-Eco L2来测试两种不同处理的清洁性能。每种处理测试五个盘。为了消除在每种设置之间转移有机材料的风险，将器皿洗涤器在每个清洁循环后清洗(关闭)并重新启动。在此过程期间，清洁器皿洗涤器的内表面。
在实验中，将器皿洗涤洗涤剂以2g/L洗涤液加入到器皿洗涤器中。两种处理的施用pH均为11。在洗涤试验中，将蛋白酶(参见表12)添加到器皿洗涤器中，如所示。
表12：洗涤试验中使用的酶
| 酶 | 洗涤试验中使用的浓度 |
| 蛋白酶：SEQ ID NO:24 | 0.519mg酶蛋白/g洗涤液 |
一旦洗涤盘后，根据测定I由受过训练的测试人员评估洗涤剂的性能。评估结果示于下表中
受过训练的测试人员评估所有盘相对于彼此的清洁度(测定I)。该图示出了来自表13中示出的处理A和B的结果的平均分数。显然，与没有蛋白酶的类似处理相比，当添加蛋白酶(12)时，存在显著的性能改善。出人意料地，这表明蛋白酶在非常短的时间间隔内起作用，即使pH为11，并且常规的器皿洗涤洗涤剂通过添加蛋白酶实现对该蛋白特定污垢的性能改善。
序列表
<110> 诺维信公司（Novozymes A/S）
<120> 酶用于洗涤的用途、洗涤方法和器皿洗涤组合物
<130> 14282-WO-PCT
<160> 24
<170> PatentIn 版本 3.5
<210> 1
<211> 485
<212> PRT
<213> 芽孢杆菌属物种
<400> 1
His His Asn Gly Thr Asn Gly Thr Met Met Gln Tyr Phe Glu Trp Tyr
1 5 10 15
Leu Pro Asn Asp Gly Asn His Trp Asn Arg Leu Arg Ser Asp Ala Ser
20 25 30
Asn Leu Lys Asp Lys Gly Ile Ser Ala Val Trp Ile Pro Pro Ala Trp
35 40 45
Lys Gly Ala Ser Gln Asn Asp Val Gly Tyr Gly Ala Tyr Asp Leu Tyr
50 55 60
Asp Leu Gly Glu Phe Asn Gln Lys Gly Thr Ile Arg Thr Lys Tyr Gly
65 70 75 80
Thr Arg Asn Gln Leu Gln Ala Ala Val Asn Ala Leu Lys Ser Asn Gly
85 90 95
Ile Gln Val Tyr Gly Asp Val Val Met Asn His Lys Gly Gly Ala Asp
100 105 110
Ala Thr Glu Met Val Arg Ala Val Glu Val Asn Pro Asn Asn Arg Asn
115 120 125
Gln Glu Val Ser Gly Glu Tyr Thr Ile Glu Ala Trp Thr Lys Phe Asp
130 135 140
Phe Pro Gly Arg Gly Asn Thr His Ser Asn Phe Lys Trp Arg Trp Tyr
145 150 155 160
His Phe Asp Gly Val Asp Trp Asp Gln Ser Arg Lys Leu Asn Asn Arg
165 170 175
Ile Tyr Lys Phe Arg Gly Asp Gly Lys Gly Trp Asp Trp Glu Val Asp
180 185 190
Thr Glu Asn Gly Asn Tyr Asp Tyr Leu Met Tyr Ala Asp Ile Asp Met
195 200 205
Asp His Pro Glu Val Val Asn Glu Leu Arg Asn Trp Gly Val Trp Tyr
210 215 220
Thr Asn Thr Leu Gly Leu Asp Gly Phe Arg Ile Asp Ala Val Lys His
225 230 235 240
Ile Lys Tyr Ser Phe Thr Arg Asp Trp Ile Asn His Val Arg Ser Ala
245 250 255
Thr Gly Lys Asn Met Phe Ala Val Ala Glu Phe Trp Lys Asn Asp Leu
260 265 270
Gly Ala Ile Glu Asn Tyr Leu Asn Lys Thr Asn Trp Asn His Ser Val
275 280 285
Phe Asp Val Pro Leu His Tyr Asn Leu Tyr Asn Ala Ser Lys Ser Gly
290 295 300
Gly Asn Tyr Asp Met Arg Gln Ile Phe Asn Gly Thr Val Val Gln Arg
305 310 315 320
His Pro Met His Ala Val Thr Phe Val Asp Asn His Asp Ser Gln Pro
325 330 335
Glu Glu Ala Leu Glu Ser Phe Val Glu Glu Trp Phe Lys Pro Leu Ala
340 345 350
Tyr Ala Leu Thr Leu Thr Arg Glu Gln Gly Tyr Pro Ser Val Phe Tyr
355 360 365
Gly Asp Tyr Tyr Gly Ile Pro Thr His Gly Val Pro Ala Met Lys Ser
370 375 380
Lys Ile Asp Pro Ile Leu Glu Ala Arg Gln Lys Tyr Ala Tyr Gly Arg
385 390 395 400
Gln Asn Asp Tyr Leu Asp His His Asn Ile Ile Gly Trp Thr Arg Glu
405 410 415
Gly Asn Thr Ala His Pro Asn Ser Gly Leu Ala Thr Ile Met Ser Asp
420 425 430
Gly Ala Gly Gly Asn Lys Trp Met Phe Val Gly Arg Asn Lys Ala Gly
435 440 445
Gln Val Trp Thr Asp Ile Thr Gly Asn Arg Ala Gly Thr Val Thr Ile
450 455 460
Asn Ala Asp Gly Trp Gly Asn Phe Ser Val Asn Gly Gly Ser Val Ser
465 470 475 480
Ile Trp Val Asn Lys
485
<210> 2
<211> 485
<212> PRT
<213> 盐敏芽孢杆菌
<400> 2
His His Asn Gly Thr Asn Gly Thr Met Met Gln Tyr Phe Glu Trp His
1 5 10 15
Leu Pro Asn Asp Gly Asn His Trp Asn Arg Leu Arg Asp Asp Ala Ser
20 25 30
Asn Leu Arg Asn Arg Gly Ile Thr Ala Ile Trp Ile Pro Pro Ala Trp
35 40 45
Lys Gly Thr Ser Gln Asn Asp Val Gly Tyr Gly Ala Tyr Asp Leu Tyr
50 55 60
Asp Leu Gly Glu Phe Asn Gln Lys Gly Thr Val Arg Thr Lys Tyr Gly
65 70 75 80
Thr Arg Ser Gln Leu Glu Ser Ala Ile His Ala Leu Lys Asn Asn Gly
85 90 95
Val Gln Val Tyr Gly Asp Val Val Met Asn His Lys Gly Gly Ala Asp
100 105 110
Ala Thr Glu Asn Val Leu Ala Val Glu Val Asn Pro Asn Asn Arg Asn
115 120 125
Gln Glu Ile Ser Gly Asp Tyr Thr Ile Glu Ala Trp Thr Lys Phe Asp
130 135 140
Phe Pro Gly Arg Gly Asn Thr Tyr Ser Asp Phe Lys Trp Arg Trp Tyr
145 150 155 160
His Phe Asp Gly Val Asp Trp Asp Gln Ser Arg Gln Phe Gln Asn Arg
165 170 175
Ile Tyr Lys Phe Arg Gly Asp Gly Lys Ala Trp Asp Trp Glu Val Asp
180 185 190
Ser Glu Asn Gly Asn Tyr Asp Tyr Leu Met Tyr Ala Asp Val Asp Met
195 200 205
Asp His Pro Glu Val Val Asn Glu Leu Arg Arg Trp Gly Glu Trp Tyr
210 215 220
Thr Asn Thr Leu Asn Leu Asp Gly Phe Arg Ile Asp Ala Val Lys His
225 230 235 240
Ile Lys Tyr Ser Phe Thr Arg Asp Trp Leu Thr His Val Arg Asn Ala
245 250 255
Thr Gly Lys Glu Met Phe Ala Val Ala Glu Phe Trp Lys Asn Asp Leu
260 265 270
Gly Ala Leu Glu Asn Tyr Leu Asn Lys Thr Asn Trp Asn His Ser Val
275 280 285
Phe Asp Val Pro Leu His Tyr Asn Leu Tyr Asn Ala Ser Asn Ser Gly
290 295 300
Gly Asn Tyr Asp Met Ala Lys Leu Leu Asn Gly Thr Val Val Gln Lys
305 310 315 320
His Pro Met His Ala Val Thr Phe Val Asp Asn His Asp Ser Gln Pro
325 330 335
Gly Glu Ser Leu Glu Ser Phe Val Gln Glu Trp Phe Lys Pro Leu Ala
340 345 350
Tyr Ala Leu Ile Leu Thr Arg Glu Gln Gly Tyr Pro Ser Val Phe Tyr
355 360 365
Gly Asp Tyr Tyr Gly Ile Pro Thr His Ser Val Pro Ala Met Lys Ala
370 375 380
Lys Ile Asp Pro Ile Leu Glu Ala Arg Gln Asn Phe Ala Tyr Gly Thr
385 390 395 400
Gln His Asp Tyr Phe Asp His His Asn Ile Ile Gly Trp Thr Arg Glu
405 410 415
Gly Asn Thr Thr His Pro Asn Ser Gly Leu Ala Thr Ile Met Ser Asp
420 425 430
Gly Pro Gly Gly Glu Lys Trp Met Tyr Val Gly Gln Asn Lys Ala Gly
435 440 445
Gln Val Trp His Asp Ile Thr Gly Asn Lys Pro Gly Thr Val Thr Ile
450 455 460
Asn Ala Asp Gly Trp Ala Asn Phe Ser Val Asn Gly Gly Ser Val Ser
465 470 475 480
Ile Trp Val Lys Arg
485
<210> 3
<211> 483
<212> PRT
<213> 地衣芽孢杆菌
<400> 3
Ala Asn Leu Asn Gly Thr Leu Met Gln Tyr Phe Glu Trp Tyr Met Pro
1 5 10 15
Asn Asp Gly Gln His Trp Arg Arg Leu Gln Asn Asp Ser Ala Tyr Leu
20 25 30
Ala Glu His Gly Ile Thr Ala Val Trp Ile Pro Pro Ala Tyr Lys Gly
35 40 45
Thr Ser Gln Ala Asp Val Gly Tyr Gly Ala Tyr Asp Leu Tyr Asp Leu
50 55 60
Gly Glu Phe His Gln Lys Gly Thr Val Arg Thr Lys Tyr Gly Thr Lys
65 70 75 80
Gly Glu Leu Gln Ser Ala Ile Lys Ser Leu His Ser Arg Asp Ile Asn
85 90 95
Val Tyr Gly Asp Val Val Ile Asn His Lys Gly Gly Ala Asp Ala Thr
100 105 110
Glu Asp Val Thr Ala Val Glu Val Asp Pro Ala Asp Arg Asn Arg Val
115 120 125
Ile Ser Gly Glu His Leu Ile Lys Ala Trp Thr His Phe His Phe Pro
130 135 140
Gly Arg Gly Ser Thr Tyr Ser Asp Phe Lys Trp His Trp Tyr His Phe
145 150 155 160
Asp Gly Thr Asp Trp Asp Glu Ser Arg Lys Leu Asn Arg Ile Tyr Lys
165 170 175
Phe Gln Gly Lys Ala Trp Asp Trp Glu Val Ser Asn Glu Asn Gly Asn
180 185 190
Tyr Asp Tyr Leu Met Tyr Ala Asp Ile Asp Tyr Asp His Pro Asp Val
195 200 205
Ala Ala Glu Ile Lys Arg Trp Gly Thr Trp Tyr Ala Asn Glu Leu Gln
210 215 220
Leu Asp Gly Phe Arg Leu Asp Ala Val Lys His Ile Lys Phe Ser Phe
225 230 235 240
Leu Arg Asp Trp Val Asn His Val Arg Glu Lys Thr Gly Lys Glu Met
245 250 255
Phe Thr Val Ala Glu Tyr Trp Gln Asn Asp Leu Gly Ala Leu Glu Asn
260 265 270
Tyr Leu Asn Lys Thr Asn Phe Asn His Ser Val Phe Asp Val Pro Leu
275 280 285
His Tyr Gln Phe His Ala Ala Ser Thr Gln Gly Gly Gly Tyr Asp Met
290 295 300
Arg Lys Leu Leu Asn Gly Thr Val Val Ser Lys His Pro Leu Lys Ser
305 310 315 320
Val Thr Phe Val Asp Asn His Asp Thr Gln Pro Gly Gln Ser Leu Glu
325 330 335
Ser Thr Val Gln Thr Trp Phe Lys Pro Leu Ala Tyr Ala Phe Ile Leu
340 345 350
Thr Arg Glu Ser Gly Tyr Pro Gln Val Phe Tyr Gly Asp Met Tyr Gly
355 360 365
Thr Lys Gly Asp Ser Gln Arg Glu Ile Pro Ala Leu Lys His Lys Ile
370 375 380
Glu Pro Ile Leu Lys Ala Arg Lys Gln Tyr Ala Tyr Gly Ala Gln His
385 390 395 400
Asp Tyr Phe Asp His His Asp Ile Val Gly Trp Thr Arg Glu Gly Asp
405 410 415
Ser Ser Val Ala Asn Ser Gly Leu Ala Ala Leu Ile Thr Asp Gly Pro
420 425 430
Gly Gly Ala Lys Arg Met Tyr Val Gly Arg Gln Asn Ala Gly Glu Thr
435 440 445
Trp His Asp Ile Thr Gly Asn Arg Ser Glu Pro Val Val Ile Asn Ser
450 455 460
Glu Gly Trp Gly Glu Phe His Val Asn Gly Gly Ser Val Ser Ile Tyr
465 470 475 480
Val Gln Arg
<210> 4
<211> 481
<212> PRT
<213> 融合蛋白
<400> 4
Val Asn Gly Thr Leu Met Gln Tyr Phe Glu Trp Tyr Thr Pro Asn Asp
1 5 10 15
Gly Gln His Trp Lys Arg Leu Gln Asn Asp Ala Glu His Leu Ser Asp
20 25 30
Ile Gly Ile Thr Ala Val Trp Ile Pro Pro Ala Tyr Lys Gly Thr Ser
35 40 45
Gln Ala Asp Val Gly Tyr Gly Ala Tyr Asp Leu Tyr Asp Leu Gly Glu
50 55 60
Phe His Gln Lys Gly Thr Val Arg Thr Lys Tyr Gly Thr Lys Gly Glu
65 70 75 80
Leu Gln Ser Ala Ile Lys Ser Leu His Ser Arg Asp Ile Asn Val Tyr
85 90 95
Gly Asp Val Val Ile Asn His Lys Gly Gly Ala Asp Ala Thr Glu Asp
100 105 110
Val Thr Ala Val Glu Val Asp Pro Ala Asp Arg Asn Arg Val Ile Ser
115 120 125
Gly Glu His Leu Ile Lys Ala Trp Thr His Phe His Phe Pro Gly Arg
130 135 140
Gly Ser Thr Tyr Ser Asp Phe Lys Trp His Trp Tyr His Phe Asp Gly
145 150 155 160
Thr Asp Trp Asp Glu Ser Arg Lys Leu Asn Arg Ile Tyr Lys Phe Gln
165 170 175
Gly Lys Ala Trp Asp Trp Glu Val Ser Asn Glu Asn Gly Asn Tyr Asp
180 185 190
Tyr Leu Met Tyr Ala Asp Ile Asp Tyr Asp His Pro Asp Val Ala Ala
195 200 205
Glu Ile Lys Arg Trp Gly Thr Trp Tyr Ala Asn Glu Leu Gln Leu Asp
210 215 220
Gly Phe Arg Leu Asp Ala Val Lys His Ile Lys Phe Ser Phe Leu Arg
225 230 235 240
Asp Trp Val Asn His Val Arg Glu Lys Thr Gly Lys Glu Met Phe Thr
245 250 255
Val Ala Glu Tyr Trp Gln Asn Asp Leu Gly Ala Leu Glu Asn Tyr Leu
260 265 270
Asn Lys Thr Asn Phe Asn His Ser Val Phe Asp Val Pro Leu His Tyr
275 280 285
Gln Phe His Ala Ala Ser Thr Gln Gly Gly Gly Tyr Asp Met Arg Lys
290 295 300
Leu Leu Asn Gly Thr Val Val Ser Lys His Pro Leu Lys Ser Val Thr
305 310 315 320
Phe Val Asp Asn His Asp Thr Gln Pro Gly Gln Ser Leu Glu Ser Thr
325 330 335
Val Gln Thr Trp Phe Lys Pro Leu Ala Tyr Ala Phe Ile Leu Thr Arg
340 345 350
Glu Ser Gly Tyr Pro Gln Val Phe Tyr Gly Asp Met Tyr Gly Thr Lys
355 360 365
Gly Asp Ser Gln Arg Glu Ile Pro Ala Leu Lys His Lys Ile Glu Pro
370 375 380
Ile Leu Lys Ala Arg Lys Gln Tyr Ala Tyr Gly Ala Gln His Asp Tyr
385 390 395 400
Phe Asp His His Asp Ile Val Gly Trp Thr Arg Glu Gly Asp Ser Ser
405 410 415
Val Ala Asn Ser Gly Leu Ala Ala Leu Ile Thr Asp Gly Pro Gly Gly
420 425 430
Ala Lys Arg Met Tyr Val Gly Arg Gln Asn Ala Gly Glu Thr Trp His
435 440 445
Asp Ile Thr Gly Asn Arg Ser Glu Pro Val Val Ile Asn Ser Glu Gly
450 455 460
Trp Gly Glu Phe His Val Asn Gly Gly Ser Val Ser Ile Tyr Val Gln
465 470 475 480
Arg
<210> 5
<211> 269
<212> PRT
<213> 迟缓芽孢杆菌
<400> 5
Ala Gln Ser Val Pro Trp Gly Ile Ser Arg Val Gln Ala Pro Ala Ala
1 5 10 15
His Asn Arg Gly Leu Thr Gly Ser Gly Val Lys Val Ala Val Leu Asp
20 25 30
Thr Gly Ile Ser Thr His Pro Asp Leu Asn Ile Arg Gly Gly Ala Ser
35 40 45
Phe Val Pro Gly Glu Pro Ser Thr Gln Asp Gly Asn Gly His Gly Thr
50 55 60
His Val Ala Gly Thr Ile Ala Ala Leu Asn Asn Ser Ile Gly Val Leu
65 70 75 80
Gly Val Ala Pro Ser Ala Glu Leu Tyr Ala Val Lys Val Leu Gly Ala
85 90 95
Ser Gly Ser Gly Ser Val Ser Ser Ile Ala Gln Gly Leu Glu Trp Ala
100 105 110
Gly Asn Asn Gly Met His Val Ala Asn Leu Ser Leu Gly Ser Pro Ser
115 120 125
Pro Ser Ala Thr Leu Glu Gln Ala Val Asn Ser Ala Thr Ser Arg Gly
130 135 140
Val Leu Val Val Ala Ala Ser Gly Asn Ser Gly Ala Gly Ser Ile Ser
145 150 155 160
Tyr Pro Ala Arg Tyr Ala Asn Ala Met Ala Val Gly Ala Thr Asp Gln
165 170 175
Asn Asn Asn Arg Ala Ser Phe Ser Gln Tyr Gly Ala Gly Leu Asp Ile
180 185 190
Val Ala Pro Gly Val Asn Val Gln Ser Thr Tyr Pro Gly Ser Thr Tyr
195 200 205
Ala Ser Leu Asn Gly Thr Ser Met Ala Thr Pro His Val Ala Gly Ala
210 215 220
Ala Ala Leu Val Lys Gln Lys Asn Pro Ser Trp Ser Asn Val Gln Ile
225 230 235 240
Arg Asn His Leu Lys Asn Thr Ala Thr Ser Leu Gly Ser Thr Asn Leu
245 250 255
Tyr Gly Ser Gly Leu Val Asn Ala Glu Ala Ala Thr Arg
260 265
<210> 6
<211> 274
<212> PRT
<213> 地衣芽孢杆菌
<400> 6
Ala Gln Thr Val Pro Tyr Gly Ile Pro Leu Ile Lys Ala Asp Lys Val
1 5 10 15
Gln Ala Gln Gly Phe Lys Gly Ala Asn Val Lys Val Ala Val Leu Asp
20 25 30
Thr Gly Ile Gln Ala Ser His Pro Asp Leu Asn Val Val Gly Gly Ala
35 40 45
Ser Phe Val Ala Gly Glu Ala Tyr Asn Thr Asp Gly Asn Gly His Gly
50 55 60
Thr His Val Ala Gly Thr Val Ala Ala Leu Asp Asn Thr Thr Gly Val
65 70 75 80
Leu Gly Val Ala Pro Ser Val Ser Leu Tyr Ala Val Lys Val Leu Asn
85 90 95
Ser Ser Gly Ser Gly Ser Tyr Ser Gly Ile Val Ser Gly Ile Glu Trp
100 105 110
Ala Thr Thr Asn Gly Met Asp Val Ile Asn Met Ser Leu Gly Gly Ala
115 120 125
Ser Gly Ser Thr Ala Met Lys Gln Ala Val Asp Asn Ala Tyr Ala Arg
130 135 140
Gly Val Val Val Val Ala Ala Ala Gly Asn Ser Gly Ser Ser Gly Asn
145 150 155 160
Thr Asn Thr Ile Gly Tyr Pro Ala Lys Tyr Asp Ser Val Ile Ala Val
165 170 175
Gly Ala Val Asp Ser Asn Ser Asn Arg Ala Ser Phe Ser Ser Val Gly
180 185 190
Ala Glu Leu Glu Val Met Ala Pro Gly Ala Gly Val Tyr Ser Thr Tyr
195 200 205
Pro Thr Asn Thr Tyr Ala Thr Leu Asn Gly Thr Ser Met Ala Ser Pro
210 215 220
His Val Ala Gly Ala Ala Ala Leu Ile Leu Ser Lys His Pro Asn Leu
225 230 235 240
Ser Ala Ser Gln Val Arg Asn Arg Leu Ser Ser Thr Ala Thr Tyr Leu
245 250 255
Gly Ser Ser Phe Tyr Tyr Gly Lys Gly Leu Ile Asn Val Glu Ala Ala
260 265 270
Ala Gln
<210> 7
<211> 268
<212> PRT
<213> 耐盐芽孢杆菌
<400> 7
Gln Thr Val Pro Trp Gly Ile Ser Phe Ile Asn Thr Gln Gln Ala His
1 5 10 15
Asn Arg Gly Ile Phe Gly Asn Gly Ala Arg Val Ala Val Leu Asp Thr
20 25 30
Gly Ile Ala Ser His Pro Asp Leu Arg Ile Ala Gly Gly Ala Ser Phe
35 40 45
Ile Ser Ser Glu Pro Ser Tyr His Asp Asn Asn Gly His Gly Thr His
50 55 60
Val Ala Gly Thr Ile Ala Ala Leu Asn Asn Ser Ile Gly Val Leu Gly
65 70 75 80
Val Ala Pro Ser Ala Asp Leu Tyr Ala Val Lys Val Leu Asp Arg Asn
85 90 95
Gly Ser Gly Ser Leu Ala Ser Val Ala Gln Gly Ile Glu Trp Ala Ile
100 105 110
Asn Asn Asn Met His Ile Ile Asn Met Ser Leu Gly Ser Thr Ser Gly
115 120 125
Ser Ser Thr Leu Glu Leu Ala Val Asn Arg Ala Asn Asn Ala Gly Ile
130 135 140
Leu Leu Val Gly Ala Ala Gly Asn Thr Gly Arg Gln Gly Val Asn Tyr
145 150 155 160
Pro Ala Arg Tyr Ser Gly Val Met Ala Val Ala Ala Val Asp Gln Asn
165 170 175
Gly Gln Arg Ala Ser Phe Ser Thr Tyr Gly Pro Glu Ile Glu Ile Ser
180 185 190
Ala Pro Gly Val Asn Val Asn Ser Thr Tyr Thr Gly Asn Arg Tyr Val
195 200 205
Ser Leu Ser Gly Thr Ser Met Ala Thr Pro His Val Ala Gly Val Ala
210 215 220
Ala Leu Val Lys Ser Arg Tyr Pro Ser Tyr Thr Asn Asn Gln Ile Arg
225 230 235 240
Gln Arg Ile Asn Gln Thr Ala Thr Tyr Leu Gly Ser Pro Ser Leu Tyr
245 250 255
Gly Asn Gly Leu Val His Ala Gly Arg Ala Thr Gln
260 265
<210> 8
<211> 275
<212> PRT
<213> 解淀粉芽孢杆菌
<400> 8
Ala Gln Ser Val Pro Tyr Gly Val Ser Gln Ile Lys Ala Pro Ala Leu
1 5 10 15
His Ser Gln Gly Tyr Thr Gly Ser Asn Val Lys Val Ala Val Ile Asp
20 25 30
Ser Gly Ile Asp Ser Ser His Pro Asp Leu Lys Val Ala Gly Gly Ala
35 40 45
Ser Met Val Pro Ser Glu Thr Asn Pro Phe Gln Asp Asn Asn Ser His
50 55 60
Gly Thr His Val Ala Gly Thr Val Ala Ala Leu Asn Asn Ser Ile Gly
65 70 75 80
Val Leu Gly Val Ala Pro Ser Ala Ser Leu Tyr Ala Val Lys Val Leu
85 90 95
Gly Ala Asp Gly Ser Gly Gln Tyr Ser Trp Ile Ile Asn Gly Ile Glu
100 105 110
Trp Ala Ile Ala Asn Asn Met Asp Val Ile Asn Met Ser Leu Gly Gly
115 120 125
Pro Ser Gly Ser Ala Ala Leu Lys Ala Ala Val Asp Lys Ala Val Ala
130 135 140
Ser Gly Val Val Val Val Ala Ala Ala Gly Asn Glu Gly Thr Ser Gly
145 150 155 160
Ser Ser Ser Thr Val Gly Tyr Pro Gly Lys Tyr Pro Ser Val Ile Ala
165 170 175
Val Gly Ala Val Asp Ser Ser Asn Gln Arg Ala Ser Phe Ser Ser Val
180 185 190
Gly Pro Glu Leu Asp Val Met Ala Pro Gly Val Ser Ile Gln Ser Thr
195 200 205
Leu Pro Gly Asn Lys Tyr Gly Ala Tyr Asn Gly Thr Ser Met Ala Ser
210 215 220
Pro His Val Ala Gly Ala Ala Ala Leu Ile Leu Ser Lys His Pro Asn
225 230 235 240
Trp Thr Asn Thr Gln Val Arg Ser Ser Leu Glu Asn Thr Thr Thr Lys
245 250 255
Leu Gly Asp Ser Phe Tyr Tyr Gly Lys Gly Leu Ile Asn Val Gln Ala
260 265 270
Ala Ala Gln
275
<210> 9
<211> 4
<212> PRT
<213> 人工
<220>
<223> 枯草杆菌蛋白酶抑制剂
<220>
<221> 尚未归类的特征
<222> (1)..(1)
<223> 乙酰基-苯丙氨酸
<220>
<221> 尚未归类的特征
<222> (4)..(4)
<223> Tyr-H
<400> 9
Phe Gly Ala Tyr
1
<210> 10
<211> 4
<212> PRT
<213> 人工
<220>
<223> 枯草杆菌蛋白酶抑制剂
<220>
<221> 尚未归类的特征
<222> (1)..(1)
<223> 乙酰基-亮氨酸
<220>
<221> 尚未归类的特征
<222> (4)..(4)
<223> Tyr-H
<400> 10
Leu Gly Ala Tyr
1
<210> 11
<211> 4
<212> PRT
<213> 人工
<220>
<223> 枯草杆菌蛋白酶抑制剂
<220>
<221> 尚未归类的特征
<222> (1)..(1)
<223> 乙酰基-酪氨酸
<220>
<221> 尚未归类的特征
<222> (4)..(4)
<223> Tyr-H
<400> 11
Tyr Gly Ala Tyr
1
<210> 12
<211> 4
<212> PRT
<213> 人工
<220>
<223> 枯草杆菌蛋白酶抑制剂
<220>
<221> 尚未归类的特征
<222> (1)..(1)
<223> 乙酰基-苯丙氨酸；MeO-CO-Phe；MeSO2-Phe；或EtSO2-Phe
<220>
<221> 尚未归类的特征
<222> (4)..(4)
<223> Leu-H
<400> 12
Phe Gly Ala Leu
1
<210> 13
<211> 4
<212> PRT
<213> 人工
<220>
<223> 枯草杆菌蛋白酶抑制剂
<220>
<221> 尚未归类的特征
<222> (1)..(1)
<223> 乙酰基-苯丙氨酸或MeO-CO-Phe
<220>
<221> 尚未归类的特征
<222> (4)..(4)
<223> Tyr-H
<400> 13
Phe Gly Ala Phe
1
<210> 14
<211> 4
<212> PRT
<213> 人工
<220>
<223> 枯草杆菌蛋白酶抑制剂
<220>
<221> 尚未归类的特征
<222> (1)..(1)
<223> 乙酰基-苯丙氨酸
<220>
<221> 尚未归类的特征
<222> (4)..(4)
<223> Tyr-H
<400> 14
Phe Gly Val Tyr
1
<210> 15
<211> 4
<212> PRT
<213> 人工
<220>
<223> 枯草杆菌蛋白酶抑制剂
<220>
<221> 尚未归类的特征
<222> (1)..(1)
<223> 乙酰基-苯丙氨酸
<220>
<221> 尚未归类的特征
<222> (4)..(4)
<223> Met-H
<400> 15
Phe Gly Ala Met
1
<210> 16
<211> 4
<212> PRT
<213> 人工
<220>
<223> 枯草杆菌蛋白酶抑制剂
<220>
<221> 尚未归类的特征
<222> (1)..(1)
<223> 乙酰基-色氨酸
<220>
<221> 尚未归类的特征
<222> (4)..(4)
<223> Tyr-H
<400> 16
Trp Leu Val Tyr
1
<210> 17
<211> 4
<212> PRT
<213> 人工
<220>
<223> 枯草杆菌蛋白酶抑制剂
<220>
<221> 尚未归类的特征
<222> (1)..(1)
<223> MeO-P(OH)(O)-Leu
<220>
<221> 尚未归类的特征
<222> (4)..(4)
<223> Leu-H
<400> 17
Leu Gly Ala Leu
1
<210> 18
<211> 237
<212> PRT
<213> 粘琼脂芽孢杆菌
<400> 18
Met Leu Thr Leu Leu Met Met Ser Phe Ala Gly Ala Ala Tyr Ala His
1 5 10 15
Asn Pro Val Thr Asp Glu Glu Val Tyr His Ser Phe Asn Ser His Asp
20 25 30
Trp Gln Asn Trp Asn Met Ser Asp Gly Trp Lys Asn Asp Asp Tyr Phe
35 40 45
Phe Gly Cys His Trp Ser Gln Asn Arg Val Asn Phe Tyr Gly Gly Gln
50 55 60
Met Glu Leu Ser Leu Arg Thr Asn Tyr Ser Tyr Ala Pro Pro Tyr Asn
65 70 75 80
Tyr Glu Cys Ala Glu Tyr Thr Thr Asn Asn Phe Tyr Gly Tyr Gly Leu
85 90 95
Tyr Glu Val Ser Met Lys Pro Ala Lys Val Ser Gly Val Ile Ser Ser
100 105 110
Phe Phe Thr Tyr Thr Gly Pro Ser Tyr Asn Gly Ala Pro Trp Asp Glu
115 120 125
Ile Asp Ile Glu Phe Leu Gly Asn Asp Thr Thr Lys Val Gln Phe Asn
130 135 140
Tyr Tyr Thr Asp Gly Val Gly Gly Asn Glu Ile Leu Tyr Asp Leu Gly
145 150 155 160
Phe Asp Ala Ala Asp Ser Tyr Asn Thr Tyr Ala Phe Asp Trp Gln Glu
165 170 175
Asn Tyr Ile Asn Trp Tyr Val Asn Gly Gln Leu Val Ala Thr Ala Thr
180 185 190
Glu Asn Ile Pro Ser Asn Pro Ser Lys Ile Met Met Asn Ile Trp Asn
195 200 205
Thr Tyr Gly Ile Asp Glu Trp Ala Gly Arg Tyr Tyr Gly Glu Asp Ala
210 215 220
Asn Ala Ser Tyr Asn Trp Val Arg Tyr Thr Pro Asn Arg
225 230 235
<210> 19
<211> 379
<212> PRT
<213> 芽孢杆菌属物种-62449
<400> 19
Val Val Lys Ile Lys Ile Asn Asn Ser Ile Arg Ile Val Met Leu Thr
1 5 10 15
Leu Ile Met Met Ser Val Ser Val Val Ala Tyr Ala Tyr Asn Pro Val
20 25 30
Thr Glu Asp Glu Leu Tyr His Ser Phe Asp Ser His Asp Ala Arg Asn
35 40 45
Trp Gln Ile Ser Asp Gly Trp Arg Asn Gly Asp Asp Phe Phe Gly Cys
50 55 60
His Trp Ser Gln Asn Arg Val Asn Phe Asn Arg Gly Glu Met Glu Leu
65 70 75 80
Ser Leu Arg Thr Asn Tyr Ser Tyr Ser Ala Pro Tyr Asn Tyr Glu Cys
85 90 95
Ala Glu Tyr Ala Thr Ser Asn Phe Tyr Gly Tyr Gly Leu Tyr Glu Val
100 105 110
Ser Met Lys Pro Ala Asn Val Ser Gly Val Ile Ser Ser Phe Phe Thr
115 120 125
Tyr Thr Gly Pro Ser Tyr Asn Gly Ala Pro Trp Asp Glu Ile Asp Ile
130 135 140
Glu Phe Leu Gly Asn Asp Thr Thr Lys Val Gln Phe Asn Tyr Tyr Thr
145 150 155 160
Asn Gly Val Gly Gly Asn Glu Ile Ile Tyr Asp Leu Gly Phe Asp Ala
165 170 175
Ala Asn Ser Phe Asn Thr Tyr Ala Phe Asp Trp Gln Glu Asn Tyr Ile
180 185 190
Ser Trp Tyr Val Asn Gly Asn Leu Val Ala Thr Ala Thr Glu Asn Ile
195 200 205
Pro Ser Asn Pro Ser Lys Ile Met Met Asn Val Trp Asn Thr Tyr Gly
210 215 220
Ile Asp Glu Trp Ala Gly Ala Tyr Gly Gly Glu Ala Ala Asn Ala Thr
225 230 235 240
Tyr Glu Trp Val Arg Tyr Thr Pro Asn Asn Gly Asn Thr Thr Pro Ser
245 250 255
Thr Ala Pro Asp Phe Gln Leu Gln Ala Cys Asp Tyr Ser Asp Ser Ser
260 265 270
Gly Ile Thr Ser Trp Ser Cys Gly Val Gly Thr Phe His Ser Ser Asn
275 280 285
Trp Ile Lys Phe Asp Ser Val Asp Leu Ser Thr Gly Tyr Asn Ala Phe
290 295 300
Ala Val Ser Tyr Thr Ser Pro Gly Ser Gly Ser Phe Asp Ile Arg Leu
305 310 315 320
Gly Ser Pro His Gly Gln Arg Ile Gly Thr Val Asn Tyr Gly Ala Thr
325 330 335
Gly Gly Trp Ser Asn Tyr Glu Trp Ser Gly Thr Pro Ser Leu Asp Val
340 345 350
Thr Val Arg Gly Ala His Asp Ile Tyr Ile Val Ala Thr Ser Gly Ala
355 360 365
Ala Asn Leu Arg Glu Phe Trp Phe Lys Asn Glu
370 375
<210> 20
<211> 379
<212> PRT
<213> 芽孢杆菌属物种-62449
<400> 20
Met Val Lys Ile Lys Ile Asn Asn Ser Ile Arg Ile Val Met Leu Thr
1 5 10 15
Leu Ile Met Met Ser Val Ser Val Val Ala Tyr Ala Tyr Asn Pro Val
20 25 30
Thr Glu Asp Glu Leu Tyr His Ser Phe Asp Ser His Asp Ala Arg Asn
35 40 45
Trp Gln Ile Ser Asp Gly Trp Arg Asn Gly Asp Asp Phe Phe Gly Cys
50 55 60
His Trp Ser Gln Asn Arg Val Asn Phe Asn Arg Gly Glu Met Glu Leu
65 70 75 80
Ser Leu Arg Thr Asn Tyr Ser Tyr Ser Ala Pro Tyr Asn Tyr Glu Cys
85 90 95
Ala Glu Tyr Ala Thr Ser Asn Phe Tyr Gly Tyr Gly Leu Tyr Glu Val
100 105 110
Ser Met Lys Pro Ala Asn Val Ser Gly Val Ile Ser Ser Phe Phe Thr
115 120 125
Tyr Thr Gly Pro Ser Tyr Asn Gly Ala Pro Trp Asp Glu Ile Asp Ile
130 135 140
Glu Phe Leu Gly Asn Asp Thr Thr Lys Val Gln Phe Asn Tyr Tyr Thr
145 150 155 160
Asn Gly Val Gly Gly Asn Glu Ile Ile Tyr Asp Leu Gly Phe Asp Ala
165 170 175
Ala Asn Ser Phe Asn Thr Tyr Ala Phe Asp Trp Gln Glu Asn Tyr Ile
180 185 190
Ser Trp Tyr Val Asn Gly Asn Leu Val Ala Thr Ala Thr Glu Asn Ile
195 200 205
Pro Ser Asn Pro Ser Lys Ile Met Met Asn Val Trp Asn Thr Tyr Gly
210 215 220
Ile Asp Glu Trp Ala Gly Ala Tyr Gly Gly Glu Ala Ala Asn Ala Thr
225 230 235 240
Tyr Glu Trp Val Arg Tyr Thr Pro Asn Asn Gly Asn Thr Thr Pro Ser
245 250 255
Thr Ala Pro Asp Phe Gln Leu Gln Ala Cys Asp Tyr Ser Asp Ser Ser
260 265 270
Gly Ile Thr Ser Trp Ser Cys Gly Val Gly Thr Phe His Ser Ser Asn
275 280 285
Trp Ile Lys Phe Asp Ser Val Asp Leu Ser Thr Gly Tyr Asn Ala Phe
290 295 300
Ala Val Ser Tyr Thr Ser Pro Gly Ser Gly Ser Phe Asp Ile Arg Leu
305 310 315 320
Gly Ser Pro His Gly Gln Arg Ile Gly Thr Val Asn Tyr Gly Ala Thr
325 330 335
Gly Gly Trp Ser Asn Tyr Glu Trp Ser Gly Thr Pro Ser Leu Asp Val
340 345 350
Thr Val Arg Gly Ala His Asp Ile Tyr Ile Val Ala Thr Ser Gly Ala
355 360 365
Ala Asn Leu Arg Glu Phe Trp Phe Lys Asn Glu
370 375
<210> 21
<211> 276
<212> PRT
<213> 秋叶氏芽孢杆菌
<400> 21
Met Lys Lys Lys Phe Val Leu Phe Ser Met Cys Leu Leu Leu Phe Ser
1 5 10 15
Gly Leu Ile Thr Gly Leu Val Gln Ser Pro Gln Val Ala Glu Ala Ala
20 25 30
Glu Arg Pro Ile Gly Thr Thr Phe Val Glu Thr Phe Glu Ser Tyr Asp
35 40 45
Ser Glu Arg Trp Ser Lys Ala Gly Val Trp Thr Asn Gly Gln Met Phe
50 55 60
Asn Ala Thr Trp Tyr Pro Glu Gln Val Thr Phe Ser Asp Gly Lys Met
65 70 75 80
Lys Leu Gln Ile Asp Lys Glu Asp Asn Glu Thr Ala Ser Pro Pro Tyr
85 90 95
Lys Ala Gly Glu Leu Arg Thr Asn Asp Phe Tyr His Tyr Gly Leu Phe
100 105 110
Glu Val Ser Met Lys Pro Ala Lys Ser Thr Gly Thr Val Ser Ser Phe
115 120 125
Phe Thr Tyr Thr Gly Pro Trp Asp Trp Asp Asn Asp Pro Trp Asp Glu
130 135 140
Ile Asp Ile Glu Phe Leu Gly Lys Asp Thr Thr Lys Ile Gln Phe Asn
145 150 155 160
Tyr Phe Thr Asn Gly Val Gly Gly Asn Glu His Tyr His Glu Leu Gly
165 170 175
Phe Asp Ala Ala Asp Asp Phe Asn Thr Tyr Ala Phe Glu Trp Arg Pro
180 185 190
Glu Ser Ile Arg Trp Phe Val Asn Gly Glu Leu Val His Thr Ala Thr
195 200 205
Glu Asn Ile Pro Gln Thr Pro Gln Lys Ile Met Met Asn Leu Trp Pro
210 215 220
Gly Ile Gly Val Asp Gly Trp Thr Gly Arg Phe Asn Gly Glu Asp Thr
225 230 235 240
Pro Val Val Thr Gln Tyr Asp Trp Val Lys Tyr Thr Pro Leu Glu Glu
245 250 255
Leu Gly Cys Tyr Asn Glu Lys Asn Asn Lys Tyr Lys Lys Cys Lys Lys
260 265 270
Thr Lys Val Lys
275
<210> 22
<211> 243
<212> PRT
<213> 莫哈韦芽孢杆菌
<400> 22
Met Ser Tyr Arg Met Lys Arg Val Leu Leu Leu Leu Val Thr Gly Leu
1 5 10 15
Phe Met Ser Leu Ser Ala Phe Thr Ser Thr Ala Ser Ala Gln Thr Gly
20 25 30
Gly Ser Phe Phe Asp Pro Phe Asn Gly Tyr Asn Ser Gly Phe Trp Gln
35 40 45
Lys Ala Asn Gly Tyr Ser Asn Gly Asn Met Phe Asn Cys Thr Trp Arg
50 55 60
Ala Asn Asn Val Ser Met Thr Ser Leu Gly Glu Met Arg Leu Ala Leu
65 70 75 80
Thr Ser Pro Ser Tyr Asn Lys Phe Asp Cys Gly Glu Asn Arg Ser Val
85 90 95
Gln Thr Tyr Gly Tyr Gly Leu Tyr Glu Val Arg Met Lys Pro Ala Lys
100 105 110
Asn Val Gly Ile Val Ser Ser Phe Phe Thr Tyr Thr Gly Pro Thr Asp
115 120 125
Gly Thr Pro Trp Asp Glu Ile Asp Ile Glu Phe Leu Gly Lys Asp Thr
130 135 140
Thr Lys Val Gln Phe Asn Tyr Tyr Thr Asn Gly Val Gly Asn His Glu
145 150 155 160
Lys Leu Val Asp Leu Gly Phe Asp Ala Ala Asn Ala Tyr His Thr Tyr
165 170 175
Ala Phe Asp Trp Gln Pro Asn Ser Ile Lys Trp Tyr Val Asp Gly Gln
180 185 190
Leu Lys His Thr Ala Thr Ser Gln Ile Pro Thr Thr Pro Gly Lys Ile
195 200 205
Met Met Asn Leu Trp Asn Gly Thr Gly Val Asp Glu Trp Leu Gly Ser
210 215 220
Tyr Asn Gly Val Thr Pro Leu Tyr Ala His Tyr Asp Trp Val Arg Tyr
225 230 235 240
Thr Lys Lys
<210> 23
<211> 230
<212> PRT
<213> 人工序列
<220>
<223> His-标记的成熟蛋白质（粘琼脂芽孢杆菌）
<400> 23
His His His His His His Pro Arg His Asn Pro Val Thr Asp Glu Glu
1 5 10 15
Val Tyr His Ser Phe Asn Ser His Asp Trp Gln Asn Trp Asn Met Ser
20 25 30
Asp Gly Trp Lys Asn Asp Asp Tyr Phe Phe Gly Cys His Trp Ser Gln
35 40 45
Asn Arg Val Asn Phe Tyr Gly Gly Gln Met Glu Leu Ser Leu Arg Thr
50 55 60
Asn Tyr Ser Tyr Ala Pro Pro Tyr Asn Tyr Glu Cys Ala Glu Tyr Thr
65 70 75 80
Thr Asn Asn Phe Tyr Gly Tyr Gly Leu Tyr Glu Val Ser Met Lys Pro
85 90 95
Ala Lys Val Ser Gly Val Ile Ser Ser Phe Phe Thr Tyr Thr Gly Pro
100 105 110
Ser Tyr Asn Gly Ala Pro Trp Asp Glu Ile Asp Ile Glu Phe Leu Gly
115 120 125
Asn Asp Thr Thr Lys Val Gln Phe Asn Tyr Tyr Thr Asp Gly Val Gly
130 135 140
Gly Asn Glu Ile Leu Tyr Asp Leu Gly Phe Asp Ala Ala Asp Ser Tyr
145 150 155 160
Asn Thr Tyr Ala Phe Asp Trp Gln Glu Asn Tyr Ile Asn Trp Tyr Val
165 170 175
Asn Gly Gln Leu Val Ala Thr Ala Thr Glu Asn Ile Pro Ser Asn Pro
180 185 190
Ser Lys Ile Met Met Asn Ile Trp Asn Thr Tyr Gly Ile Asp Glu Trp
195 200 205
Ala Gly Arg Tyr Tyr Gly Glu Asp Ala Asn Ala Ser Tyr Asn Trp Val
210 215 220
Arg Tyr Thr Pro Asn Arg
225 230
<210> 24
<211> 269
<212> PRT
<213> 人工序列
<220>
<223> Savinase的变体
<400> 24
Ala Gln Ser Val Pro Trp Gly Ile Glu Arg Val Gln Ala Pro Ala Ala
1 5 10 15
His Asn Arg Gly Leu Thr Gly Ser Gly Val Lys Val Ala Val Leu Asp
20 25 30
Thr Gly Ile Ser Thr His Pro Asp Leu Arg Ile Arg Gly Gly Ala Ser
35 40 45
Phe Val Pro Gly Glu Pro Ser Thr Gln Asp Gly Asn Gly His Gly Thr
50 55 60
His Val Ala Gly Thr Ile Ala Ala Leu Asp Asn Ser Ile Gly Val Leu
65 70 75 80
Gly Val Ala Pro Ser Ala Glu Leu Tyr Ala Val Lys Val Leu Gly Ala
85 90 95
Ser Gly Ser Gly Ser Val Ser Ser Ile Ala Gln Gly Leu Glu Trp Ala
100 105 110
Gly Asn Asn Gly Met His Val Ala Asn Leu Ser Leu Gly Ser Pro Ser
115 120 125
Pro Ser Ala Thr Leu Glu Gln Ala Val Asn Ser Ala Thr Ser Arg Gly
130 135 140
Val Leu Val Val Ala Ala Ser Gly Asn Ser Gly Ala Gly Ser Ile Ser
145 150 155 160
Tyr Pro Ala Arg Tyr Ala Asn Ala Met Ala Val Gly Ala Thr Asp Gln
165 170 175
Asn Asn Asn Arg Ala Ser Phe Ser Gln Tyr Gly Ala Gly Leu Asp Ile
180 185 190
Val Ala Pro Gly Val Asn Ile Leu Ser Thr Trp Pro Gly Ser Thr Tyr
195 200 205
Ala Ser Leu Asn Gly Thr Ser Met Ala Thr Pro His Val Ala Gly Ala
210 215 220
Ala Ala Leu Val Lys Gln Lys Asn Pro Ser Trp Ser Asn Val Gln Ile
225 230 235 240
Arg Asn His Leu Lys Asn Thr Ala Thr Ser Leu Gly Asp Thr Trp Glu
245 250 255
Tyr Gly Ser Gly Leu Val Asn Ala Glu Ala Ala Thr Arg
260 265
Claims (24)
1.一种淀粉酶和/或蛋白酶用于去除和/或减少表面上的污垢、和/或用于减少再沉积的用途，其中将所述表面暴露于所述淀粉酶和/或蛋白酶持续10至240秒的时间段，例如在10至220秒的范围内、例如在10至200秒的范围内、在10至180秒的范围内、在10至160秒的范围内、在10至140秒的范围内、在10至120秒的范围内、在10至100秒的范围内、在10至80秒的范围内、在10至70秒的范围内、在10至66秒的范围内、在20至66秒的范围内、在25至66秒的范围内、在28至66秒的范围内、在28至60秒的范围内、在28至55秒的范围内、在28至50秒的范围内或在28至45秒的范围内。
2.根据权利要求1所述的用途，其中所述淀粉酶和/或蛋白酶包含在液体中，所述液体具有的pH在7-10.5的范围内、例如在7.5-10.5的范围内、例如在7.5-10的范围内、在7.5-9.5的范围内、在7.5-9.0的范围内、在7.5-8.5的范围内、在7.5-8.2的范围内、或在7.8-8.2的范围内。
3.根据权利要求1或2所述的用途，其中使用淀粉酶，并且所述淀粉酶与SEQ ID NO:1、2、3或4的序列具有至少70％，例如至少75％、例如至少80％、例如至少85％、例如至少90％、例如至少95％、例如至少98％、例如至少99％、例如100％的序列同一性。
4.根据权利要求3所述的用途，其中所述淀粉酶是α-淀粉酶变体，所述变体在与以下位置对应的一个或多个位置处包含修饰：SEQ ID NO:4的H1、N54、V56、K72、G109、F113、R116、T134、W140、W159、W167、Q169、Q172、L173、A174、R181、G182、D183、G184、W189、E194、N195、V206、G255、N260、F262、A265、W284、F289、S304、G305、W347、K391、Q395、W439、W469、R444、F473、G476和G477，其中所述α-淀粉酶变体与SEQ ID NO:4具有至少75％但小于100％的序列同一性，并且其中所述α-淀粉酶变体具有α-淀粉酶活性。
5.根据权利要求4所述的用途，其中所述一个或多个位置处的修饰选自下组，该组由以下组成：H1*、H1A、N54S、V56T、K72R、G109A、F113Q、R116Q、R116H、T134E、W140Y、W140F、W140H、W159Y、W159F、W159H、W167Y、W167H、W167F、Q169E、Q172K、Q172G、Q172N、L173P、A174*、A174S、R181*、G182*、D183*、G184*、G184T、W189Y、W189F、W189H、W189E、W189D、W189Q、W189N、E194D、E194N、E194S、N195F、V206L、V206F、V206Y、G255A、N260G、N260P、N260A、N260G、N260P、N260A、A265G、W284G、W284H、F289H、S304K、S304R、S304Q、S304E、G305K、G305R、G305Q、G305E、W347Y、W347F、W347H、K391A、Q395P、W439N、W439Q、W439T、R444Q、W469T、W469N、F473R、G476R、G476Q、G476E、G476K G477K、G477R、G477Q、以及G477E，其中这些位置对应于SEQ ID NO:4的位置。
6.根据权利要求5所述的用途，其中所述至少一种α-淀粉酶变体在与SEQ ID NO:4的R181+G182；R181+D183；R181+G184；G182+D183；G182+G184或D183+G184对应的位置处包含缺失。
7.根据权利要求5-6所述的用途，其中所述α-淀粉酶变体选自下组，该组由以下组成：
SEQ ID NO:4的多肽的H1*+N54S+V56T+G109A+Q169E+Q172K+A174*+G182*+D183*+N195F+V206L+K391A+G476K；
H1*+N54S+V56T+G109A+R116H+A174S+G182*+D183*+N195F+V206L+K391A+G476K；
H1*+N54S+V56T+K72R+G109A+F113Q+R116Q+W167F+Q172G+A174S+G182*+D183*+G184T+N195F+V206L+K391A+P473R+G476K；
H1*+N54S+V56T+G109A+F113Q+R116Q+Q172N+A174S+G182*+D183*+N195F+V206L+A265G+K391A+P473R+G476K；
H1*+N54S+V56T+K72R+G109A+F113Q+W167F+Q172R+A174S+G182*+D183*+N195F+V206L+K391A+G476K；
H1*+N54S+V56T+K72R+G109A+R116H+T134E+W167F+Q172G+L173V+A174S+G182*+D183*+N195F+V206L+G255A+K391A+G476K；
H1*+N54S+V56T+K72R+G109A+R116H+T134E+W167F+Q172G+L173V+A174S+G182*+D183*+N195F+V206L+G255A+K391A+Q395P+T444Q+P473R+G476K；
H1*+N54S+V56T+G109A+T134E+A174S+G182*+D183*+N195F+V206L+K391A+G476K；
H1*+N54S+V56T+K72R+G109A+A174S+G182*+D183*+N195F+V206L+G255A+K391A+G476K；
H1*+N54S+V56T+K72R+G109A+F113Q+R116Q+W167F+Q172G+A174S+G184T+N195F+V206L+K391A+P473R+G476K，以及
H1*+N54S+V56T+G109A+W167F+Q172E+L173P+A174K+G182*+D183*+N195F+V206L+K391A+G476K，并且其中所述α-淀粉酶变体与SEQ ID NO:4的多肽共享至少80％，例如至少85％、例如至少90％、例如至少93％、例如至少94％、例如至少95％、例如至少96％、例如至少97％、例如至少98％但小于100％的序列同一性，并且其中所述α-淀粉酶变体具有α-淀粉酶活性。
8.根据前述权利要求中任一项所述的用途，其中使用蛋白酶，并且所述蛋白酶选自下组，该组由以下组成：
i.与SEQ ID NO:5、6、7或8的序列具有至少70％，例如至少75％、例如至少80％、例如至少85％、例如至少90％、例如至少95％、例如至少98％、例如至少99％、例如100％的序列同一性的蛋白酶；
ii.在与SEQ ID NO:3的位置9、15、36、61、68、76、99、106、120、167、170、194、195、205、218、235、245或261对应的一个或多个位置处包含取代的蛋白酶变体，其中所述蛋白酶变体与SEQ ID NO:5具有至少75％但小于100％的序列同一性，
iii.SEQ ID NO:24的蛋白酶。
9.根据权利要求8所述的用途，其中所述蛋白酶选自下组，该组由以下组成：SEQ IDNO:5的M222S、*36D+N76D+N120D+G195E+K235L、Y167A+R170S+A194P、S99SE、V68A+S106A、S9R+A15T+V68A+N218D+Q245R、S9R+A15T+G61E+V68A+A194P+V205I+Q245R+N261D和S99AD，其中所述蛋白酶变体与SEQ ID NO:5具有至少75％但小于100％的序列同一性，并且其中所述蛋白酶变体具有蛋白酶活性。
10.根据前述权利要求中任一项所述的用途，其中使用另外的酶，所述酶选自下组，该组由以下组成：蛋白酶、脂肪酶、角质酶、淀粉酶、糖酶、纤维素酶、果胶酶、甘露聚糖酶、阿拉伯糖酶、半乳聚糖酶、木聚糖酶、氧化酶、地衣多糖酶、漆酶和/或过氧化物酶。
11.根据前述权利要求中任一项所述的用途，其中所述表面是器皿洗涤机的内表面或器皿的表面。
12.一种器皿洗涤洗涤剂组合物，所述组合物包含淀粉酶和/或蛋白酶和一种或多种洗涤剂组分，所述组合物具有在7-10.5范围内的pH。
13.根据权利要求12所述的组合物，其中所述洗涤剂组分选自下组，该组由以下组成：表面活性剂、助洗剂、螯合剂或螯合试剂、漂白体系或漂白组分、聚合物、增泡剂、抑泡剂、染料、香料、晦暗抑制剂、光学增亮剂、杀细菌剂、杀真菌剂、污垢悬浮剂、抗腐蚀剂、酶稳定剂、酶抑制剂或活化剂、一种或多种转移酶、水解酶、氧化还原酶、上蓝剂和荧光染料、抗氧化剂、以及增溶剂。
14.根据权利要求12或13所述的组合物，其中所述组合物进一步包含一种或多种蛋白酶抑制剂，所述蛋白酶抑制剂中至少一种是肽醛、其亚硫酸氢盐加合物或半缩醛加合物。
15.根据权利要求12-14中任一项所述的组合物，其中所述组合物包含淀粉酶，并且所述淀粉酶是α-淀粉酶。
16.根据权利要求15所述的组合物，其中淀粉酶与SEQ ID NO:1、2、3或4的序列具有至少70％，例如至少75％、例如至少80％、例如至少85％、例如至少90％、例如至少95％、例如至少98％、例如至少99％、例如100％的序列同一性。
17.根据权利要求16所述的组合物，其中所述淀粉酶是α-淀粉酶变体，所述变体在与以下位置对应的一个或多个位置处包含修饰：SEQ ID NO:4的H1、N54、V56、K72、G109、F113、R116、T134、W140、W159、W167、Q169、Q172、L173、A174、R181、G182、D183、G184、W189、E194、N195、V206、G255、N260、F262、A265、W284、F289、S304、G305、W347、K391、Q395、W439、W469、R444、F473、G476和G477，其中所述α-淀粉酶变体与SEQ ID NO:4具有至少75％但小于100％的序列同一性，并且其中所述α-淀粉酶变体具有α-淀粉酶活性。
18.根据权利要求16或17所述的组合物，其中所述一个或多个位置处的修饰选自下组，该组由以下组成：H1*、H1A、N54S、V56T、K72R、G109A、F113Q、R116Q、R116H、T134E、W140Y、W140F、W140H、W159Y、W159F、W159H、W167Y、W167H、W167F、Q169E、Q172K、Q172G、Q172N、L173P、A174*、A174S、R181*、G182*、D183*、G184*、G184T、W189Y、W189F、W189H、W189E、W189D、W189Q、W189N、E194D、E194N、E194S、N195F、V206L、V206F、V206Y、G255A、N260G、N260P、N260A、N260G、N260P、N260A、A265G、W284G、W284H、F289H、S304K、S304R、S304Q、S304E、G305K、G305R、G305Q、G305E、W347Y、W347F、W347H、K391A、Q395P、W439N、W439Q、W439T、R444Q、W469T、W469N、F473R、G476R、G476Q、G476E、G476K G477K、G477R、G477Q、以及G477E，其中这些位置对应于SEQ ID NO:4的位置。
19.根据权利要求16-18中任一项所述的组合物，其中所述至少一种α-淀粉酶变体在与SEQ ID NO:4的R181+G182；R181+D183；R181+G184；G182+D183；G182+G184或D183+G184对应的位置处包含缺失。
20.根据权利要求16-19中任一项所述的组合物，其中所述α-淀粉酶变体选自下组，该组由以下组成：
SEQ ID NO:4的多肽的H1*+N54S+V56T+G109A+Q169E+Q172K+A174*+G182*+D183*+N195F+V206L+K391A+G476K；
H1*+N54S+V56T+G109A+R116H+A174S+G182*+D183*+N195F+V206L+K391A+G476K；
H1*+N54S+V56T+K72R+G109A+F113Q+R116Q+W167F+Q172G+A174S+G182*+D183*+G184T+N195F+V206L+K391A+P473R+G476K；
H1*+N54S+V56T+G109A+F113Q+R116Q+Q172N+A174S+G182*+D183*+N195F+V206L+A265G+K391A+P473R+G476K；
H1*+N54S+V56T+K72R+G109A+F113Q+W167F+Q172R+A174S+G182*+D183*+N195F+V206L+K391A+G476K；
H1*+N54S+V56T+K72R+G109A+R116H+T134E+W167F+Q172G+L173V+A174S+G182*+D183*+N195F+V206L+G255A+K391A+G476K；
H1*+N54S+V56T+K72R+G109A+R116H+T134E+W167F+Q172G+L173V+A174S+G182*+D183*+N195F+V206L+G255A+K391A+Q395P+T444Q+P473R+G476K；
H1*+N54S+V56T+G109A+T134E+A174S+G182*+D183*+N195F+V206L+K391A+G476K；
H1*+N54S+V56T+K72R+G109A+A174S+G182*+D183*+N195F+V206L+G255A+K391A+G476K；
H1*+N54S+V56T+K72R+G109A+F113Q+R116Q+W167F+Q172G+A174S+G184T+N195F+V206L+K391A+P473R+G476K，以及
H1*+N54S+V56T+G109A+W167F+Q172E+L173P+A174K+G182*+D183*+N195F+V206L+K391A+G476K，并且其中所述α-淀粉酶变体与SEQ ID NO:4的多肽共享至少80％，例如至少85％、例如至少90％、例如至少93％、例如至少94％、例如至少95％、例如至少96％、例如至少97％、例如至少98％但小于100％的序列同一性，并且其中所述α-淀粉酶变体具有α-淀粉酶活性。
21.根据权利要求12-20中任一项所述的组合物，其中所述组合物包含蛋白酶，并且所述蛋白酶选自下组，该组由以下组成：
i.与SEQ ID NO:5、6、7或8的序列具有至少70％，例如至少75％、例如至少80％、例如至少85％、例如至少90％、例如至少95％、例如至少98％、例如至少99％、例如100％的序列同一性的蛋白酶；
ii.在与SEQ ID NO:3的位置9、15、36、61、68、76、99、106、120、167、170、194、195、205、218、235、245或261对应的一个或多个位置处包含取代的蛋白酶变体，其中所述蛋白酶变体与SEQ ID NO:5具有至少75％但小于100％的序列同一性，
iii.SEQ ID NO:24的蛋白酶。
22.根据权利要求21所述的组合物，其中所述蛋白酶选自下组，该组由以下组成：SEQID NO:5的M222S、*36D+N76D+N120D+G195E+K235L、Y167A+R170S+A194P、S99SE、V68A+S106A、S9R+A15T+V68A+N218D+Q245R、S9R+A15T+G61E+V68A+A194P+V205I+Q245R+N261D和S99AD，其中所述蛋白酶变体与SEQ ID NO:5具有至少75％但小于100％的序列同一性，并且其中所述蛋白酶变体具有蛋白酶活性。
23.根据权利要求12-22中任一项所述的组合物，所述组合物进一步包含选自下组的另外的酶，该组由以下组成：另外的蛋白酶、脂肪酶、角质酶、另外的淀粉酶、糖酶、纤维素酶、果胶酶、甘露聚糖酶、阿拉伯糖酶、半乳聚糖酶、木聚糖酶、氧化酶、地衣多糖酶、漆酶和/或过氧化物酶。
24.一种用于去除和/或减少表面上的污垢的方法，其中清洁循环包括以下步骤：
i.洗涤步骤，其中将所述表面暴露于包含以下项的洗涤液
c.淀粉酶和/或蛋白酶和任选的洗涤剂组分，或
d.根据权利要求12-23中任一项所述的器皿洗涤洗涤剂组合物，
ii.任选地排出部分所述洗涤液，
iii.任选地漂洗所述表面，
iv.任选地干燥所述表面；
其中将所述表面暴露于所述洗涤液持续在10至240秒范围内的时间段。
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| CN114174485A (zh) * | 2019-07-22 | 2022-03-11 | 汉高股份有限及两合公司 | 具有改善的酶稳定性的清洗剂和清洁剂 |
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| CN110777136B (zh) * | 2019-11-26 | 2022-12-30 | 山西大学 | 一种洗涤用的碱性蛋白酶突变体及其在液体洗涤剂中的应用 |
Also Published As
| Publication number | Publication date |
|---|---|
| US20200140786A1 (en) | 2020-05-07 |
| EP3519548A1 (en) | 2019-08-07 |
| WO2018060216A1 (en) | 2018-04-05 |
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