CN103249313A - 疏水化的蛋白水解产物 - Google Patents
疏水化的蛋白水解产物 Download PDFInfo
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Abstract
本发明涉及酶疏水化的蛋白水解产物、它们的制备和用途,还涉及包含所述水解产物的化妆品制剂。
Description
发明领域
本发明涉及酶疏水化的蛋白水解产物、它们的制备和用途,还涉及包含这些水解产物的化妆品制剂。
背景技术
蛋白和蛋白水解产物是一类受关注的原材料,因为它们容易获得、是天然来源的且可生物降解的。然而,由于缺少亲脂性基团,所以蛋白的界面活性性质非常不明显。因此,必须引入其它亲脂性基团,以获得有效的蛋白系界面活性化合物。根据现有技术,期望的改性蛋白已获得了较长的时间,其是通过缩合蛋白水合物和酰基氯(下文称为PHFSK)来制备,并且由于它们的表面活性性质而用于各种应用(例如,用于制备乳液、泡沫,护理皮肤和头发,将颜料分散在各种溶剂中,等等)。
然而,合成(例如,用亚硫酰氯,由脂肪酸混合物合成)所需的酰基氯的分离从生态学角度是不可接受的,此外,在缩合反应期间产生不可忽视的量的盐;这能相当大地改变产物性质,因此必须将其分离,这可能涉及到高花费。此外,获得的改性程度非常低,或仅能用大量过剩的酸来实现(Roussel-Philippe等人,European Journal of Lipid Science and Technology102[2],97-101.2000)。最终,衍生化改变了可获得的碱性基团的所有组成成分(repertoire),因为赖氨酸残基的伯氨基优先被酰胺化。这是不利的,因为在例如头发护理的某些应用中期望阳离子基团的存在,但是赖氨酸残基在酰胺化之后不再可得。
转谷氨酰胺酶(TG)用于蛋白和蛋白水解产物的交联的用途为人们所知已有较长时间。反应是在蛋白的赖氨酸和谷氨酰胺残基之间的转酰胺基反应,其间释放氨并形成异肽键。
同样已知的是,伯烷基胺还能在转谷氨酰胺酶催化的转酰胺基反应中替代赖氨酸用作亲核体。这已在关于合成作为模型底物的二肽的文献(Ohtsuka等人,(2000)J Agric.Food Chem48:6230-6233)以及关于完整蛋白的文献(Nieuwenhuizen等人,(2004)Biotechnol Bioeng85:248-258)中表明。
仅考虑起始材料和产物的结构,那么,其在形式上为肽的烷基化。因此,对于本发明,讨论的是“烷基化蛋白水解产物”或“烷基化”。
然而,对于完整蛋白,与PHFSK相比,仅能实现低程度的改性(g烷基基团/g蛋白)(对于PHFSK为6-8%,对于TG催化烷基化为0.2-0.4%,参阅Ohtsuka等人,(2000)J Agric.Food Chem48:6230-6233,Nieuwenhuizen等人,(2004)Biotechnol Bioeng85:248-258以及Roussel-Philippe等人,EuropeanJournal of Lipid Science and Technology102[2],97-101.2000)。
因此,这些反应产物的两亲特性非常不明显,并且这些通过转谷氨酰胺酶催化而疏水化的蛋白不能用于替代传统的PHFSK。
本发明的目的是提供克服现有技术的至少一个缺点的疏水化肽。
发明内容
令人惊讶地,已发现借助转谷氨酰胺酶烷基化并在下面描述的蛋白水解产物能实现本发明的目的。
因此,本发明提供酶疏水化的蛋白水解产物、它们的制备和用途。
本发明还提供了包含本发明的疏水化的蛋白水解产物的制剂,特别是化妆品配制剂。
本发明的一个优点是:在合成期间不需要酰基氯。
另一优点是:由于有时蛋白水解产物非常高的谷氨酰胺含量,所以产物能具有高度的衍生化,同时,因为与酰基氯相反,不发生二次反应(水解),所以必须使用较小浓度的烷基胺。
因此,能有利地观察到优异的起泡行为。优点还在于,产生的副产物是易于馏出的氨而非氯化钠(在酰基氯的情况下)。此外,反应在中性pH范围内进行,意味着由于pH调节而不引入盐。最后,重要的优点在于,蛋白水解产物的氨基很大程度上保持完整,因为在烷基胺的存在下,通过转谷氨酰胺酶催化主要转化谷氨酰胺残基。蛋白水解产物的伯氨基(赖氨酸的末端氨基和ε-氨基)对产物的理化性质产生重要贡献(例如,促进与/向皮肤和头发的负电荷表面的相互作用/结合=直接性)。在用酰基氯衍生化期间,这些亲核氨基优选被转化为酰胺,并且因此不能再促进直接性。
本发明提供可通过包括下列工艺步骤的方法获得的烷基化肽混合物:
A)水解至少一种包含至少一个谷氨酰胺残基的蛋白以产生蛋白水解产物,并任选地纯化所述蛋白水解产物,
B)使所述蛋白水解产物与转谷氨酰胺酶和至少一种通式(I)的伯胺或仲胺(特别是伯胺)接触,
其中R1和R2彼此独立地相同或不同并选自任选不饱和的、任选取代的、任选支化的具有5至40个、优选5至22个、特别是6至18个碳原子的有机基团,
C)纯化所述烷基化肽混合物。
对于本发明,术语“烷基化肽混合物”应理解为表示包含至少两种各自在至少一个谷氨酰胺上被烷基化的肽的混合物。因此,显而易见的是,对于在工艺步骤A)中仅一种类型的蛋白被水解的情况,该蛋白必须具有至少两个谷氨酰胺残基。
除非另有规定,提及的所有百分比(%)均为质量百分比。
实际上,在工艺步骤A)中使用容易获得的蛋白源是有利的;这些蛋白源特别地可以蛋白混合物的形式获得。因此,所述至少一种蛋白优选选自包括下列并优选由下列组成的清单:
分离的植物储藏蛋白,例如小麦蛋白(谷蛋白)、大豆蛋白、豌豆蛋白、大米蛋白、玉米蛋白、羽扇豆蛋白;
动物蛋白,例如胶原、角蛋白、酪蛋白、乳清蛋白(乳球蛋白)、丝蛋白(丝心蛋白);以及
微生物蛋白,例如酵母蛋白提取物、藻类蛋白或细菌生物质(SCP=单细胞蛋白)。
根据本发明,在工艺步骤A)中使用具有高分数谷氨酰胺残基的蛋白混合物是有利的,因此所述蛋白优选选自包括下列并优选由下列组成的清单:小麦谷蛋白,豆类、特别是大豆、豌豆、羽扇豆的分离的储存蛋白,以及奶蛋白、特别是酪蛋白和乳球蛋白,并且小麦谷蛋白是非常特别优选的。
工艺步骤A)中的水解优选通过添加酸、特别优选通过使用酶来催化。合适的工艺是本领域技术人员已知的;同样地,无需努力既可调节各个工艺参数以使在工艺步骤A)中形成具有所需平均分子量的蛋白水解产物。关于酶催化水解工艺的此类说明可由本领域技术人员在Aaslyng等人,(1988)J Agric. Food Chem 46:481-489以及Adler-Nissen J (1976) J Agric. FoodChem 24:1090-1093中找到,对于由酸或碱催化的工艺的此类说明可在Aaslyng等人,(1998) J Agric.Food Chem 46:481-489中找到。
根据本发明,来自工艺步骤A)的蛋白水解产物优选具有下列的平均分子量:203g/mol至100000g/mol,优选500g/mol至20000g/mol,特别是1000g/mol至15000g/mol。
可根据工艺步骤A)制备并直接用于工艺步骤B)的蛋白水解产物还是可商购的;这些蛋白水解产物例如为:Meripro 810和Meripro 711(小麦蛋白水解产物,酶法和化学法的,Syral)、NaturalysW(小麦蛋白水解产物,Roquette)、Cropeptide W、Hydrotriticum 2000、Tritisol、Tritisol XM (具有不同分子量分布的小麦蛋白水解产物,Croda)、Hydrosoy 2000(大豆蛋白水解产物,Croda)、GluadinW20和GluadinWLM(具有不同分子量分布的小麦蛋白水解产物,Cognis)、AMCO HCA411和HLA-198(酪蛋白或乳清蛋白水解产物,American Casein Company)。
在工艺步骤B)中,原则上可使用本领域技术人员已知的属于EC类2.3.2.13的所有转谷氨酰胺酶,也可以使用这些转谷氨酰胺酶的具有相应的酶活性的片段。这类酶可分离自例如轮枝链霉菌属(Streptoverticillium)、芽孢杆菌属(Bacillus)、各种放线菌和黏菌,而且也可分离自植物、鱼和哺乳动物来源,例如猪肝。EP 2123756和WO 2009101762描述了与野生型相比稳定的转谷氨酰胺酶,优选将其用在本发明的工艺步骤B)中。
优选的是,在工艺步骤B)中使用的转谷氨酰胺酶可分离自选自枯草芽孢杆菌(Bacillus subtilis)、茂原链轮丝菌(Streptomyces mombaraensis)(以前称为茂原轮枝链霉菌(Streptoverticillium mobaraense))。就此而言,特别优选的转谷氨酰胺酶选自来自Ajinomoto的、可以商品名“Activa”获得的转谷氨酰胺酶(来自茂源链轮丝菌的转谷氨酰胺酶),例如ActivaWM、ActivaEB、ActivaPB、ActivaWS、ActivaYG。
在工艺步骤B)中,所述蛋白水解产物优选以下列浓度使用:以总反应混合物(其中溶剂和/或分散液(dispersant)优选为水)计,5重量%至40重量%,优选15重量%至25重量%。在一些情况下,可能有利是:在工艺步骤B)中添加转谷氨酰胺酶之前,将反应混合物加热至超过50℃,优选超过70℃,以增加水合过程的速率,在所述水和过程期间优选进行反应混合物的彻底混合(例如通过搅拌)。
工艺步骤B)中的通式(I)的伯胺或仲胺的R1和R2基团优选选自烷基和烯基,优选直链、未取代的烷基和烯基,特别是辛基、癸基、十二烷基、十四烷基、十六烷基、十八烷基、十八烯基、十八碳二烯基、二十烷基、二十二烷基。
R1和R2基团还可为烷基的混合物,特别是这些烷基的工业级混合物。这类工业级混合物的烷基优选得自脂肪酸混合物,其可通过各种方法从植物脂肪酸混合物获得并且可通过各种方法分馏。这类植物脂肪酸混合物的脂肪酸组成根据用于分离的油籽而变化,并且是本领域技术人员已知的,例如以任选分馏的菜籽油脂肪酸、大豆油脂肪酸、向日葵油脂肪酸、牛脂油脂肪酸、椰子油脂肪酸的形式。
因此,在工艺步骤B)中优选使用的烷基胺选自:油菜籽脂肪胺、大豆脂肪胺、向日葵脂肪胺、牛脂脂肪胺、棕榈脂肪胺、棕榈仁脂肪胺和椰油脂肪胺。
通式(I)的胺优选以下列浓度用于工艺步骤B)中:以总反应混合物计,0.25重量%至10重量%,特别是0.5重量%至5重量%。工艺步骤B)中的反应混合物的酶活性优选为10-25000U/l、优选200-1000U/l、特别优选300-600 U/l,其中单位U可根据Folk和Cole(1966),Biochim.Biophys.Acta122:244-264所述的氧肟酸盐测定来测定。
在工艺步骤B)中,pH优选为5至10,优选为6至8,特别优选为6.5至7.5。
优选地,在工艺步骤B)中的转谷氨酰胺酶反应期间进行反应混合物的彻底混合(例如通过搅拌)。
在工艺步骤B)中的转谷氨酰胺酶反应期间,反应混合物的温度优选为20℃至50℃,优选为30℃至45℃,并且特别优选为35℃至40℃。
工艺步骤B)中的转谷氨酰胺酶反应的反应时间高达数小时,取决于所用的温度。
如果在工艺步骤A)中通过使用至少一种酶催化所述水解,那么,出于节约时间的原因,有利的是同时进行工艺步骤A)和工艺步骤B)。
本发明还提供可用于制备本发明的肽混合物的上述方法。本发明优选的方法为产生上述优选的本发明肽混合物的那些方法。
本发明的烷基化肽混合物可有利地用于清洁组合物、化妆品制剂或药物制剂以及作物保护制剂中。
因此,本发明还提供包含本发明的烷基化肽混合物的化妆品制剂、皮肤病学制剂或药物制剂、作物保护制剂,以及护理组合物和清洁组合物及表面活性剂浓缩物。
术语“护理组合物”在本文中理解为表示满足下列目的的制剂:使物体保留其原始形式,降低或消除外界影响(例如时间、光、温度、压力、污染、与其它接触所述物体的其他反应性化合物的化学反应)的作用,例如老化、污染、材料疲劳、褪色,或甚至改善所述物体的期望的积极性质。对于最后一点,可以提及的是例如在缩合下,物体改善的毛发光泽或更大的弹性。
“作物保护制剂”应理解为表示根据它们的配制物的性质而明显用于作物保护的那些制剂;如果在所述制剂中存在来自下述类别的至少一种化合物:除草剂、杀真菌剂、杀虫剂、杀螨剂、杀线虫剂、针对鸟的保护剂、植物营养物和土壤结构改进剂,则尤其是这种情况。
本发明优选的化妆品组合物选自:乳膏、洗剂、润发露和洗发剂。
本发明的肽混合物具有有利的乳化和稳定泡沫的性质。因此,本发明的其他主题为本发明的肽混合物作为乳化剂(如O/W或W/O乳化剂)、皮肤和头发护理剂、分散助剂(特别是对于化妆品色素)、发泡剂(foam former)或泡沫稳定剂的用途。
在下面所列的实施例中,通过实例来描述本发明,并不旨在将本发明限制成实施例所述的实施方案,本发明的范围由整个说明书和权利要求书限定。
下列附图形成实施例的一部分:
图1:通过转谷氨酰胺酶催化的改性小麦蛋白水解产物的疏水化改善泡沫稳定性。(“MP810”(正方形)=Meripro810,Syral;“MP810+OA+TG(失活的)”(三角形)=Meripro 810+辛胺(OA)+失活的转谷氨酰胺酶(TG)=阴性对照;“MP810+OA+TG”(菱形)=Meripro 810+辛胺(OA)+转谷氨酰胺酶(TG)
实施例:
实施例1:小麦蛋白水解产物与辛胺和月桂胺的转谷氨酰胺酶催化的疏水化,与未水解的小麦蛋白的对比以及与未疏水化的小麦蛋白水解产物的对比
商购小麦蛋白(Amygluten 110,Syral,分子量>200kD)和从其制备的水解产物(Meripro 810,分子量~10kD)各自以pH=7.5和10重量%的浓度,连同辛胺或月桂胺(2.5重量%)一起分散在水中。添加1重量%的商购转谷氨酰胺酶制剂(Activa WM,Ajinomoto)并将混合物在45℃下搅拌超过24小时。然后在80℃的温度下使酶失活。作为对照,分别进行具有失活酶的混合物以及没有烷基胺的混合物。与对照反应相比,在用1-氯-2,4-二硝基苯(CDNB)衍生化之后,通过光度计测定来测定烷基胺的转化(Ekladius和King,(1957)Biochem J65:128-131)。
然而,在与未水解小麦蛋白(Amygluten110,Syral)反应的情况下,未能检测到烷基胺的转化,在水解产物的情况下,测量到烷基胺转化大于50%。约10%的氨基酸残基和~30%的可利用谷氨酰胺残基被改性。
实施例2:表面活性
通过垂滴法测定对于空气的表面张力和/或对于石蜡和/或碳酸二乙基己酯(DEC)的界面张力。对用辛胺改性的小麦蛋白水解产物的1%浓度溶液和相应的对照反应进行测定。作为改性的结果,界面活性能得到非常大的改善(界面张力和表面张力降低,表1)。
表1:转谷氨酰胺酶催化的小麦蛋白水解产物(Meripro810,Syral)的疏水化对界面活性的影响
实施例3:泡沫形成和泡沫稳定性
在1%溶液的振荡实验中,与相应对照比较小麦蛋白水解产物与辛胺的疏水化对泡沫形成和泡沫稳定性的作用。为此,将10ml的相应样品倾倒入50ml的具有体积标度的聚丙烯离心管中,并且在相同条件下振荡1分钟。期间读出液体上的泡沫体积,以评价起始泡沫体积和泡沫稳定性。在此发现了疏水化的小麦蛋白水解产物显著的稳定泡沫的作用(图1)。
实施例4:乳液性能
在振荡实验中,以1ml的级别来研究用辛胺改性的小麦蛋白水解产物的乳化性质以及用月桂胺改性的小麦蛋白水解产物的乳化性质。对于20/79/1的甘油三酯/水/乳化剂,研究各种样品和对照。通过剧烈振荡来制备乳液,并且监测相分离的动力学。在此发现,在疏水化的蛋白水解产物的情况下的相分离明显慢于在相应的对照的情况下的相分离,并且是不完全的。
实施例5:与酰基氯改性的小麦蛋白水解产物的比较
如实施例1所述合成月桂胺改性的小麦蛋白水解产物;所用的月桂胺的浓度为0.625%(w/w)。
借助于酰基氯,使用与转谷氨酰胺酶催化的制备中相同的材料浓度和相同的小麦蛋白水解产物,制备了月桂酰氯(Laurylchlorid)改性的小麦蛋白水解产物(PHFSK)。对于Schotten-Baumann缩合反应,程序依据文献所述的最佳反应条件(Roussel-Philippe等人,European Journal of Lipid Scienceand Technology102[2],97-101.2000):在向小麦蛋白水解产物(在水中,10重量%)添加月桂酰氯之前,通过添加NaOH确立pH为9。然后,在4℃的温度下,逐步添加月桂酰氯,直至浓度为0.625重量%。4小时后,通过添加HCl,将pH调节至5,以将可能未反应的酰基氯水解为脂肪酸。然后,通过添加NaOH将pH调节至7.5。将烷基胺改性的小麦蛋白水解产物和酰基氯改性的小麦蛋白水解产物的泡沫体积和泡沫稳定性如实施例3所述那样相互比较。对于实验,将样品调节至蛋白含量为1重量%。在烷基胺改性的小麦蛋白水解产物的情况下,观察到更高的泡沫形成(为15ml,而非在酰基氯改性的小麦蛋白水解产物的情况下的10ml)。
Claims (11)
2.如权利要求1所述的烷基化肽混合物,其特征在于,所述至少一种蛋白选自:分离的植物储藏蛋白、动物蛋白和微生物蛋白。
3.如权利要求1或2所述的烷基化肽混合物,其特征在于,通过添加至少一种酸或通过使用至少一种酶来催化工艺步骤A)中的水解。
4.如前述权利要求中至少一项权利要求所述的烷基化肽混合物,其特征在于,来自工艺步骤A)的蛋白水解产物具有203g/mol至100000g/mol的平均分子量。
5.如前述权利要求中至少一项权利要求所述的烷基化肽混合物,其特征在于,来自工艺步骤A)的蛋白水解产物对应于可商购的产品Meripro810、Meripro711、Naturalys W、Cropeptide W、Hydrotriticum 2000、Tritisol、Tritisol XM、Hydrosoy2000、Gluadin W20、Gluadin WLM、AMCO HCA411或HLA-198。
6.如前述权利要求中至少一项权利要求所述的烷基化肽混合物,其特征在于,工艺步骤B)中使用的转谷氨酰胺酶可从枯草芽孢杆菌(Bacillussubtilis)、茂原链轮丝菌(Streptoverticillium mombaraensis)分离。
7.如前述权利要求中至少一项权利要求所述的烷基化肽混合物,其特征在于,工艺步骤B)中的通式(I)的伯胺或仲胺的R1和R2基团选自烷基和烯基,优选直链、未取代的烷基和烯基,特别是辛基、癸基、十二烷基、十四烷基、十六烷基、十八烷基、十八烯基、十八碳二烯基、二十烷基、二十二烷基。
8.如前述权利要求中至少一项权利要求所述的烷基化肽混合物,其特征在于,在工艺步骤A)中,通过使用至少一种酶来催化所述水解,并且工艺步骤A)和工艺步骤B)同时进行。
9.用于制备烷基化肽混合物的方法,其包括下列工艺步骤:
A)水解至少一种包含至少一个谷氨酰胺残基的蛋白以产生蛋白水解产物,并任选地纯化所述蛋白水解产物,
B)使所述蛋白水解产物与转谷氨酰胺酶和至少一种通式(I)的伯胺或仲胺接触,
其中R1和R2彼此独立地相同或不同并选自任选不饱和的、任选取代的、任选支化的具有5至40个碳原子的有机基团以及H,以及,任选地
C)纯化所述烷基化肽混合物。
10.包含权利要求1至8中至少一项权利要求所述的至少一种肽混合物的化妆品制剂、皮肤病学制剂或药物制剂、作物保护制剂、护理组合物和清洁组合物或者表面活性剂浓缩物。
11.权利要求1至8中至少一项权利要求所述的至少一种肽混合物作为乳化剂、分散助剂、皮肤和毛发护理剂、发泡剂或泡沫稳定剂的用途。
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DE102010062600A DE102010062600A1 (de) | 2010-12-08 | 2010-12-08 | Hydrophobisiertes Proteinhydrolysat |
PCT/EP2011/069811 WO2012076284A1 (de) | 2010-12-08 | 2011-11-10 | Hydrophobisiertes proteinhydrolysat |
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DE102012205372A1 (de) * | 2012-04-02 | 2013-10-02 | Evonik Industries Ag | Glutaminreiche Peptide als Luftporenbildner in Baustoffmassen |
CN106082752B (zh) * | 2016-06-15 | 2017-11-24 | 中原工学院 | 一种酶交联混合水解蛋白水泥发泡剂的制备方法 |
CN112998010A (zh) * | 2021-03-03 | 2021-06-22 | 成都嘉佑美康新材料科技有限公司 | 一种无人机植保飞防专用助剂及其制备方法和应用 |
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CN115233450B (zh) * | 2022-08-04 | 2023-12-26 | 江南大学 | 一种生物法制备醇溶蛋白疏水整理剂的方法 |
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US20130251658A1 (en) | 2013-09-26 |
DE102010062600A1 (de) | 2012-06-14 |
BR112013012390A8 (pt) | 2017-08-15 |
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