CN103182387A - 防止、去除、减少或破坏生物膜的方法 - Google Patents
防止、去除、减少或破坏生物膜的方法 Download PDFInfo
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- CN103182387A CN103182387A CN2012103570756A CN201210357075A CN103182387A CN 103182387 A CN103182387 A CN 103182387A CN 2012103570756 A CN2012103570756 A CN 2012103570756A CN 201210357075 A CN201210357075 A CN 201210357075A CN 103182387 A CN103182387 A CN 103182387A
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Abstract
本发明涉及防止、去除、减少或破坏生物膜的方法,具体的涉及防止、去除、减少或破坏表面上的生物膜的方法,包括使所述表面与来自细菌的α-淀粉酶接触。
Description
本发明是申请日为2005年09月07日,申请号为“200580030095.0”(国际申请号为PCT/US2005/031813),名称为“防止、去除、减少或破坏生物膜的方法”的发明专利申请的分案申请。
相关申请的交叉引用
本申请要求2004年9月8日提交的名为“防止、去除、减少或破坏生物膜的方法”的美国临时申请(序号60/608,535)的优先权,在此将其并入作为参考。
发明领域
本申请涉及防止、去除、减少或破坏表面上的生物膜生成的方法。
发明背景
生物膜(biofilms)是产生并持续存在于含水环境中的生物或非生物性物体表面上的生物膜,它是微生物细胞吸附到所述固体表面上造成的。这种吸附使这些微生物具有竞争优势,因为它们能够繁殖,能够获得更多样的营养物和氧条件,不被冲走,而且对抗微生物剂的敏感性降低。生物膜的形成还伴随着外泌性(exo-)聚合物质(多糖、聚糖醛酸、藻酸盐、糖蛋白和蛋白质)的产生,其与细胞一道形成由充水的空间分隔的厚层的分化结构。居留的微生物可以是单个物种的微生物细胞,或者是微生物细胞的混合群落,这些微生物细胞可包括好氧和厌氧的细胞,藻类、原生动物,和真菌。因此,生物膜是活的微生物的复杂的集合,这些微生物被包埋在由居留的微生物分泌的一种或多种基质聚合物所构成的有机结构中。
生物膜可发展为厚达数毫米或厘米,并覆盖广大表面区域的宏观结构。这些形成物可能是管道系统中限制或完全阻断流动,热交换器中减少热传递,或在城市供水系统、食品加工、医疗设备(例如导管、整形外科设备、植入物、内窥镜)中造成病原性问题的因素。另外,生物膜通过其包埋的微生物介导的腐蚀作用经常缩短材料的寿命。在工业水处理系统、纸浆和纸生产过程、冷却水系统、油回收用的注入井、冷却塔、多孔介质(砂和土壤)、海洋环境、空调系统,以及任何封闭的水再循环系统中,生物结垢(biologicalfouling)是严重的经济性问题。在医疗科学和工业中,生物膜也是严重的问题,其造成牙垢(dental plaques)、感染(Costerton,1999等人,Science 284:1318-1322),内窥镜和隐形眼镜污染,假体装置的定殖(colonisation),及医用植入物上生物膜的形成。
常规上,去除或防止生物膜需要使用分散剂、表面活性剂、去污剂、酶制剂、抗微生物剂(anti-microbials)、杀生物剂(biocides)、煮沸(boil-out)方法,和/或腐蚀性化学品,例如碱。使用这些手段的方法是本领域公知的。例如,在纸浆和造纸工业中,去除造纸机中的生物膜积聚常规上需要沉积物控制程序(deposit control program),包括合理的保养(housekeeping),以保持表面上没有溅上的原料,对新鲜的水和添加物作抗微生物处理,使用杀生物剂减少机器上的微生物生长,和按方案进行煮沸以去除确实产生的沉积物。
在生物膜中生长的细菌对抗生素和消毒剂的抗性比浮游的细胞更强,而且该抗性随着生物膜的年龄而增加。生物膜还对干燥、极端温度或光显示更高的物理抗性。如已提到的,生物膜的形成造成工业上、环境上和医学上的问题,而且在很多产业中,用化学品清除和消毒细菌生物膜是人们十分关心的问题。另外,消毒和清洁组合物趋向变得更温和,以减轻其环境影响,这样可能使得对覆盖生物膜的表面的清洁更加不足。
本发明的目的是提供防止或去除表面上存在的生物膜的改进的方法。
附图说明
图1显示三种不同的α-淀粉酶对粗小麦淀粉的总水解的百分率(%)的比较。
图2是比较1)α-淀粉酶A;2)单独的去污剂;3)α-淀粉酶C的生物膜去除的色谱图。
发明概述
本发明涉及防止、去除、减少或破坏表面上的生物膜的方法,包括使所述表面与来自细菌的α-淀粉酶接触。
术语“表面”在本文中定义为任何可能被生物膜覆盖或倾向于形成生物膜的表面。表面的例子包括:任何硬表面,例如金属、塑料、橡胶、板、玻璃、木、纸、混凝土、岩石、大理石、石膏和陶瓷材料,这些材料可选地被包被,例如用油漆或瓷漆包被;任何软表面,例如任何种类的纤维(例如纱线、织物、植物纤维、矿棉(rock wool)和毛);或任何多孔表面;皮肤(人或动物的);角质材料(例如甲(nails));和内部器官(例如肺)。所述硬表面可以作为冷却塔、水处理设备、水槽、乳品间(dairy)、食品加工设备、化学或制药过程设备,或医疗装置(例如导管、整形外科装置、植入物)的部分存在。多孔表面可以存在于滤器,例如膜滤器中。
术语“有效量”在本文中定义为足以降解由微生物所产生且包含α-1,4-葡糖苷键的生物膜的一种或多种α-淀粉酶的量。一种或多种α-淀粉酶的有效量依赖于包括下列的因素:所述α-淀粉酶,目标是否是防止、去除或减少表面上存在的生物膜,和用来例如降解微生物产生的生物膜的所希望的时间。一般而言,较高量/浓度的酶需要较短的处理时间,而较低量/浓度的酶需要较长的处理时间。另外,例如,在易于形成生物膜的表面上防止生物膜通常比从相应的污染的表面上实际去除生物膜需要更低量/浓度的酶。但是,典型的有效使用水平是0.005到500mg α-淀粉酶蛋白每升生物膜控制溶液,优选0.01-100mg酶蛋白每升生物膜控制溶液。术语“生物膜控制溶液”是指根据本发明用于防止、去除、减少或破坏表面上存在的生物膜的溶液。以下面实施例4给出的条件下的平均平板计数计,本发明的方法可使生物膜减少到10-108分之一(10-108-fold),优选103-106分之一。
具体地,本发明涉及如下各项:
1.一种防止、去除、减少或破坏表面上存在的生物膜的方法,包括使表面与源自细菌的α-淀粉酶接触。
2.项1的方法,其中所述α-淀粉酶源自芽孢杆菌属的菌株,优选来自芽孢杆菌属菌种NCIB12289,NCIB 12512,NCIB 12513或DSM 9375,或DSMZ no.12649,KSM AP1378,或KSM K36或KSM K38的菌株。
3.项2的方法,其中所述α-淀粉酶源自具有SEQ ID NO:2,4或6中所示序列的芽孢杆菌属菌株,或者与SEQ ID NO:2,4或6具有60%同一性的α-淀粉酶。
4.项2或3的方法,其中所述芽孢杆菌属α-淀粉酶在D183和/或G184位置(SEQ ID NO:2中)具有缺失。
5.项3或4的方法,其中所述芽孢杆菌属α-淀粉酶在N195F位置(SEQID NO:2中)具有取代。
6.项2-5中任一项的方法,其中所述芽孢杆菌属α-淀粉酶在D183+G184位置具有缺失,优选其中所述芽孢杆菌属α-淀粉酶变体还具有一种或多种下列的取代:R118K,N195F,R320K,R458K,特别是其中所述α-淀粉酶具有下面的突变:
Δ(D183+G184)+R118K+N195F+R320K+R458K(在SEQ ID NO:2中)。
7.项1的方法,其中使被生物膜污染或易于产生生物膜的表面接触1分钟到2天。
8.项1到7中任一项的方法,其中还存在表面活性剂。
9.项1到8中任一项的方法,其中所述α-淀粉酶在其N末端氨基酸区域中包含Asn-Gly-Thr-Met-Met-Gln-Tyr-Phe-Glu-Trp。
10.项1到9中任一项的方法,其中所述α-淀粉酶以0.005-500mg酶蛋白,优选0.01-100mg酶蛋白每升生物膜控制溶液的浓度使用。
11.项1到10中任一项的方法,其中所述α-淀粉酶在40℃、3mg酶蛋白每g淀粉、pH 8.0下5小时后,具有高于15,优选25,特别是35的水解淀粉百分率(%)。
12.项1到11中任一项的方法,其中还存在其它的酶,这些酶选自:氨肽酶、淀粉酶、糖酶、羧肽酶、过氧化氢酶、纤维素酶、几丁质酶、角质酶、环糊精糖基转移酶、脱氧核糖核酸酶、酯酶、α-半乳糖苷酶、β-半乳糖苷酶、葡糖淀粉酶、α-葡萄糖苷酶、β-葡萄糖苷酶、卤素过氧化物酶、转化酶、漆酶、脂肪酶、甘露糖苷酶、氧化还原酶、果胶分解酶、肽谷氨酰胺酶、过氧化物酶、肌醇六磷酸酶、多酚氧化酶、蛋白水解酶、核糖核酸酶、转谷氨酰胺酶或木聚糖酶。
13.项12的方法,其中所述果胶分解酶选自果胶反式消除酶(pectintranseliminase)、多聚半乳糖醛酸酶、果胶酯酶。
14.项13的方法,其中所述纤维素酶是多组分纤维素酶制剂或内切葡聚糖酶,优选腐质霉属(Humicola)内切葡聚糖酶,特别是特异腐质霉(Humicolainsolens)内切葡聚糖酶,更优选来自特异腐质霉DSM 1800的EG I或EG V内切葡聚糖酶或其变体或内切葡聚糖酶,优选梭孢壳属(Thielavia)内切葡聚糖酶,优选土生梭孢霉(Thielavia terrestris)内切葡聚糖酶,或其变体。
15.项12的方法,其中所述果胶分解酶是蛋白酶,优选丝氨酸蛋白酶,特别是源自芽孢杆菌属菌株,例如迟缓芽孢杆菌或克劳氏芽孢杆菌(Bacillusclausii),或其变体。
16.项1-15中任一项的方法,其中还存在选自分散剂、表面活性剂、抗微生物剂和杀生物剂的一种或多种试剂。
17.项1-16中任一项的方法,其中所述表面是硬、软或多孔表面。
18.项18的方法,其中所述表面是膜(membrane)。
19.项1-18中任一项的方法,其中所述生物膜去除是在10-70℃,优选40-60℃的温度下进行的。
20.α-淀粉酶在防止或去除表面的生物膜中的用途。
21.项20的用途,其中所述α-淀粉酶是项1-19中任一项定义的α-淀粉酶。
22.项20或21的用途,其中使用项1-19中定义的其它酶和试剂。
发明详述
本发明涉及防止、去除、减少或破坏表面上的生物膜的改进方法,包括使所述表面与如下定义的有效量的α-淀粉酶接触。本发明的方法可以用来防止、去除、减少或破坏表面上的生物膜形成。本领域的一般技术人员将认识到,这样的方法可以在生物膜形成的不同阶段使用。
通过对表面使用有效量的α-淀粉酶,生物膜的防止和/或去除得到了改善,特别是当生物膜中的某些微生物产生α-1,4连接的葡萄糖多糖,例如直链淀粉、支链淀粉、这两种多糖的混合物(例如淀粉)、和糖原时。
本发明的第一个方面涉及一种防止或去除表面上的生物膜的方法,包括使该表面与源自细菌的α-淀粉酶接触。在一个优选的实施方案中,所述细菌α-淀粉酶来自芽孢杆菌属(Bacillus)。
α-淀粉酶
根据本发明所使用的α-淀粉酶来自细菌,优选来自芽孢杆菌属菌种的菌株,特别是选自:WO 00/60060中作为SEQ ID NO:2公开的AA560α-淀粉酶(本文的SEQ ID NO:2),美国专利申请10/877,847中公开的黄热芽孢杆菌,WO 95/26397中公开的芽孢杆菌属菌种的α-淀粉酶,来自芽孢杆菌属菌种NCIB 12289,NCIB 12512,NCIB 12513,DSM 9375,DSMZ no.12649,KSMAP1378(WO 97/00324),KSM K36或KSM K38(EP1022334)的α-淀粉酶,和Tsukamoto等人,Biochemical and Biophysical Research Communications,151(1988),pp.25-31所公开的#707α-淀粉酶。
在本发明的一个优选的具体实施方案中,所述α-淀粉酶是本文SEQ IDNO:2的中所示的AA560α-淀粉酶和/或本文SEQ ID NO:4中所示的AMY1048α-淀粉酶,或与本文SEQ ID NO:2或4所示的任何序列具有至少60%,优选至少70%,更优选至少80%,更优选至少90%,例如至少95%,至少96%,至少97%,至少98%或至少99%的同一性程度的α-淀粉酶。
在一个优选的实施方案中,所用的α-淀粉酶是作为亲本的本文中SEQID NO:2所公开的α-淀粉酶的变体,其在D183和/或G184位置具有缺失,优选其中所述α-淀粉酶变体还含有在N195F位置或相应的位置上具有取代,特别是其中亲本α-淀粉酶在本文SEQ ID NO:2中具有一种或多种下列的缺失/取代:Δ(R81-G182);Δ(D183-G184);Δ(D183-G184)+N195F;R181Q+N445Q+K446N;Δ(D183-G184)+R181Q,Δ(D183-G184)和一种或多种下列的取代:R118K,N195F,R320K,R458K,特别是其中所述亲本α-淀粉酶具有下列突变:
Δ(D183+G184)+R118K+N195F+R320K+R458K(即,在本文的SEQ IDNO:2中)。
在另一个优选的实施方案中,所述α-淀粉酶是SEQ ID NO:2中所示的AA560α-淀粉酶,或其变体,该变体还含有一种或多种下列的取代:M9L,M202L,V214T,M323T,M382Y或M9L,M202L,V214T,M323T和E345R。
在一个优选的实施方案中,所述α-淀粉酶在40℃、3mg酶蛋白每g淀粉,pH8.0下5小时后的水解粗淀粉百分率(%)高于15,优选25,特别是35(见实施例2和图1)。
在另一个优选的实施方案中,所述α-淀粉酶在其N末端氨基酸区域中包含Asn-Gly-Thr-Met-Met-Gln-Tyr-Phe-Glu-Trp。这样的α-淀粉酶的例子包括实施例2中使用的α-淀粉酶A和α-淀粉酶B。
在一个实施方案中所述α-淀粉酶来自地衣芽孢杆菌(Bacilluslicheniformis)的菌株,其序列如本文SEQ ID NO:6所示;或者是与本文SEQID NO:6所示的任何序列具有至少60%,优选至少70%,更优选至少80%,更优选至少90%,例如至少95%,至少96%,至少97%,至少98%或至少99%的同一性程度的α-淀粉酶,优选在对应于M197位的位置上具有取代,优选M197L,T,I,N,D,Q,E,P,W,特别是M197L或T。
可商购的α-淀粉酶产品或包含α-淀粉酶的产品包括以下列商品名出售的产品:STAINZYMETM,DURAMYLTM(Novozymes A/S,丹麦),BIOAMYLASE D(G),BIOAMYLASETM L(Biocon India Ltd.),KEMZYMTMAT 9000(Biozym Ges.m.b.H,奥地利),PURASTARTM ST,PURASTARTMHPAmL,PURAFECTTM OxAm,RAPIDASETM TEX(Genencor Int.Inc,美国),KAM(KAO,日本)。
在优选的实施方案中,可以在生成任何生物膜之前对易于产生生物膜的表面使用本发明的方法作为预防性手段,从而没有生物膜生成。或者,在出现生物膜生成的最初征象时,可以使用所述方法来防止进一步的生成,并去除已经沉积在表面上的生物膜。另外,在表面上积聚了大量生物膜的情况下,可以使用所述方法来降低生物膜的水平,或部分地或全部地去除它。
生物膜可包含一种或两种微生物的整体化的群落,或者主要包含某种特定的微生物(Palmer和White,1997,Trends in Microbiology 5:435-440;Costerton等人,1987,Annual Reviews of Microbiology 41:435-464;Mueller,1994,TAPPI Proceedings,1994 Biological Sciences Symposium 195-201)。在本发明的方法中,所述一种或多种微生物可以是任何参与生物膜形成的微生物,包括但不限于,好氧细菌或厌氧细菌(革兰氏阳性和革兰氏阴性)、真菌(酵母或丝状真菌)、藻类、和/或原生动物。考虑到的细菌包括选自下列的细菌:假单胞菌属(Pseudomonas)的一些种,包括铜绿假单胞菌(Pseudomonasaeruginosa);维涅兰德固氮菌(Azotobacter vinelandii);大肠杆菌(Escherichiacoli);白喉棒杆菌(Corynebacterium diphteriae);肉毒梭菌(Clostridiumbotulinum);链球菌属(Streptococcus)的一些种;醋杆菌属(Acetobacter);明串珠菌属(Leuconostoc);贝塔杆菌属(Betabacterium);肺炎球菌属(Pneumococci);结核分枝杆菌(Mycobacterium tuberculosis);气单胞菌属(Aeromonas);伯克霍尔德氏菌属(Burkholderie);黄杆菌属(Flavobacterium);沙门氏菌属(Salmonella);葡萄球菌属(Staphylococcus)。
在一个优选的实施方案中,所述微生物是好氧细菌。在一个更优选的实施方案中,所述好氧细菌是气单胞菌属菌株。在另一个更优选的实施方案中,所述好氧细菌是伯克霍尔德氏菌属菌株。在另一个更优选的实施方案中,所述好氧细菌是黄杆菌属菌株。在另一个更优选的实施方案中,所述好氧细菌是微杆菌属(Microbacterium)菌株。在另一个更优选的实施方案中,所述好氧细菌是假单胞菌属菌株。在另一个更优选的实施方案中,所述好氧细菌是沙门氏菌属菌株。在另一个更优选的实施方案中,所述好氧细菌是葡萄球菌属菌株。在另一个更优选的实施方案中,所述好氧细菌是来自肠杆菌科(Enterobacteriaceae)(包括例如大肠杆菌)。
在一个最优选的实施方案中,所述好氧细菌为洋葱伯克霍尔德氏菌(Burkholderie cepacia)。在另一个最优选的实施方案中,所述好氧细菌为蛾微杆菌(Microbacterium imperiale)或结核分枝杆菌。在另一个最优选的实施方案中,所述好氧细菌为铜绿假单胞菌。在另一个最优选的实施方案中,所述好氧细菌为荧光假单胞菌(Pseudomonas fluorescens)。在另一个最优选的实施方案中,所述好氧细菌为食油假单胞菌(Pseudomonas oleovorans)。在另一个最优选的实施方案中,所述好氧细菌为类产碱假单胞菌(Pseudomonaspseudoalcaligenes)。在另一个最优选的实施方案中,所述好氧细菌为肠炎沙门氏菌(Salmonella enteritidis)。在另一个最优选的实施方案中,所述好氧细菌为金黄色葡萄球菌(Staphylococcus aureus)。在另一个最优选的实施方案中,所述好氧细菌为表皮葡萄球菌(Staphylococcus epidermidis)。
在另一个优选的实施方案中,所述微生物是厌氧细菌。在另一个更优选的实施方案中,所述厌氧细菌是脱硫弧菌属(Desulfovibrio)菌株。在另一个最优选的实施方案中,所述厌氧细菌是脱硫脱硫弧菌(Desulfovibrio desulfuricans)。
在另一个优选的实施方案中,所述微生物是真菌例如酵母或丝状真菌。在另一个优选的实施方案中,所述酵母是假丝酵母(Candida)菌株。在另一个最优选的实施方案中,所述酵母是白色假丝酵母(Candida albicans)。
如上所述的,防止或去除生物膜的处理时间取决于α-淀粉酶的剂量、表面上的或所述区域倾向形成的生物膜的水平,但优选地,所述处理时间应该与用抗生素、杀生物剂、杀菌剂(bactericides)、杀真菌剂(fungicides)、漂白剂(bleaching agents)、表面活性剂(surfactants)、腐蚀剂(caustic)合伙生物聚合物降解剂进行常规处理所正常使用的时间相适应。因此,α-淀粉酶的剂量可以根据常规处理中所用的时间来调节。但是,当α-淀粉酶处理是加工中的单独的步骤时,α-淀粉酶的剂量取决于完成处理所希望的时间。
从α-淀粉酶活性方面来说,防止或去除生物膜的合适的α-淀粉酶剂量表面上的或所述区域倾向形成的生物膜的量。技术人员可决定合适的α-淀粉酶单位剂量。该剂量可以表示为α-淀粉酶单位。α-淀粉酶单位可作为“KNU”测定,使用下面的“材料和方法”部分描述的测定方法。被生物膜污染的或易于产生生物膜的区域优选以0.005到500mg α-淀粉酶蛋白每升生物膜控制溶液,优选0.01到100mg α-淀粉酶蛋白每升生物膜控制溶液的α-淀粉酶剂量处理1分钟到2天,优选10分钟到1天,优选1到15小时,更优选少于10小时。
所述α-淀粉酶可以是本发明的方法中要使用的组合物的部分。所述组合物可以是任何适于所述用途的形式,例如,干粉、聚结粉末(agglomeratedpowder),或颗粒(granulate),特别是非粉化(non-dusting)颗粒,液体,特别是稳定化的液体,或被保护的α-淀粉酶。颗粒和聚结粉末可以用常规方法制备,例如通过在流化床制粒机中将α-淀粉酶喷雾到载体上。所述载体可由具有合适粒度的颗粒物核心(particulate core)组成。载体可以是可溶的或不可溶的,例如,盐(例如氯化钠或硫酸钠),糖(例如蔗糖或乳糖),糖醇(例如山梨糖醇),或淀粉。α-淀粉酶可包含于缓释制剂中。制备缓释制剂的方法是本领域公知的。液体α-淀粉酶制备可以,例如,根据已建立的方法,通过加入营养上可接受的稳定剂诸如糖、糖醇或另一多元醇,和/或乳酸或另一有机酸来稳定化。
该组合物还可添加一种或多种防止或去除生物膜生成的药剂。这些药剂可包括,但不限于,分散剂、表面活性剂、去污剂、其它的酶,抗微生物剂,和杀生物剂。
在一个优选的实施方案中,所述药剂是表面活性剂。所述表面活性剂可以是非离子型包括半极性和/或阴离子型和/或两性离子型的表面活性剂。
所考虑的阴离子表面活性剂包括线性苯磺酸烷基酯、α-烯属磺酸酯、硫酸烷基酯(脂肪醇硫酸酯)、脂肪醇乙氧基硫酸盐、二级链烷磺酸盐、α-磺基脂肪酸甲酯、烷基或烯基琥珀酸或肥皂。
所考虑的非离子表面活性剂包括脂肪醇乙氧基化物、壬基苯酚乙氧基化物、烷基多苷、烷基二甲基胺氧化物、乙氧基化脂肪酸单乙醇胺、脂肪酸单乙醇胺、多羟基烷基脂肪酰胺、或葡糖胺(“葡萄糖胺”(“glucamides”))的N-酰基N-烷基衍生物。
表面活性剂的可以以所述酶生物膜去除组合物的重量的0.1%到60%的水平存在。
在更优选的实施方案中,所述表面活性剂是十二烷基硫酸钠、季铵化合物、溴化烷基吡啶(alkyl pyridinium iodides),Tween 80,Tween,85,TritonX-100,Brij 56,生物表面活性剂、鼠李糖脂、表面活性蛋白、visconsin或磺酸盐或酯(sulfonates)。
生物膜的形成还伴随产生外泌性聚合物质(多糖、聚糖醛酸、藻酸盐、糖蛋白和蛋白质),其与细胞一道形成由充水的空间分隔的厚层的分化结构(McEldowney和Fletcher,1986,Journal of General Microbiology 132:513-523;Sutherland,Surface Carbohydrates of the Prokaryotic Cell,Academic Press,New York,1977,pp.27-96)。在本发明的方法中,所述α-淀粉酶组合物可以还包含一种或多种能够降解所述外泌性聚合物质例如多糖、聚糖醛酸、藻酸盐、糖蛋白和蛋白质的其它的酶。
其它的酶活性
在一个优选的实施方案中,所述一种或多种其它的酶可选自氨肽酶、淀粉酶、糖酶、羧肽酶、过氧化氢酶、纤维素酶、几丁质酶、角质酶、环糊精糖基转移酶、脱氧核糖核酸酶、酯酶、α-半乳糖苷酶、β-半乳糖苷酶、葡糖淀粉酶、α-葡萄糖苷酶、β-葡萄糖苷酶、卤素过氧化物酶、转化酶、氧化酶,包括糖氧化酶、过氧化物酶、漆酶、脂肪酶、甘露糖苷酶、果胶分解酶、肽谷氨酰胺酶、肌醇六磷酸酶、多酚氧化酶、蛋白水解酶、核糖核酸酶、转谷氨酰胺酶或木聚糖酶。
所述其它的酶可根据要去除的特定生物膜的性质来选择,或者可以选择具有不同酶活性的数种酶的组合。
在优选的实施方案中,所述其它酶选自:1,2-1,3-α-D-甘露聚糖甘露糖水解酶(1,2-1,3-alpha-D-mannan mannohydrolase),1,3-β-D-木聚糖木聚糖水解酶(1,3-beta-D-xylan xylanohydrolase),1,3-β-D-葡聚糖葡聚糖水解酶(1,3-beta-D-glucan glucanohydrolase),1,3(1,3;1,4)-α-D-葡聚糖3-葡聚糖水解酶(1,3(1,3;1,4)-alpha-D-glucan 3-glucanohydrolase),1,3(1,3;1,4)-β-D-葡聚糖3(4)-葡聚糖水解酶(1,3(1,3;1,4)-beta-D-glucan 3(4)-glucanohydrolase),1,3-1,4-α-D-葡聚糖4-葡聚糖水解酶(1,3-1,4-alpha-D-glucan4-glucanohydrolase),1,4-α-D-葡聚糖葡聚糖水解酶(1,4-alpha-D-glucanglucanehydrolase),1,4-α-D-葡聚糖葡萄糖水解酶(1,4-alpha-D-glucanglucohydrolase),1,4-(1,3:1,4)-β-D-葡聚糖4-葡聚糖水解酶(1,4-(1,3:1,4)-beta-D-glucan 4-glucanohydrolase),1,4-β-D-葡聚糖葡萄糖水解酶(1,4-beta-D-glucan glucohydrolase),1,4-β-D-木聚糖木聚糖水解酶(1,4-beta-D-xylan xylanohydrolase),1,4-β-D-甘露聚糖甘露聚糖水解酶(1,4-beta-D-mannan mannanohydrolase),1,5-α-L-阿聚糖1,5-α-L-阿聚糖水解酶(1,5-alpha-L-arabinan 1,5-alpha-L-arabinanohydrolase),1,4-α-D-葡聚糖麦芽糖水解酶(1,4-alpha-D-glucan maltohydrolase),1,6-α-D-葡聚糖6-葡聚糖水解酶(1,6-alpha-D-glucan 6-glucanohydrolase),2,6-β-D-果聚糖果聚糖水解酶(2,6-beta-D-fructan fructanohydrolase),α-糊精6-葡聚糖水解酶(alpha-Dextrin6-glucanohydrolase),α-D-半乳糖苷半乳糖水解酶(alpha-D-galactosidegalactohydrolase),α-D-葡糖苷葡萄糖水解酶(alpha-D-glucosideglucohydrolase),α-D-甘露糖苷甘露糖水解酶(alpha-D-mannosidemannohydrolase),酰基神经氨酰水解酶(acylneuraminyl hydrolase),气杆菌(Aerobacter)-荚膜多糖半乳糖水解酶(Aerobacter-capsular-polysaccharidegalactohydrolase),β-D-呋喃果糖苷果糖水解酶(beta-D-fructofuranosidefructohydrolase),β-D-岩藻糖苷岩藻糖水解酶(beta-D-fucoside fucohydrolase),β-D-果聚糖果糖水解酶(beta-D-fructan fructohydrolase),β-D-半乳糖苷半乳糖水解酶(beta-D-galactoside galactohydrolase),β-D-葡糖苷葡萄糖水解酶(beta-D-glucoside glucohydrolase),β-D-葡糖醛酸苷葡糖醛酸苷水解酶(beta-D-glucuronoside glucuronosohydrolase),β-D-甘露糖苷甘露糖水解酶(beta-D-mannoside mannohydrolase),β-N-乙酰-D-氨基己糖苷N-乙酰己糖胺水解酶(beta-N-acetyl-D-hexosaminide N-acetylhexosamino hydrolase,),硫酸纤维素磺基水解酶(cellulose-sulfate sulfohydrolase),胶原酶(collagenase),糊精6-α-D-葡聚糖水解酶(dextrin 6-alpha-D-glucanohydrolase),糖蛋白-磷脂酰肌醇磷脂酰水解酶(glycoprotein-phosphatidylinositol phosphatidohydrolase),透明质酸4-聚糖水解酶(hyaluronate 4-glycanohydrolase),透明质酸葡糖醛酸糖苷酶(hyaluronoglucuronidase),果胶果胶酰水解酶(pectin pectylhydrolase),肽聚糖N-乙酰胞壁酰水解酶(peptidoglycan N-acetylmuramoylhydrolase),磷脂酰胆碱2-酰基水解酶(phosphatidylcholine 2-acylhydrolase),磷脂酰胆碱1-酰基水解酶(phosphatidylcholine 1-acylhydrolase),聚(1,4-α-D-半乳糖醛酸苷)半乳糖醛酸水解酶(poly(1,4-alpha-D-galacturonide),聚(1,4-(N-乙酰-β-D-氨基葡糖苷))-聚糖水解酶poly(1,4-(N-acetyl-beta-D-glucosaminide))-glycanohydrolase),蔗糖α-葡糖苷酶(sucrose alpha-glucosidase),三酰基甘油酰基水解酶(triacylglycerol acylhydrolase),和三酰基甘油蛋白酰基水解酶(triacylglycerol protein-acylhydrolase)。
蛋白水解酶(proteolytic enzyme)
所述其它酶可以是任何在实际过程条件下具有蛋白水解活性的酶。因此,所述酶可以是植物来源的蛋白水解酶,例如木瓜蛋白酶,菠萝蛋白酶,无花果蛋白酶,或动物来源的蛋白水解酶,例如胰蛋白酶和胰凝乳蛋白酶,或微生物来源,即细菌、酵母或丝状真菌来源的蛋白水解酶。应当理解,多种蛋白水解酶中的任何混合物都可适用于本发明的过程。
在另一个优选的实施方式中,所述其它酶是蛋白水解酶,例如丝氨酸蛋白酶、金属蛋白酶或天冬氨酸蛋白酶。
丝氨酸蛋白酶的一个亚类通常被称为枯草蛋白酶(subtilisins)。枯草蛋白酶是革兰氏阳性细菌或真菌产生的丝氨酸蛋白酶。已经测定了多种枯草蛋白酶的氨基酸序列,包括至少6种来自芽孢杆菌属菌株的枯草蛋白酶,即:枯草蛋白酶168,枯草蛋白酶BPN,枯草蛋白酶Carlsberg,枯草蛋白酶DY,枯草蛋白酶amylosacchariticus,和mesentericopeptidase,一种来自放线菌目(actinomycetales)的枯草蛋白酶,来自普通高温放线菌(Thermoactinomycesvulgaris)的thermitase,和一种真菌枯草蛋白酶,来自Tritirachium album的蛋白酶K。Subtilases是更新近被承认的枯草蛋白酶的另一亚类。Subtilases被描述为高度碱性的枯草蛋白酶,包括例如枯草蛋白酶PB92(Gist-Brocades NV),枯草蛋白酶309(Novozymes A/S),和枯草蛋白酶147(Novozymes A/S)。
“枯草蛋白酶变体或突变的枯草蛋白酶蛋白酶”在本文中定义为由表达来自亲本微生物的突变基因的生物体产生的枯草蛋白酶,所述亲本微生物具有原基因或称亲本基因并产生相应的亲本酶,所述亲本基因已经被突变以产生突变基因,该突变基因在合适的宿主中表达时,产生所述突变的枯草蛋白酶蛋白酶。这些被提到的枯草蛋白酶和其变体构成在本发明的方法中有用的优选蛋白酶类群。有用的枯草蛋白酶变体的例子有枯草蛋白酶309变体其中在195位上甘氨酸被取代为苯丙氨酸(G195F或195Gly到195Phe)。
本发明的方法中可使用可商购的蛋白酶。这样的商品化蛋白酶的例子有(地衣芽孢杆菌菌株深层发酵生产的),(芽孢杆菌属的嗜碱性菌种深层发酵生产的),(Mucor miehei的非病原性菌株深层发酵生产的),(遗传修饰的芽孢杆菌属菌株深层发酵生产的),例如在公开的国际专利申请WO 92/19729中披露的变体,以及(的蛋白质工程变体),POLARZYMETM,和EVERLASETM。上述所有的商品化蛋白酶都可以从Novozymes A/S,DK-2880Bagsvaerd,丹麦获得。
其它优选的丝氨酸蛋白酶有来自曲霉属(Aspergillus)、芽孢杆菌属例如嗜碱芽孢杆菌(Bacillus alcalophilus)、蜡状芽孢杆菌(Bacillus cereus)、Bacillusvulgatus、蕈状芽孢杆菌(Bacillus mycoide)和根霉属(Rhizopus)的蛋白酶,和来自芽孢杆菌属的枯草蛋白酶,特别是来自拟诺卡氏菌属(Nocardiopsis)菌种,例如Nocardiopsis natto和达松维尔拟诺卡氏菌(Nocardiopsis dassonvillei)(参见WO 88/03947),特别是来自拟诺卡氏菌属菌种NRRL 18262和达松维尔拟诺卡氏菌NRRL 18133的蛋白酶。其它优选的蛋白酶有来自国际专利申请PCT/DK89/00002和WO 91/00345中公开的芽孢杆菌属枯草蛋白酶的突变体的丝氨酸蛋白酶,和EP 415296中公开的蛋白酶。
另一类优选的蛋白酶是微生物来源的金属蛋白酶。本发明中可以使用常规的发酵的商品化金属蛋白酶,例如(Zn)(由枯草芽孢杆菌(Bacillus subtilis)的菌株深层发酵生产),可获自Novozymes A/S,DK-2880Bagsvaerd,丹麦;WO和SI,可获自Sandoz AG,Basle,瑞士;可获自Toyo Boseki Co.Ltd.,日本;及(由芽孢杆菌属菌种KSM-K16的菌株深层发酵生产),可获自Kao Corporation Ltd.,日本。
该蛋白酶可以0.005到500mg酶蛋白每升生物膜控制溶液,优选0.01到100mg酶蛋白每升生物膜控制溶液的剂量使用。
脂肪酶
在另一优选的实施方案中,所述其它酶是脂肪酶,特别是微生物脂肪酶。就此而言,所述脂肪酶可选自酵母,例如假丝酵母;细菌,例如假单胞菌或芽孢杆菌;或丝状真菌,例如腐质霉属(Humicola)或根毛霉属(Rhizomucor)。更具体地,合适的脂肪酶可以是Rhizomucor miehei脂肪酶(例如,如EP 238 023描述地制备的),Thermomyces lanuginosa脂肪酶,例如按EP 305 216的描述制备的,特异腐质霉脂肪酶,施氏假单胞菌(Pseudomonas stutzeri)脂肪酶,洋葱假单胞菌(Pseudomonas cepacia)脂肪酶、Candida antarctica脂肪酶A或B,或来自rGPL,Absidia blakesleena,伞枝犁头霉(Absidia corymbifera),茄病镰孢(Fusarium solani),尖孢镰孢(Fusarium oxysporum),圆弧青霉(Penicillumcyclopium),皮落青霉(Penicillum crustosum),扩展青霉(Penicillum expansum),Rhodotorula glutinis,Thiarosporella phaseolina,小孢根霉(Rhizopusmicrosporus),Sporobolomyces shibatanus,出芽短柄霉(Aureobasidiumpullulans),异常汉逊氏酵母(Hansenula anomala),Geotricum penicillatum,弯曲乳杆菌(Lactobacillus curvatus),热杀索丝菌(Brochothrix thermosohata),Coprinus cinerius,Trichoderma harzanium,Trichoderma reesei,日本根霉(Rhizopus japonicus),或植物假单胞菌(Pseudomonas plantari)的脂肪酶。其它合适的脂肪酶的例子可以是上面提到的任何一种脂肪酶的变体,例如WO92/05249或WO 93/11254中描述的。
可商购的脂肪酶的例子包括:LIPOLASETM,LIPOLASE ULTRATM,LIPOPRIMETM,和LIPEXTM,来自Novozymes,丹麦。
所述脂肪酶可以使用的剂量为0.005到500mg酶蛋白每升生物膜控制溶液,优选0.01-100mg酶蛋白每升生物膜控制溶液。
纤维素酶
在另一个优选的实施方案中,所述其它酶是纤维素酶(cellulase)或纤维素水解酶(cellulolytic enzyme),其指催化纤维素降解为葡萄糖、纤维二糖、三糖和其它纤维寡糖(cellooligosaccharides)的酶。优选地,所述纤维素酶是内切葡聚糖酶(endoglucanase),更优选微生物内切葡聚糖酶,特别是细菌或真菌内切葡聚糖酶。细菌内切葡聚糖酶的例子有从选自假单胞菌属的细菌或灿烂芽孢杆菌(Bacillus lautus)得到的或可由其产生的内切葡聚糖酶。
纤维素酶或内切葡聚糖酶可以是酸性、中性或碱性的纤维素酶或内切葡聚糖酶,即,分别在酸性、中性或碱性的pH范围表现最大的纤维素水解活性。因此,有用的纤维素酶或内切葡聚糖酶是酸性纤维素酶或内切葡聚糖酶,优选真菌酸性纤维素酶或内切葡聚糖酶,更优选在酸性条件下具有显著的纤维素水解活性的真菌酸性纤维素酶或内切葡聚糖酶,其中所述酶是从选自木霉属(Trichoderma)、放线菌属(Actinomyces)、漆斑菌属(Myrothecium)、曲霉属和葡萄孢属(Botrytis)的真菌得到或可由其产生的。
优选的酸性纤维素酶或内切葡聚糖酶是从由黑曲霉(Aspergillus niger),米曲霉(Aspergillus oryzae)、灰色葡萄孢(Botrytis cinerea),疣孢漆斑菌(Myrothecium verrucaria),长枝木霉(Trichoderma longibrachiatum),里氏木霉(Trichoderma reesei),和绿色木霉(Trichoderma viride)构成的组得到的。
另一种有用的纤维素酶或内切葡聚糖酶是中性或碱性纤维素酶或内切葡聚糖酶,优选真菌中性或碱性纤维素酶或内切葡聚糖酶,更优选在中性或碱性条件下具有显著的纤维素水解活性的真菌中性或碱性纤维素酶或内切葡聚糖酶,其中所述酶从选自支顶孢属(Acremonium)、曲霉属、毛壳霉属(Chaetomium)、头孢属(Cephalosporium)、镰孢属(Fusarium)、胶霉属(Gliocladium)、腐质霉属、耙菌属(Irpex)、毁丝霉属(Myceliophthora)、疣孢霉属(Mycogone),漆斑菌属,丝葚霉属(Papulospora),青霉属(Penicillium),帚霉属(Scopulariopsis),葡萄穗霉属(Stachybotrys),和轮枝孢属(Verticillium)的真菌获得或可由其产生。
优选的碱性纤维素酶或葡聚糖酶是从头孢属的菌种、尖孢镰孢,特异腐质霉,或Myceliopthora thermophila,或优选从头孢属菌种RYM-202,Fusarium oxysporum,DSM 2672,特异腐质霉,DSM 1800,或Myceliopthorathermophila,CBS 117.65获得的。
在另一个优选的实施方案中,所述其它酶是木聚糖酶,例如内切1,3-β-木糖苷酶(endo-1,3-β-xylosidase)(EC 3.2.1.32),木聚糖1,4-β-木糖苷酶(xylan1,4-β-xylosidase)(EC 3.2.1.37),和α-L-阿拉伯呋喃糖苷酶(α-L-arabinofuranosidase)(EC 3.2.1.55)。优选地,所述木聚糖酶选自Aspergillusaculeatus(一种表现木聚糖酶活性的酶,该酶与针对来自Aspergillus aculeatusCBS 101.43的纯化的木聚糖酶的抗体有免疫反应性,参见例如WO 94/21785);米曲霉(参见例如SU 4610007);出芽短柄霉(参见例如EP 0 373 107 A2);环状芽孢杆菌(Bacillus circulans)(WO 91/18978);短小芽孢杆菌(Bacillus pumilus)(参见例如WO 92/03540);嗜热脂肪芽孢杆菌(Bacillus stearothermophilus)(参见例如WO 91/18976,WO 91/10724);芽孢杆菌属菌种AC13(特别是NCIMB40482菌株,参见例如WO 94/01532);特异腐质霉(参见例如WO 92/17573);红嗜热盐菌属(Rhodothermus)(参见例如WO 93/08275);浅青紫链霉菌(Streptomyces lividans)(参见例如WO 93/03155);绿孢链霉菌(Streptomycesviridosporus)(参见例如EP 496 671 A);地衣芽孢杆菌(参见例如JP 9213868);橙色热子囊菌(Thermoascus aurantiacus)(参见例如美国专利4,966,850);Trichoderma longibrachiatum和Chainia属的菌种(参见例如EP 0 353 342 A1);Trichoderma harzianum and Trichoderma reseei(参见例如美国专利4,725,544);Thermomyces lanuginosus(参见例如EP 0 456 033 A2);褐色热单胞(Thermomonospora fusca)(参见例如EP 0 473 545 A2);Trichodermalongibrachiatum(参见W.J.J.van den Tweel等编,Stability of Enzymes,Proceedings of an International Symposium held in Maastrich,The Netherlands,1992.11.22-25,Fisk,R.S.和Simpson,pp.323-328);网球菌属(Dictyoglomus)(参见例如WO 92/18612);链霉菌属(Streptomyces)(参见例如美国专利5,116,746);和/或栖热袍菌属(Thermotoga)(参见例如WO 93/19171)。其它合适的木聚糖酶的例子有上述任一种酶具有木聚糖水解活性的变体(衍生物或同源物)。
可商购的含纤维素酶产品的例子包括:NOVOZYMTM 342,CELLUZYMETM,CAREZYMETM,RENOZYMETM(都来自Novozymes,丹麦)。
该纤维素酶可以0.005到500mg酶蛋白每升生物膜控制溶液,优选0.01到100mg酶蛋白每升生物膜控制溶液的剂量使用。
果胶酶
在另一优选的实施方案中,所述其它的酶是果胶酶,例如多聚半乳糖醛酸酶(polygalacturonase)(EC 3.2.1.15)、果胶酯酶(pectinesterase)(EC 3.2.1.11),或胶质裂合酶(pectin lyase)(EC4.2.2.10)。果胶酶的合适的来源生物可以是黑曲霉。
在另一个优选的实施方案中,所述α-淀粉酶组合物中的其它酶包括由真菌棘孢曲霉(Aspergillus aculeatus),优选棘孢曲霉,CBS 101.43所产生的水解性酶的组合物。已知该菌株产生包含果胶分解(pectinolytic)和多种半纤维素分解(hemicellulolytic)酶活性。
可商购的含果胶酶的产品的例子包括:BioPrepTM,SCOURZYMETM和PECTAWASHTM(Novozymes,丹麦)。
该果胶酶可以0.005到500mg酶蛋白每升生物膜控制溶液,优选0.01到100mg酶蛋白每升生物膜控制溶液的剂量使用。
氧化还原酶
在本发明的另一实施方案中,所述α-淀粉酶与氧化还原酶,例如氧化酶、过氧化物酶或漆酶组合。
a)漆酶作用于分子氧,产生水(H2O),而不需任何过氧化物(例如H2O2),
b)氧化酶作用于分子氧,产生过氧化物(H2O2),
c)过氧化物酶作用于过氧化物(例如H2O2),产生水(H2O)。
漆酶(E.C.1.10.3.2)的例子包括来自多孔菌属(Polyporus)菌种的菌株,特别是Polyporus pinsitus或变色多孔菌(Polyporus versicolor)的菌株,或毁丝霉属菌种的菌株,特别是M.thermophila,Scytalidium属菌种的菌株,特别是S.thermophilium,丝核菌(Rhizoctonia)属菌种的菌株,特别是Rhizoctoniapraticola或茄属丝核菌(Rhizoctonia solani),或Rhus属菌种的菌株,特别是Rhus vernicifera。所述漆酶还可以来自真菌例如金钱菌属(Collybia),层孔菌属(Fomes),香菇属(Lentinus),灰侧耳菌属(Pleurotus),曲霉属,脉孢霉属(Neurospora),Podospora属,射脉菌属(Phlebia),例如辐射射脉菌(P.radiata)(WO 92/01046),革盖菌属(Coriolus)的菌种,例如毛革盖菌(C.hirsitus)(JP2-238885),或葡萄孢属。
在具体考虑的实施方案中,所述漆酶可以选自WO 96/00290中描述的Polyporus pinisitus漆酶(也称为Trametes villosa漆酶),WO 95/33836中描述的Myceliophthora thermophila漆酶,WO 95/33837中描述的Scytalidiumthermophilium漆酶,可从SIGMA购买的商品名为SIGMA no.L5510的Pyricularia oryzae漆酶,WO 96/06930中描述的Coprinus cinereus漆酶,及WO 95/07988中描述的茄属丝核菌漆酶。
过氧化物酶(1.11.1.7)的例子包括来自植物的过氧化物酶(例如辣根过氧化物酶)或来自微生物的过氧化物酶,包括真菌和细菌,例如Coprinus属菌种,诸如Coprinus cinereus或Coprinus macrorhizus的菌株,或细菌,例如芽孢杆菌属,诸如短小芽孢杆菌。
在特别考虑的实施方案中,所述过氧化物酶可选自:WO 95/10602中公开的Coprinus cinereus IFO8371过氧化物酶或其变体,以及来源于WO97/04102中描述的Curvularia verruculosa CBS 147.63菌株的卤素过氧化物酶(haloperoxidase)。
考虑到的氧化酶特别包括糖氧化酶(carbohydrate oxidases),这些酶被归类为EC 1.1.3。糖氧化酶包括葡萄糖氧化酶(E.C.1.1.3.4),己糖氧化酶(E.C.1.1.3.5),木糖醇氧化酶,半乳糖氧化酶(E.C.1.1.3.9),吡喃糖氧化酶(E.C.1.1.3.10),醇氧化酶(E.C.1.1.3.13)。
糖氧化酶可来自任何来源,包括细菌、真菌、酵母或哺乳动物来源。
葡萄糖氧化酶的例子包括来自曲霉属的菌种,例如黑曲霉的菌株,或来自Cladosporium属的菌种,尤其是Cladosporium oxysporum,特别是WO95/29996中描述的Cl.oxysporum CBS 163的葡萄糖氧化酶。
己糖氧化酶的例子包括由红色海藻Chondrus crispus(通常称为角叉菜(Irish moss)产生的己糖氧化酶(Sullivan和Ikawa,(1973),Biochim.Biophys.Acts,309,p.11-22;Ikawa,(1982),Meth.in Enzymol.89,carbohydratemetabolism part D,145-149),其氧化广谱的糖类,以及产生容易提取的己糖氧化酶的红色海藻Iridophycus flaccidum所产生的己糖氧化酶,其氧化数种不同的单糖和双糖(Bean和Hassid,(1956),J.Biol.Chem,218,p.425;Rand等,(1972),J.of Food Science 37,p.698-710)。
该氧化还原酶可以0.005到500mg酶蛋白每升生物膜控制溶液,优选0.01到100mg酶蛋白每升生物膜控制溶液的剂量使用。
本发明的最后一方面涉及使用芽孢杆菌α-淀粉酶来防止、去除、减少或破坏表面上的生物膜生成物。在一个优选的实施方案中,所述α-淀粉酶是芽孢杆菌α-淀粉酶,优选上面的“α-淀粉酶”部分提到的α-淀粉酶。
下面的实施例对本发明进行进一步的说明,它们不应被理解为对本发明范围的限制。
材料和方法
作为缓冲剂和试剂使用的化学品都是商品化的产品,至少为试剂级。
酶:
α-淀粉酶-A是作为亲本的WO 00/60060的SEQ ID NO:2所描述的芽孢杆菌属菌种的α-淀粉酶的变体。所述α-淀粉酶的氨基酸序列具有下面6个氨基酸缺失/取代:
D183*+G184*+R118K+N195F+R320K+R458K。
该变体在WO 01/66712也有公开。该碱性α-淀粉酶以批号03AGE014-4生产。
α-淀粉酶B来自黄热芽孢杆菌菌株,并在SEQ ID NO:4中公开。
α-淀粉酶C来自地衣芽孢杆菌菌株,并在WO 99/19467的SEQ ID NO:6中显示。
蛋白酶E是克劳氏芽孢杆菌(Bacillus clausii)(旧名:迟缓芽孢杆菌(Bacillus lentus)C360=NCIB 10309)的一种枯草蛋白酶,具有取代M222S,并被EP专利396,608-B1所覆盖(可从Novozymes,丹麦索取)。
脂肪酶A是源自疏棉状腐质霉(Humicola lanuginosa)菌株DSM 4109的脂肪酶变体,其具有下列突变:T231R,N233R,公开于美国专利6,939,702-B(可从Novozymes索取)。
纤维素酶A是来自特异腐质霉的多组分纤维素酶(可从Novozymes索取)。
细菌菌株
得自ATCC 10774的枯草芽孢杆菌
大肠杆菌ATCC#11229和ATCC#25922
生物膜培养基根据供应商的指导制备胰胨豆胨肉汤(Tryptic SoyBroth,TSB,购自VWR,P/N DF0370-07)培养基,再用水稀释到5%。每升加入2ml微量元素。
琼脂根据供应商的指导使用胰胨豆胨琼脂(Tryptic Soy Agar,TSA,购自VWR,P/N DF0369-17)。
微量元素溶液每升:1.5g CaCl2,1.0g FeSO4·7H2O,0.35g MnSO4.2H2O,0.5g NaMoO4
不锈钢试片(coupons)不锈钢试片No.304自Metal Samples Company(Munford,AL)获得。
BioLC离子色谱系统该IC系统由下列组件构成:
GP50梯度泵(P/N 059493)
ED50A电化学检测器(P/N 059499)
AS50温控自动进样器(P/N 056565)
用于积分电流检测(Integrated Amperometry)的电化学检测池(Electrochemical Cell),备全了金电极和Ag/AgCl参比电极(P/N 060386)
Chromelion数据控制软件CHM-1-IC (P/N 060930)
CDC生物膜反应器:购自Biosurface Technologies,Inc.(P/N CBR 90-2),备全了聚碳酸盐试片(每个反应器24个,P/N RD 128-PC)。
去污剂清洁基料(Detergent Cleaner Base),得自Weiman Products(IL,美国),品名为Burnishine ME-多酶去污剂。在使用前通过微波炉高档位(highsetting)加热1分钟来使酶变性。
方法:
α-淀粉酶活性(KNU)
可使用马铃薯淀粉作为底物测定淀粉水解活性。该方法基于酶降解变性的(modified)马铃薯淀粉,通过将淀粉/酶溶液的样品与碘溶液混合来追踪该反应。开始,生成蓝黑色,但在淀粉降解的过程中蓝色变弱,并逐渐变成红棕色,将其与有色玻璃标准比较。
1千Novo α-淀粉酶单位(KNU)定义为在标准条件下(即37°C+/-0.05;0.0003M Ca2+;pH 5.6)糊精化(dextrinize)5260mg的Merck Amylum solubile淀粉干物质的酶量。
更详细地描述这种分析方法的小册子EB-SM-0009.02/01可从Novozymes A/S,丹麦索取,在此将该小册子并入本文作为参考。
两个序列之间的同一性程度的确定
为了本发明的目的,可以通过Clustal方法(Higgins,1989,CABIOS 5:151-153)确定两个氨基酸序列间的同一性程度,其中上述方法使用的是LASERGENETM MEGALIGNTM软件(DNASTAR,Inc.,Madison,WI),该软件带有同一性列表以及以下多个比对参数:空位罚分(gap penalty)10,空位长度罚分(gap length penalty)10。配对比对参数如下:Ktuple=1,空位罚分=3,windows=5,diagonals=5。
实施例
实施例1
使用α-淀粉酶A和α-淀粉酶C去除生物膜
生物膜反应器由400ml烧杯、磁力搅拌器和2个不锈钢试片(coupon)组成。将试片垂直地用胶带固定(taped)在烧杯的壁上,并使试片的底边落在烧杯的底上。加入搅拌子,用圆形铝箔覆盖烧杯并高压蒸汽灭菌。向每个烧杯中加入200ml无菌的生物膜培养基。为了培养接种物,将每种细菌菌株(来自枯草芽孢杆菌)在平板计数琼脂(plate count agar)上28℃培养过夜。用无菌的拭子将每种菌株悬浮在无菌水中至OD686为0.100,然后进一步稀释至10-1。每个测试由4个没有酶的对照烧杯、2个具有50mg酶蛋白每升溶液的烧杯,和2个具有100mg酶蛋白每升溶液的烧杯组成。首先在37℃搅拌下将烧杯温育过夜以在不锈钢试片上生长生物膜。该温育步骤后,以上述的2种剂量按照下表加入酶,在40℃下再温育2小时。然后,用无菌水小心地洗涤每个烧杯和不锈钢试片,用结晶紫染色,用无菌水清洗,用乙酸溶解残余的生物膜,然后用分光光度计在600nm下测量等份的每种溶液的吸光度。所测得的这些溶液的吸光度直接地指示不锈钢试片上残余的生物膜的量。低的吸光度对应于酶的效用良好,几乎没有生物膜残余;高的吸光度对应于酶的效用差(或没有),有显著的生物膜残余。
样品# | 所用的酶 | 酶蛋白浓度 |
1 | α-淀粉酶A | 50mg每L和100mg每L |
2 | α-淀粉酶C | 50mg每L&100mg每L |
3 | 无酶(对照) | NA |
实施例2
使用α-淀粉酶A、B和C溶解粗淀粉
测量不同的α-淀粉酶溶解粗的(raw)、非水化的(unhydrated)小麦淀粉的速率。该研究中分别使用α-淀粉酶A、B和C。
将具有pH 8Tris缓冲液、15°dH的1%粗小麦淀粉溶液25毫升倒入带盖的管中,放在40℃水浴中。在加入酶之前,测量“还原端”(reducing ends)的初始水平。该研究中所用的酶浓度为3mg酶蛋白每g粗小麦淀粉。在不同的时间取出1ml的样品。加入20微升的1M HCl,然后在99℃温育10分钟。酸和热的联合作用使淀粉酶失活。加入20μL的1M NaOH以确保样品不再为酸性。然后将样品稀释,与显色试剂(color reagent)(PHABH,酒石酸钠钾盐,NaOH)在95℃下共同温育10分钟,最后离心,再测量上清在410nm处的OD。将1M HCl中的粗小麦淀粉的1%溶液在110℃的烘箱中温育4小时来制备对照(100%水解的淀粉)。使用该处理来计算每克粗小麦淀粉所能够产生的最大量的葡萄糖。该值在图1所示图表中设为100%。
对α-淀粉酶A和B而言,可见在最初的5小时中观察到的粗小麦淀粉溶解初始速率显著地快于α-淀粉酶C。因此,在整个这段时间中,被前两种α-淀粉酶溶解的淀粉的百分率高于后一种酶。
实施例3
使用α-淀粉酶A和C与蛋白酶E和去污剂组合的生物膜去除
在预先灭菌的CDC生物膜反应器中,在聚碳酸酯试片上生长大肠杆菌(ATCC#11229)的单组分生物膜。在实验的开始,在胰胨豆胨琼脂(TSA)上37℃过夜生长大肠杆菌培养物。次日早晨,用1微升无菌接种环从平板上挑取单菌落,加到40g TSB每升水的溶液中。将该溶液在37℃培养过夜,使培养物长起。第二天,将1毫升的该培养物加到CDC生物膜反应器中所含的400ml的基础培养基(0.30g TSB每升无菌水)中。以130rpm缓慢地搅拌该溶液,并以非补料分批模式在22℃下生长2天。2天的生长期后,将试片固定杆(holder rods)和试片从反应器移出,在无菌的稀释水中洗去浮游的细胞,从杆上小心地移下试片,并在40℃下,在下列溶液中(每种30毫升)温育1小时:
A:单独的去污剂清洁基料,0.21g去污剂,于无菌水中。
B:去污剂清洁基料,0.21g+0.51mg酶蛋白的蛋白酶E+0.06mg酶蛋白的α-淀粉酶A。
C:去污剂清洁基料,0.21g+0.51mg酶蛋白的蛋白酶E+0.16mg酶蛋白的α-淀粉酶C。
在温育步骤后,移去试片。将溶液通过0.45μm尼龙注射器式滤器过滤,并用离子色谱分析其糖含量。并使用PA100保护柱(guard)和分析柱(P/N043055)来分离。用60/40去离子水/100mM NaOH与100%100mM NaOH/1M乙酸钠之间的流动相梯度(指数梯度从进入分离后10分钟开始到85分钟为止)来实现分离。图2显示本实验的3个色谱图的重叠。当使用α-淀粉酶A时,相对于单独的去污剂或使用α-淀粉酶C,生成了显著更高水平的低分子量糖类(葡萄糖=glu,麦芽糖=mal,麦芽三糖=DP3,麦芽四糖=DP4,麦芽五糖=DP5)。这显示通过对大肠杆菌细菌产生的支链淀粉外泌多糖(exopolysaccharides)的降解的增加,生物膜去除的水平增加。
实施例4
使用α-淀粉酶A和C与蛋白酶E、纤维素酶A、脂肪酶A和去污剂组
合的生物膜去除
将两个装有聚碳酸酯试片的CDC生物膜反应器高压灭菌,注入无菌的1/10浓度的胰胨豆胨肉汤(TSB,3g/l的浓度),并接种1ml大肠杆菌(ATCC#25922)的对数期培养物。反应器中的起始细胞计数平均为5×108cfu/mL。将两个反应器都以分批模式在37℃下运行24小时(没有流入或流出)。这段时间以后,开始以12ml/min的流速、37℃连续流加1/10TSB。将大肠杆菌生物膜生长4天。此时,从每个反应器(标为反应器1或2)拉出一个杆,放在含有200毫升下列经过过滤除菌的溶液的烧杯中:
A:单独的去污剂清洁基料,1.4g去污剂,于无菌水中。
B:去污剂清洁基料,1.4g+3.4mg酶蛋白的蛋白酶E+0.48mg酶蛋白的脂肪酶A+0.23mg酶蛋白的纤维素酶A+0.40mg酶蛋白的α-淀粉酶A。
C:去污剂清洁基料,1.4g+3.4mg酶蛋白的蛋白酶E+0.48mg酶蛋白的脂肪酶A+0.23mg酶蛋白的纤维素酶A+0.40mg酶蛋白的α-淀粉酶C。
每个烧杯中的溶液在温和搅拌下40℃温育30分钟,然后用无菌水轻柔地清洗每个杆。最后,用胰胨豆胨琼脂(TSA)对每个杆的3个试片中的2个上的大肠杆菌计数。该研究得到的平均平板计数结果如下:
处理 | 试片上的平均log10cfu/cm2 |
A | 4x107 |
B | 3x104 |
C | 2x105 |
本文所描述并要求保护的发明并不限于本文所公开的具体实施方案,因为这些实施方案意在作为本发明的一些方面来说明。意图将任何等价的实施方案都将包括本发明的范围中。事实上,除了本文中示出并描述的那些以外,本领域的技术人员从前面的描述将显而易见地想到多种对本发明的修改。所附的权利要求也意在将这些修改包括在其范围之内。在冲突的情况下,将以包括定义的本公开为准。
本文引用了多种文献,在此将它们全部的公开并入本文作为参考。
Claims (17)
1.一种防止、去除、减少或破坏表面上存在的生物膜的方法,包括使表面与具有SEQ ID NO:4所示序列的α-淀粉酶或与SEQ ID NO:4具有至少90%同一性的α-淀粉酶接触。
2.权利要求1的方法,其中所述α-淀粉酶来源于芽孢杆菌属菌株。
3.权利要求1或2的方法,其中使被生物膜污染或易于产生生物膜的表面接触1分钟到2天。
4.权利要求1到3中任一项的方法,其中还存在表面活性剂。
5.权利要求1到4中任一项的方法,其中所述α-淀粉酶在其N末端氨基酸区域中包含Asn-Gly-Thr-Met-Met-Gln-Tyr-Phe-Glu-Trp。
6.权利要求1到5中任一项的方法,其中所述α-淀粉酶以0.005-500mg酶蛋白,优选0.01–100mg酶蛋白每升生物膜控制溶液的浓度使用。
7.权利要求1到6中任一项的方法,其中所述α-淀粉酶在40℃、3mg酶蛋白每g淀粉、pH 8.0下5小时后,具有高于15,优选25,特别是35的水解淀粉百分率(%)。
8.权利要求1到7中任一项的方法,其中还存在其它的酶,这些酶选自:氨肽酶、淀粉酶、糖酶、羧肽酶、过氧化氢酶、纤维素酶、几丁质酶、角质酶、环糊精糖基转移酶、脱氧核糖核酸酶、酯酶、α-半乳糖苷酶、β-半乳糖苷酶、葡糖淀粉酶、α-葡萄糖苷酶、β-葡萄糖苷酶、卤素过氧化物酶、转化酶、漆酶、脂肪酶、甘露糖苷酶、氧化还原酶、果胶分解酶、肽谷氨酰胺酶、过氧化物酶、肌醇六磷酸酶、多酚氧化酶、蛋白水解酶、核糖核酸酶、转谷氨酰胺酶或木聚糖酶。
9.权利要求8的方法,其中所述果胶分解酶选自果胶反式消除酶(pectintranseliminase)、多聚半乳糖醛酸酶、果胶酯酶。
10.权利要求9的方法,其中所述纤维素酶是多组分纤维素酶制剂或内切葡聚糖酶,优选腐质霉属(Humicola)内切葡聚糖酶,特别是特异腐质霉(Humicola insolens)内切葡聚糖酶,更优选来自特异腐质霉DSM 1800的EG I或EG V内切葡聚糖酶或其变体或内切葡聚糖酶,优选梭孢壳属(Thielavia)内切葡聚糖酶,优选土生梭孢霉(Thielavia terrestris)内切葡聚糖酶,或其变体。
11.权利要求10的方法,其中所述蛋白水解酶是蛋白酶,优选丝氨酸蛋白酶,特别是源自芽孢杆菌属菌株,例如迟缓芽孢杆菌或克劳氏芽孢杆菌(Bacillus clausii),或其变体。
12.权利要求1-11中任一项的方法,其中还存在选自分散剂、表面活性剂、抗微生物剂和杀生物剂的一种或多种试剂。
13.权利要求1-12中任一项的方法,其中所述表面是硬、软或多孔表面。
14.权利要求13的方法,其中所述表面是膜(membrane)。
15.权利要求1-14中任一项的方法,其中所述生物膜的去除是在10-70℃的温度下进行的,优选40-60℃的温度。
16.权利要求1-15任一项所定义的α-淀粉酶在防止或去除表面的生物膜中的用途。
17.权利要求16的用途,其中使用权利要求1-15任一项中定义的其它酶和/或试剂。
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JP5345781B2 (ja) | 2013-11-20 |
DK2258836T3 (en) | 2016-07-25 |
US20190256803A1 (en) | 2019-08-22 |
EP1791966A2 (en) | 2007-06-06 |
CN103181400B (zh) | 2016-08-10 |
EP2258836B1 (en) | 2016-05-04 |
EP1791966A4 (en) | 2008-12-03 |
CN101040052A (zh) | 2007-09-19 |
CN102919273A (zh) | 2013-02-13 |
US20130217099A1 (en) | 2013-08-22 |
EP2258837A1 (en) | 2010-12-08 |
CN102919273B (zh) | 2016-03-16 |
US20110104141A1 (en) | 2011-05-05 |
US20080248558A1 (en) | 2008-10-09 |
WO2006031554A3 (en) | 2006-09-28 |
US20200181539A9 (en) | 2020-06-11 |
CN103181400A (zh) | 2013-07-03 |
EP2258836A1 (en) | 2010-12-08 |
CN103182387B (zh) | 2016-01-06 |
JP2008512468A (ja) | 2008-04-24 |
WO2006031554A2 (en) | 2006-03-23 |
EP1791966B1 (en) | 2014-06-04 |
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