CN101151081B - 蛋白质作为破乳剂的用途 - Google Patents
蛋白质作为破乳剂的用途 Download PDFInfo
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- CN101151081B CN101151081B CN2006800101415A CN200680010141A CN101151081B CN 101151081 B CN101151081 B CN 101151081B CN 2006800101415 A CN2006800101415 A CN 2006800101415A CN 200680010141 A CN200680010141 A CN 200680010141A CN 101151081 B CN101151081 B CN 101151081B
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Abstract
本发明涉及至少一种蛋白质特别是至少一种疏水蛋白或者至少一种疏水蛋白衍生物的用途,用于改进包含至少两种液相的细合物的相分离;涉及分离包含至少两种液相的组合物中至少两种液相的方法;也涉及包括至少一种化合物和至少一种蛋白质特别是至少一种疏水蛋白或其衍生物的制剂,所述化合物选自燃料、可燃物、原油、水溶性/油溶性聚合物溶液。
Description
发明领域
本发明涉及至少一种疏水蛋白或者至少一种疏水蛋白衍生物的用途,用于改进包含至少两种液相的组合物的相分离;涉及分离包含至少两种液相的组合物中至少两种液相的方法;也涉及包括至少一种化合物和至少一种疏水蛋白或其衍生物的制剂,所述化合物选自燃料、可燃物、原油、水溶性/油溶性聚合物溶液。
技术背景
疏水蛋白是丝状真菌如普通裂褶菌(Schizophillum commune)所特有的大约100至150个氨基酸的小蛋白质。通常具有八个半胱氨酸单元。
疏水蛋白显示出对界面的显著亲和力,因此适合包被表面,其通过形成两亲性膜以改变界面的性质。例如,用疏水蛋白包被铁氟龙(Teflon)可以获得亲水表面。
疏水蛋白可以从天然源中分离。制备疏水蛋白及其衍生物的方法也是已知的。例如,DE 10 2005 007 480.4公开了制备疏水蛋白及其衍生物的方法。
现有技术指出疏水蛋白在多种应用中的用途。
WO96/41882指出疏水蛋白可以作为乳化剂、增稠剂或者表面活性剂,用以赋予疏水表面亲水性、提高亲水物质的防水性、制备水包油乳剂或油包水乳剂。该文件也指出疏水蛋白的药物用途,例如可以制备膏剂或霜剂,以及化妆品方面的用途,例如皮肤防护或制备洗发剂或染发剂。除此之外,WO96/41882要求保护的组合物,尤其是药物用途的组合物包含疏水蛋白。
EP-A1 252 516公开了在30至80℃条件下利用含疏水蛋白的溶液包被窗、隐形眼镜、生物传感器、医疗设备、实施测定或贮藏用容器、船体货舱、固体微粒或框架或轿车车体。
WO 03/53383公开了疏水蛋白在化妆品应用中处理角蛋白材料的用途。
WO 03/10331公开了疏水蛋白表现出表面活性的性质。该文件公开了疏水蛋白包被的传感器(如测量电极),该传感器非共价连接有其他物质如电活性物质、抗体或酶。
WO 2004/000880也公开了疏水蛋白或疏水蛋白样物质包被的表面,其进一步公开了可以添加疏水蛋白稳定水包油乳剂或油包水乳剂。
WO 01/74864涉及疏水蛋白样蛋白质,也公开了这些蛋白可以用于稳定分散剂和乳剂。
原则上,利用蛋白质进行相分离是已知的。
GB 195,876公开了利用胶体破坏油包水乳剂的方法。所述的胶体实例为蛋白质或多糖,蛋白质如明胶、酪蛋白和白蛋白,多糖如阿拉伯胶或黄蓍胶。
JP-A 11-169177公开了具有脂肪酶活性的蛋白质在破坏乳剂中的用途。
WO 06/60916公开了由至少一种水溶性蛋白质、至少一种水溶性多糖和至少一种水溶性聚合物如聚环氧乙烷组成的无表面活性剂的混合物,其不同的应用也包括反乳化原油。
以上引用的文件中无一公开过疏水蛋白在相分离中的用途。
发明内容
利用蛋白质的优点在于其是自然存在并且可以生物降解的物质,所以不会导致任何持久的环境污染。
对于很多大规模的工业应用,例如当分离原油水乳剂时,尽可能快的进行相分离是很重要的。本发明的目的是提供一种利用蛋白质进行相分离的改进方法。
根据本发明,通过利用至少一种疏水蛋白来改进包含至少两种液相的组合物的相分离来实现该目的。
在这方面,根据本发明,原则上可以使用任意量的疏水蛋白,只要确保改进包含至少两种液相的组合物的相分离。
在本发明中,“改进相分离”可以理解为当混合物中添加某物质时比没有添加该物质的同一混合物发生更快的两种液相的分离,或者指只有添加了该物质才 能进行两种液相的分离。
在本发明中,疏水蛋白也可以理解为其衍生物或者修饰的疏水蛋白。修饰的或衍生的疏水蛋白可以是,例如疏水蛋白融合蛋白质或这样的蛋白质:该蛋白质的氨基酸序列与疏水蛋白具有至少60%的同一性,例如至少70%,优选至少80%同一性,更优选至少90%同一性,尤其优选至少95%同一性,而且该蛋白质可以达到疏水蛋白50%的生物学特征,例如60%,优选70%,更优选80%的生物学特征,特别是通过该蛋白质包被可以改变界面特性的性质,利用该蛋白质包被玻璃界面前后使水滴的接触角增长至少20°,优选增长至少25°,更优选增长至少30°。
惊奇地发现疏水蛋白或其衍生物改进至少两种液相的分离。
该方法对于完成快速相分离或者避免乳剂形成尤其有利。在这方面,甚至及其少量都是非常有效的。在破坏已形成的乳剂时也可以利用该性质。破坏乳剂的化合物也称为破乳剂。
本发明也涉及如上所述的至少一种疏水蛋白或者至少一种疏水蛋白衍生物的用途,其中所述至少一种疏水蛋白或至少一种疏水蛋白衍生物作为破乳剂。
在这方面,疏水蛋白的结构特异性而不是序列特异性对于定义疏水蛋白是至关重要的。虽然天然的疏水蛋白的氨基酸序列极为多样化,但它们都具有高度保守的八个半胱氨酸残基这一特征模式。这些残基形成四个分子内二硫键。
N末端和C末端在相对宽的范围内是可变的。融合配偶体蛋白质的长度为10至500个氨基酸,而且发现,例如本领域技术人员可以依据分子生物学技术将融合配偶体蛋白质添加至这些末端。
除此之外,具有相似结构和同等功能的蛋白质也应理解为是本发明意义中的疏水蛋白或其衍生物。
本发明中,术语“疏水蛋白”在下文指具有如下通用结构式(I)的多肽:
Xn-C1-X1-50-C2-X0-5-C3-X1-100-C4-X1-100-C5-X1-50-C6-X0-5-C7-X1-50-C8-Xm(I)
其中X可为20种天然氨基酸中的任一种(苯丙氨酸Phe、亮氨酸Leu、丝氨酸Ser、酪氨酸Tyr、半胱氨酸Cys、色氨酸Trp、脯氨酸Pro、组氨酸His、谷氨酰胺Gln、精氨酸Arg、异亮氨酸Ile、甲硫氨酸Met、苏氨酸Thr、天冬酰胺Asn、赖氨酸Lys、缬氨酸Val、丙氨酸Ala、天冬氨酸Asp、谷氨酸Glu和甘氨酸Gly)。在 每种情况下,此处的X可以相同也可以不同。在该结构式中,每一例X的下标表示氨基酸的数目,C代表半胱氨酸、丙氨酸、丝氨酸、甘氨酸、甲硫氨酸或苏氨酸,其中至少四个C指代的基团为半胱氨酸,下标n和m彼此独立地是0至500的自然数,优选15至300。
结构式(I)的多肽的特征还在于,在室温条件下,相对于非包被玻璃表面上同样大小的水滴所形成的接触角,该多肽可使包被后玻璃表面水滴的接触角增加至少20°,优选增加至少25°,更优选增加30°。
由C1至C8表示的氨基酸优选半胱氨酸;但它们也可被具有相似空间填充的其他氨基酸替换,优选丙氨酸、丝氨酸、苏氨酸、甲硫氨酸或甘氨酸。然而,C1 至C8位的氨基酸中至少4个,优选至少5个,更优选至少6个,尤其优选至少7个应当由半胱氨酸组成。本发明所涉及蛋白质中的半胱氨酸可以以还原形式存在或彼此间形成二硫键。
更优选分子内形成C-C桥,尤其其中是包括至少1个,优选2个,更优选3个,尤其优选4个分子内二硫键。在上述利用具有相似空间填充的氨基酸替换半胱氨酸时,最好所述C位点成对替换,从而可彼此形成分子内二硫键。
当X指代位点为半胱氨酸、丝氨酸、丙氨酸、甘氨酸、甲硫氨酸或苏氨酸时,通式中单个C位点的编号可相应改变。
优选使用式(II)的疏水蛋白:
Xn-C1-X3-25-C2-X0-2-C3-X5-50-C4-X2-35-C5-X2-15-C6-X0-2-C7-X3-35-C8-Xm(II)
其中X、C以及X和C的下标定义如上,下标n和m是0至300的数字,而且该蛋白质的特征还在于上述的接触角改变,为了实现本发明,C指代的残基中至少有6个为半胱氨酸,特别优选所有C残基都为半胱氨酸。
更优选使用式(III)的疏水蛋白:
Xn-C1-X5-9-C2-C3-X11-39-C4-X2-23-C5-X5-9-C6-C7-X6-18-C8-Xm (III)
其中X、C以及X的下标定义如上,下标n和m是0至200的数字,而且该蛋白质的特征还在于上述的接触角改变,此外C指代的残基中至少有6个为半胱氨酸,特别优选所有C残基都为半胱氨酸。
残基Xn和Xm可为与疏水蛋白天然相连的肽序列。然而,残基Xn和Xm之一 或两者均可为与疏水蛋白非天然相连的肽序列。这也应理解为包括这样的Xn和/或Xm残基,其中天然存在于疏水蛋白中肽序列的由非天然存在于疏水蛋白中的肽序列所延伸。
当Xn和/或Xm为与疏水蛋白非天然相连的肽序列时,这些序列的长度通常为至少20个氨基酸,优选至少35个氨基酸,更优选至少50个氨基酸,尤其优选至少100个氨基酸。这些与疏水蛋白非天然相连的残基,在下文也称为融合配偶体。这是为了表明该蛋白质由至少一个疏水蛋白部分和融合配偶体部分组成,而在自然界中不以该形式出现。
融合配偶体部分可选自多种蛋白质。几个融合配偶体部分也可以连接于一个疏水蛋白部分,例如连接于疏水蛋白部分的氨基末端(Xn)或羧基末端(Xm)。然而,也可以例如将两个融合配偶体连接于本发明蛋白质的一个位点(Xn或Xm)。
天然存在于微生物特别是大肠杆菌(E.coli)或枯草芽孢杆菌(Bacillussubtilis)中的蛋白质是特别合适的融合配偶体。这些融合配偶体的实例为序列yaad(SEQ ID NO:15和16)、yaae(SEQ ID NO:17和18)及硫氧化还原蛋白。只包含部分所述序列,例如所述序列的70-99%,优选所述序列的5-55%,更优选所述序列的10-40%的片段或衍生物,或者相对于所述序列个别氨基酸或核苷酸发生改变的片段或衍生物也是非常合适的。
在另一个优选的实施例中,除作为Xn或Xm的融合配偶体之外,疏水蛋白融合蛋白也显示出亲和结构域(亲和标签/亲和尾巴)。原则上已知亲和结构域指能够与给定的互补基团相互作用而且可以用来简化蛋白质建立和纯化的锚定基团。这样的亲和结构域的实例包括(His)k、(Arg)k、(Asp)k、(Phe)k和(Cys)k基团,k一般指1至10的自然数。亲和结构域优选(His)k基团,其中k为4至6。
还可以通过糖基化、酰基化或化学交联(如利用戊二醛交联)修饰本发明所使用的疏水蛋白或其衍生物的多肽序列。
本发明所使用的疏水蛋白或其衍生物的特性之一在于改变了该蛋白质包被表面的表面性质。可通过实验方式确定表面性质的改变,例如测量用蛋白质包被 表面前后的水滴接触角并确定两次测量的差异。
原则上,测量接触角对于本领域技术人员来说是已知的。该测量基于室温条件、5μl水滴和玻璃板作为基底。实验部分描述了例如适于测量接触角的确切实验条件。在实验部分的所述条件下,相对于非包被玻璃表面上相同大小的水滴的接触角,本发明所使用的融合蛋白具有可以增加接触角至少20°、优选至少25°、更优选至少30°的特性。
实施本发明尤其优选的疏水蛋白为dewA、rodA、hypA、hypB、sc3、basf1、basf2型的疏水蛋白,后面的序列表对其进行了结构表征。然而,疏水蛋白也可以是所述疏水蛋白的部分或衍生物。也可以将相同或不同结构的几个优选2个或3个疏水蛋白部分一起连接于非天然连接疏水蛋白的相应的合适多肽序列上。
具有SEQ ID NO:20所示多肽序列的yaad-Xa-dewA-his、SEQ ID NO:22所示多肽序列的yaad-Xa-rodA-his、SEQ ID NO:24所示多肽序列的yaad-Xa-basf1-his的融合蛋白及其编码核酸序列,尤其是SEQ ID NO:19、21、23所示序列尤其适合本发明。特别优选的实施方案还包括由SEQ IDNO:20、22或24所示多肽序列衍生的,通过至少1个至多10个、优选5个、更优选所有氨基酸5%的取代、插入或缺失产生且仍然具有所述起始蛋白的至少50%的生物学特征的蛋白质。此处,蛋白质的生物学特征应理解为是指所描述的至少20°的接触角改变。
尤其适合实施本发明的衍生物为由yaad-Xa-dewA-his(SEQ ID NO:20)、yaad-Xa-rodA-his(SEQ ID NO:22)或yaad-Xa-basf1-his(SEQ IDNO:24)衍生的截短yaad融合配偶体后形成的残基。使用截短的yaad残基,而不是包含294个氨基酸的完整的yaad融合配偶体(SEQ ID NO:16)是更有利的。然而,截短的残基应当包含至少20个氨基酸,优选至少35个氨基酸。例如,使用具有20至293个氨基酸,优选25至250个氨基酸,更优选35至150个氨基酸,如35至100个氨基酸的截短的残基。
可以利用在疏水蛋白与融合配偶体之间或者融合配偶体之间的裂解位点来释放非衍生形式的“纯”疏水蛋白,例如利用BrCN在甲硫氨酸位点 裂解、Xa因子裂解、肠激酶裂解、凝血酶裂解、TEV(烟草蚀纹病毒蛋白酶)裂解等。
还可以利用一种融合配偶体(例如yaad或yaae)和几种疏水蛋白[包括一个接一个的不同序列(如DewA-RodA或Sc3-DewA或Sc3-RodA)]产生融合蛋白质。同样也可以利用高达70%同源性的疏水蛋白片段(如N末端或C末端截短体)或突变蛋白质。在每种情况下选择与给定应用即待分离液相有关的最适构建体。
本发明所用的疏水蛋白或本发明制剂中存在的疏水蛋白可通过肽合成的已知技术以化学方法制备,例如通过Merrifield固相合成。
融合蛋白优选通过重组方法制备,其中将编码融合配偶体的核酸序列(特别为DNA序列)与编码疏水蛋白部分的核酸序列(尤其为DNA序列)组合,从而通过在宿主微生物中表达组合的核酸序列以产生目的蛋白质。此类制备方法已经公开,如DE 102005007480.4。
在这方面,用于所述制备方法的合适的宿主微生物(生产微生物)可以为原核生物(包括古生菌)或真核生物,尤其为包括嗜盐菌(halobacteria)和甲烷球菌(methanococci)的细菌、真菌、昆虫细胞、植物细胞和哺乳动物细胞,更优选大肠杆菌、枯草芽孢杆菌、巨大芽孢杆菌(Bacillusmegaterium)、米曲霉(Aspergillus oryzea)、构巢曲霉(Aspergillus nidulans)、黑曲霉(Aspergillus niger)、巴斯德毕赤酵母(Pichiapastoris)、假单胞菌属物种(Pseudomonas spec)、乳酸杆菌(lactobacilli)、多形汉逊酵母(Hansenula polymorpha)、里氏木霉(Trichoderma reesei)、SF9(或相关细胞)等。
本发明也涉及在调节核酸序列遗传控制下的包含编码本发明所用多肽的核酸序列的表达构建体以及包括至少一种所述表达构建体的载体的用途。
所述的构建体优选包含特定编码序列的5’上游启动子和3’下游终止 子,适用的情况下也包括其他常规调控元件,其中的每一个与编码序列有效连接。
根据本发明,“有效连接”指按启动子、编码序列、终止子以及适用情况下的附加调控元件的有序排列,从而使每一调控元件能够实现其表达编码序列的预期功能。
有效连接序列的实例为寻靶序列、增强子、聚腺苷化信号等。其他调控元件包括可选择标记、扩增信号、复制起点等。合适的调控序列的实例描述于Goeddel,Gene Expression Technology:Methods in Enzymology185,Academic Press,San Diego,CA(1990)中。
除了这些调控序列,在实际的结构基因的上游可能仍然存在对这些序列的天然调控,且适用的情况下可以对其进行遗传修饰,以关闭天然调控而增强基因表达。
优选的核酸构建体最好也包括一个或多个与启动子功能性连接的增强子序列,能够增强核酸序列的表达。其他有利的序列如其他调控元件或终止子也可以插入DNA序列的3’端。
存在于构建体中的核酸可以是一个或多个拷贝。适用的情况下,为选择所述构建体,该构建体还可以包括其他标记,如抗生素抗性或营养缺陷型互补基因。
有利于制备的调控序列的实例存在于,例如启动子中,如cos、tac、trp、tet、trp-tet、Ipp、lac、Ipp-lac、laclq-T7、T5、T3、gal、trc、ara、rhaP(rhaPBAD)SP6、lambda-PR或imlambda-P启动子,所述启动子最好用于革兰氏阴性菌。其他有利的调控序列的实例存在于革兰氏阳性启动子amy和SP02、酵母或真菌启动子ADC1、MFα、AC、P-60、CYC1、GAPDH、TEF、rp28、ADH中。
也可使用人工启动子进行调控。
为在宿主生物中表达,优选将核酸构建体插入载体(如质粒或噬菌体)中,从而使基因在宿主中达到最佳表达。除了质粒和噬菌体外,载体也指本领域技术人员已知的其他任何载体,例如病毒(如SV40、CMV、杆状 病毒和腺病毒)、转座子、IS元件、噬菌粒、粘粒和线性或环状DNA,以及农杆菌(Agrobacterium)系统。
这些载体在宿主生物中可以自主复制或随染色体复制。合适质粒的实例为,大肠杆菌中的pLG338、pACYC184、pBR322、pUC18、pUC19、pKC30、pRep4、pHS1、pKK223-3、pDHE19.2、pHS2、pPLc236、pMBL24、pLG200、pUR290、pIN-III″3-B1、tgt11或pBdCI,链霉菌(Streptomyces)中的pIJ101、pIJ364、pIJ702或pIJ361,杆菌中的pUB110、pC194或pBD214,棒状杆菌(Corynebacterium)中的pSA77或pAJ667,真菌中的pALS1、pIL2或pBB116,酵母中的2α、pAG-1、YEp6、YEp13或pEMBLYe23,或植物中的pLGV23、pGHlac+、pBIN19、pAK2004或pDH51。这些质粒是合适质粒的一小部分。其他质粒对于本领域技术人员是已知的并且可以在例如书籍Cloning Vectors(Pouwels P.H.等人编辑、Elsevier,Amsterdam-NewYork-Oxford,1985,ISBN 0 444 904018)中找到。
为表达其他存在的基因,核酸构建体中最好还包括3’-和/或5’-末端调控序列或基因以增强表达,根据宿主生物和基因的选择而选择所述序列以达到最佳表达。
这些调控序列使得能够选择性表达基因和蛋白质。根据宿主生物,这可能意味着如基因在诱导后最佳表达或过表达,或即刻表达和/或过表达。
在这方面,优选具有正面影响的调控序列或因子,从而增强引入基因的表达。因此,最好使用强转录信号(如启动子和/或增强子)在转录水平增强调控元件。然而,除此之外,也可以通过如提高mRNA的稳定性来增强翻译。
在载体的另一个实施方案中,含有核酸构建体或核酸的载体可最好以线性DNA的形式引入微生物,并通过异源或同源重组整合于宿主生物体的基因组中。线性DNA可由线性化载体如质粒组成,或仅由该核酸构建体或核酸组成。
为在生物中实现异源基因的最佳表达,可改变核酸序列使其与该生物特定的密码子使用一致。通过计算机分析所研究生物的其他已知基因,可 以确定密码子的使用。
将合适的启动子与合适的编码核酸序列及终止子或聚腺苷化信号融合,制备表达盒。常规重组和克隆技术见于如T.Maniatis,E.F.Fritsch和J.Sambrook,Molecular Cloning:A Laboratory Manual,Cold SpringHarbor Laboratory,Cold Spring Harbor,NY(1989),及T.J.Silhavy,M.L.Berman和L.W.Enquist,Experiments with Gene Fusions,ColdSpring Harbor Laboratory,Cold Spring Harbor,NY(1984),以及Ausubel,F.M.等人,Current Protocols in Molecular Biology,Greene PublishingAssoc.and Wiley Interscience(1987)中,可用于此目的。
为了在合适的宿主生物中表达,优选将重组核酸构建体或基因构建体插入宿主特异性载体中,所述载体可使基因在宿主中得到最佳表达。载体对于本领域技术人员来说是已知的,且可见如“Cloning Vectors”(PouwelsP.H.等人编辑,Elsevier,Amsterdam-New York-Oxford,1985)。
可以利用载体制备如由至少一个载体转化的可用于生产本发明所用疏水蛋白或其衍生物的重组微生物。优选将上述重组构建体引入合适的宿主系统并表达。在这方面,优选使用本领域技术人员已知的常用的克隆和转染技术以在特定表达系统中表达所述核酸,例如共沉淀、原生质体融合、电穿孔、逆转录病毒转染等。合适系统的描述见于如Current Protocols inMolecular Biology,F.Ausubel等人编辑,Wiley Interscience,New York1997,或Sambrook等人.Molecular Cloning:A Laboratory Manual.第2版,Cold Spring Harbor Laboratory,Cold Spring Harbor Laboratory Press,Cold Spring Harbor,NY,1989。
也可以制备同源重组的微生物。为此,制备包括本发明所用基因或编码序列的至少一个片段的载体,适用的情况下,在所述片段中引入至少一个氨基酸缺失、添加或取代,从而改变例如功能性破坏该序列(敲除载体)。引入序列可以是如相关微生物的同源物或从哺乳动物、酵母或昆虫来源衍生而来。或者,可设计用于同源重组的载体使内源性基因在同源重组时发生突变或其他改变,但仍然编码功能性蛋白质(例如改变上游调控区域从 而改变内源性蛋白质的表达)。本发明所用基因改变了的部分位于同源重组载体中。适于同源重组的载体的构建见于如Thomas,K.R.和Capecchi,M.R.(1987)Cell 51:503。
原则上,适用于本发明所用的核酸或核酸构建体的重组宿主生物可为任何原核或真核生物。优选使用微生物如细菌、真菌或酵母作为宿主生物。革兰氏阳性或革兰氏阴性菌,优选肠杆菌科(Enterobacteriaceae)、假单胞菌科(Pseudomonadaceae)、根瘤菌科(Rhizobiaceae)、链霉菌科(Streptomycetaceae)或诺卡氏菌科(Nocardiaceae)的细菌,特别优选使用的细菌为埃希氏菌属(Escherichia)、假单胞菌属(Pseudomonas)、链酶菌属(Streptomyces)、诺卡氏菌属(Nocardia)、伯克霍尔德菌属(Burkholderia)、沙门氏菌属(Salmonella)、农杆菌属(Agrobacterium)或红球菌属(Rhodococcus)的细菌。
根据宿主生物的不同,以本领域技术人员已知的方法培养用于制备融合蛋白的在上述方法中所使用的微生物。通常微生物生长于0至100℃、优选10至60℃,同时供以氧气的液体培养基中,所述液体培养基包括碳源(通常以糖的形式存在)、氮源(通常以有机氮源如酵母膏或盐如硫酸铵的形式存在)、微量元素(如铁盐、锰盐和镁盐),以及适用情况下的维生素。在这方面,营养液的pH值可保持某固定值,即培养期间可以调节也可不调节。可通过批量发酵法、半批量发酵法或连续发酵法进行培养。可在发酵起始时加入营养物质,也可以随后半批量或连续的方式进行加料。可以通过实施例中所述的方法从生物中分离酶,也可以粗提物的形式用于反应。
可以通过重组制备的方法制备本发明使用的疏水蛋白或其功能性生物活性片段,通过培养产生多肽的微生物,适用的情况下诱导蛋白质的表达,并从培养物中分离所述蛋白质。如有需要也可通过该方法在工业规模上生产所述蛋白质。可通过已知的方法培养和发酵重组微生物。例如,可以在温度20至40℃、pH 6-9的TB培养基或LB培养基中繁殖细菌。合适的培养条件详细描述于T.Maniatis,E.F.Fritsch和J.Sambrook,MolecularCloning:A Laboratory Manual,Cold Spring Harbor Laboratory,Cold Spring Harbor,NY(1989)中。
若多肽没有分泌至培养基中,则破碎细胞并通过分离蛋白质的已知方法从裂解物中获取产物。根据需要,可以通过高频超声、高压(如弗氏细胞压碎器)、渗透溶解(osmolysis)、通过去污剂、裂解酶或有机溶剂作用、利用匀浆器或所列方法的两种或多种组合来破碎细胞。
可以利用已知的层析方法纯化蛋白质,层析方法如分子筛层析(凝胶过滤),例如Q琼脂糖凝胶层析、离子交换层析和疏水层析,也可使用其他常规方法如超滤、结晶、盐析、透析和非变性凝胶电泳。合适的方法见述于Cooper,F.G.,Biochemische Arbeitsmethoden,[Biochemical workingmethods],Verlag Walter de Gruyter,Berlin,New York,或Scopes,R.,Protein Purification,Springer Verlag,New York,Heidelberg,Berlin中。
带有特定锚定基团的疏水蛋白融合蛋白更有利于分离和纯化,所述特定锚定基团是能够结合到固相载体特别是聚合物上的相应互补基团。所述固相载体,例如可以用来填充层析柱,以这种方式通常可以显著提高分离效率。这样的分离方法也称为亲和层析方法。为了加入锚定基团,在制备蛋白质时,可使用载体系统或寡核苷酸,通过特定的核苷酸序列延长cDNA,从而编码改变的蛋白质或融合蛋白质。为了易于纯化,利用包括起锚定作用的“标签”修饰蛋白质,例如利用六组氨酸锚的修饰。可以利用层析方法纯化六组氨酸锚修饰的疏水蛋白融合蛋白,例如,利用镍-琼脂糖作为柱填料。采用合适的洗脱方式,例如咪唑溶液洗脱,疏水蛋白融合蛋白可以再次从柱子上洗脱下来。
在简化的纯化方法中,可以不使用层析纯化。为此,首先采用合适的方法从发酵液中分离细胞,例如利用微滤或离心方法。然后利用合适的方法破碎细胞,例如上文提及的方法,并使细胞残渣与包涵体分离。后者的步骤最好通过离心完成。最后利用已知的方式破碎包涵体以释放疏水蛋白融合蛋白。该步骤可通过例如利用酸、碱和/或去污剂完成。利用0.1M的氢氧化钠在约1小时的时间内,通常可以完全溶解本发明所使用的包括疏水蛋白融合蛋白的包含体。利用此简化方法所获得的疏水蛋白融合蛋白的纯 度通常为以重量计总蛋白量的60-80%。上述利用这种简化方法获得的溶液可以用来实施本发明,而不需要进一步的纯化。
如所述制备的疏水蛋白可以作为融合蛋白直接使用,或在切割并移去融合配偶体后作为“纯”疏水蛋白使用。
当需要移去融合配偶体时,最好在融合蛋白质的疏水蛋白部分和融合配偶体部分之间加入潜在的裂解位点(蛋白酶的特异识别位点)。合适的裂解位点尤其指通过生物信息学工具确定的既不存在于疏水蛋白部分也不存在于融合配偶体部分的肽序列。特别合适的如BrCN甲硫氨酸裂解或蛋白酶介导的Xa因子裂解、肠激酶裂解、凝血酶、TEV(烟草蚀纹病毒蛋白酶)裂解。
根据本发明,疏水蛋白或其衍生物可以用来改进包含至少两种液相的组合物的相分离。就此而言,所述组合物可以为具有至少两种液相的任何组合物。
特别的,组合物可以为这样的组合物,在加入至少一种疏水蛋白或其衍生物前,以乳剂形式存在。
在这方面,在本发明的上下文中,组合物也可以具有除至少两种液相之外的其他相。
所述至少两种液相是两种不同密度的液相,例如油和水、两种不同密度的水性溶液、两种不同密度的有机溶液、燃料和水、可燃物和水或者溶剂和水。就此而言。在本发明的上下文中,水性溶液指包括水,适用的情况下也包括其他溶剂的溶液;每种液相也可以包含其他物质。
根据本发明,油类优选原油。
合适的溶剂指任何可以与水形成两相混合物的液体,尤其指有机溶剂,例如醚、芳香族化合物(如甲苯或苯)、醇、烃类、烯烃、环烷烃、环烯烃、酯类、酮、环烷(naphthene)或卤化烃。
根据本发明的另一个实施方案,本发明涉及如上所述的,至少一种疏水蛋白或至少一种疏水蛋白衍生物的用途,其中包含至少两种液相的组合物选自
-包含油类优选原油和水的组合物;
-包含燃料/可燃物和水的组合物;
-包含至少两种液相的反应混合物。
在本发明的上下文中,组合物也可以包含其他相,例如固相或液相,尤其是固相。
可以利用疏水蛋白或其衍生物进行本领域技术人员已知的任何应用。在本发明中,尤其要提及如下应用:在汽油/水混合物中作为破乳剂以及在其他燃料或可燃物/水混合物中作为破乳剂的用途,化学反应相分离,尤其是大规模工业过程中,破坏原油提取或原油生产中原油和水之间的乳剂,以及以水提取原油时对原油进行脱盐随后破坏形成的乳剂。适宜的大规模工业化学过程是涉及相分离的那些工业化学过程,例如使用钴催化剂的聚异丁烯加氢甲酰化中,其中从水性环境中分离催化剂。
根据本发明,也可以利用疏水蛋白或其衍生物来改进包含至少两种液相的组合物的相分离,所述的至少两种液相可以出现在反应过程中,即在反应过程中形成;也可以因为添加某种溶剂或某种组分而形成。根据本发明,疏水蛋白或其衍生物可以缩短相分离的时间,而且能降低有价值产物的损失。
根据本发明,同样可以改进包含两种不同密度水相的组合物的相分离,其中所述水相指包含水的相,适当的情况下含有其他溶剂。根据本发明,疏水蛋白或其衍生物可以,例如用来改进水性体系中分级聚合物的相分离。在这方面,尤其可以分级水溶性聚合物。
一般情况下,需要提及的是本领域技术人员公知的水溶性和油溶性聚合物,尤其是聚丙烯酸酯及其共聚物,取决于制备过程,其摩尔质量分布或多分散性大于1.1。
可通过添加破乳剂破坏乳剂。因此,例如,提取的矿物油通常以相对稳定的油包水乳剂存在,可以包含高达以重量计90%的水,这取决于沉淀物的性质。当开采和纯化原油时,在分离绝大部分水之后,可获得原油,但其仍包含以重量计约2-3%的水。这2-3%的水与油形成稳定的乳剂,利 用离心和添加常规的破乳剂也不能完全分离该乳剂。就此而言形成了某些问题,首先,水包含大量的盐类,因此具有腐蚀作用,其次,残留的水增加了运输和贮存的体积,导致成本增加。根据本发明,发现疏水蛋白或其衍生物可以用来显著改进这些组合物的相分离。可以实现十分快速的分离。
就此而言,为了达到最佳效果,破乳剂必须适合于乳化的油类和脂肪以及任何可能存在的乳化剂和表面活性剂的性质。可以通过提高温度来进一步增强乳剂的破坏,例如0-100℃的温度,例如10-80℃,优选20-60℃。
本发明其他应用的实例包括板材业和纺织工业浸渍乳剂的破乳化,以及药物乳剂的破乳化。另一个应用是有机加工废液的破乳化,所述废液形成油/水乳剂,例如工业和贸易废液以及家庭来源的废液,尤其来自金属加工,例如来自金属加工的切削液,来自制革厂和矿物油精炼厂。所述废液在例如精炼厂和石油化工厂的矿物油加工过程中形成。在将这些废液导入净化设备之前,有必要分离往往以乳剂形式存在的油类残渣。
根据本发明的另一个应用是水包油或油包水混合物的破乳化,例如作为切削液使用且需再循环使用的乳剂。例如,在海船上也形成作为船底污水的水/油混合物。在这个方面,为了分离水和减少需要处理的溶剂的量,有必要分离乳剂。
所使用的疏水蛋白或其衍生物的量可在很大范围内变动,其量优选与组合物本身相适配,且适用的情况下与其他存在于组合物中的成分相适配。
例如,如果组合物包含能迟滞或削弱分离至少两种液相的物质,例如表面活性剂或乳化剂,那么,最好使用较大量的疏水蛋白或其衍生物。
因为油类,尤其原油,是由很多化学化合物组成的混合物,而油类和水中的化学组合物和盐级分不同,破乳化作用的具体条件(如温度)不同,破乳化作用的持续时间不同,与混合物中其他组分的比例分配以及相互作用的性质不同,所以有必要使破乳剂与具体条件相适配。
惊奇的发现,甚至少量的疏水蛋白或其衍生物即可改进相分离。
根据本发明,至少一种疏水蛋白或其衍生物可以以任何合适的量使用。通常,所使用的至少一种疏水蛋白或其衍生物基于总组合物的量在0.0001 至1000ppm的范围;优选0.001至500ppm,尤其优选0.01至200ppm或0.01至100ppm,特别优选0.1至50ppm。
在本发明的上下文中,ppm表示mg/kg。
根据另一个实施方案,本发明涉及上文描述的基于总组合物使用量0.0001至1000ppm的至少一种疏水蛋白或至少一种疏水蛋白衍生物的用途。本领域技术人员根据所要破乳化的组合物的性质指定其使用的浓度。
如果组合物是包含燃料或可燃物和水的组合物,通常,所使用的疏水蛋白或其衍生物的量在0.001至10ppm范围内,优选0.005至2ppm,尤其0.01至1ppm,尤其优选0.05至0.5ppm,更优选0.01至0.1ppm。
如果组合物是包含原油和水的组合物,通常,所使用的疏水蛋白或其衍生物的量在1至1000ppm范围内,优选1至800ppm,尤其5至500ppm,尤其优选10至200ppm,更优选15至100ppm(例如20至50ppm)。
如果组合物是包含两种不同密度水相的组合物,其中,相是在例如分级水溶性聚合物时形成,通常,所使用的疏水蛋白或其衍生物的量在1至1000ppm范围内,优选1至500ppm,尤其5至250ppm,尤其优选10至200ppm,更优选15至100ppm。
根据本发明,除了至少一种疏水蛋白或其衍生物以外,组合物也可以包括能改进相分离的其他化合物。在这方面,化合物可以是本领域技术人员已知的具有该性质的任何化合物。适合用于改进相分离,尤其用于原油生产中作为破乳剂的应用的其他化合物的实例是烷氧基化的酚甲醛树脂、EO/PO嵌段共聚物、交联的双环氧化合物、聚酰胺或它们的烷氧基化物、磺酸盐、乙氧基化脂肪胺、琥珀酸盐以及在DE 10 2005 006 030.7中详细说明的用于该应用的具有该性质的化合物。
根据另一个实施方案,本发明涉及上文描述的用途,其中除了至少一种疏水蛋白或至少一种疏水蛋白衍生物外,使用至少一种可以改进相分离的其他化合物。
根据另一个方面,本发明也涉及分离包含至少两种液相的组合物中至少两种液相的方法,该方法包括向组合物中添加至少一种疏水蛋白或至少 一种疏水蛋白衍生物。
就此而言,组合物可以是如上文描述的包括至少两种液相的组合物。
根据优选的实施方案,本发明涉及该性质的方法,其中包括至少两种液相的组合物选自
-包含油类优选原油和水的组合物;
-包含燃料/可燃物和水的组合物;
-包含至少两种液相的反应混合物。
在本发明的上下文中,原则上可以使用能够改进相分离的任意量的疏水蛋白或其衍生物。基于总组合物的量,疏水蛋白或其衍生物的使用量在0.001至1000ppm范围内是尤其合适的。
本发明也涉及如上所述的方法,其中所使用的至少一种疏水蛋白或至少一种疏水蛋白衍生物基于总组合物的量在0.001至1000ppm范围内。已经提及了各个系统的优选量。
根据本发明,所述的方法可以包括附加步骤,例如,改进相分离或破坏乳剂的步骤。在这方面,所述步骤可以是,例如,提高温度或者离心。这样的步骤可以在添加至少一种疏水蛋白或其衍生物之前、期间或之后实施。
根据另一个实施方案,本方面涉及如上所述的方法,其中该方法包括在添加至少一种疏水蛋白或至少一种疏水蛋白衍生物之前或之后,提高包含至少两种液相的组合物的温度。
根据本发明,可以添加疏水蛋白或其衍生物到例如包含燃料或可燃物的制剂中。当制剂接触到水时,能够发生快速的分离或阻止乳剂的形成。例如,贮存箱中的乳剂的形成将使我们需要对制剂进行复杂的纯化步骤。
为了例如阻止乳剂的形成,向原油中添加疏水蛋白或其衍生物也同样有益。
就此而言,在本发明的上下文,包括燃料或可燃物的制剂可以还包括通常存在于具有该性质的制剂中的添加剂。
例如WO2004/087808详细说明了合适的添加剂。
本发明也涉及包括至少一种化合物和至少一种疏水蛋白或其衍生物的制剂,所述化合物选自燃料、可燃物、原油、水溶性/油溶性聚合物溶液。
只要保证当制剂接触到水时可以改进相分离,所使用的疏水蛋白或其衍生物的量可以不同,这由其他的添加物质而定。
根据本发明,疏水蛋白或其衍生物的使用量优选在0.0001至1000ppm范围内,更优选0.001至500ppm,尤其优选0.01至100ppm。
本发明也涉及如上所述的制剂,其中在该制剂中存在的疏水蛋白或其衍生物基于总制剂的量在0.0001至1000ppm范围内。
如果制剂是包含原油的混合物,通常,添加到该制剂的疏水蛋白或其衍生物的量在1至1000ppm范围内,优选10至800ppm,尤其10至500ppm。
如果制剂是包含燃料或可燃物的混合物,通常,添加到该制剂的疏水蛋白或其衍生物的量在0.001至0.5ppm范围内,优选0.005至0.3ppm,尤其0.01至0.2ppm。
因此,根据另一个实施方案,本发明涉及如上所述的制剂,其中该制剂包括至少一种燃料或可燃物以及疏水蛋白或其衍生物,所述存在于制剂中的疏水蛋白或其衍生物基于总制剂的量在0.001至0.5ppm范围内。
在本发明的上下文中,可燃物可以理解为,例如,轻、中或重燃料油。
在本发明的上下文中,燃料可以理解为,例如汽油、柴油机燃料或汽轮机燃料。尤其优选汽油。
燃料可以包含其他添加剂。通常本领域技术人员熟知常规的添加剂。例如,WO2004/087808中详细说明了合适的添加剂和溶剂。
根据本发明,具有去污剂效果和/或具有阀座磨损抑制效果的添加剂(在下文中称为去污剂添加剂),例如,适合用作其他添加成分。去污剂添加剂具有至少一个疏水烃链残基,所述烃链残基具有85至20 000g/mol的数均分子量Mn和至少一种选自如下的极性基团:
(a)具有高达6个氮原子的单氨基或多氨基,至少一个氮原子是碱性的;
(b)硝基,适用的情况下与羟基组合;
(c)羟基与单氨基或多氨基的组合,其中至少一个氮原子是碱性的;
(d)羧基或其碱金属/碱土金属盐;
(e)磺酸基或其碱金属/碱土金属盐;
(f)聚C2-C4氧化烯基团,以羟基、具有至少一个碱性氮原子的单氨基或多氨基,或氨基甲酸酯封端;
(g)羧酸酯基团;
(h)具有羟基和/或氨基和/或酰氨基和/或亚氨基的琥珀酐衍生基团;和/或
(i)由取代酚与醛和一元胺或多元胺通过曼尼希反应产生的基团;
在上述的去污添加剂中,造成在燃料中足够溶解度的疏水烃链残基,具有85至20 000的数均分子量(Mn),特别是113至10 000,尤其是300至5000。具有Mn=300-5000,特别是Mn=500-2500,尤其是Mn=700-2300的聚丙烯、聚丁烯和聚异丁烯考虑作为一般的疏水烃链残基,尤其是与极性基团(a)、(c)、(h)和(i)组合。
如下提及的可作为上述去污添加剂基团的实例。
包括单氨基或多氨基(a)的添加剂优选以数均分子量Mn在300至5000的聚丙烯或常规的(即,具有主要位于中心的双键)聚丁烯或聚异丁烯为基础的聚烯烃一元胺或聚烯烃多元胺。如果利用具有主要位于中心的双键(通常在β位和γ位)的聚丁烯或聚异丁烯作为制备所述添加剂的起始材料,通过氯化、然后氨化或者通以空气或臭氧氧化双键以得到羰基或羧基化合物、然后在还原(氢化)条件下氨化的制备线路是适合的。在这种情况下,胺例如氨、一元胺或多元胺(如二甲氨基丙胺、乙二胺、二亚乙基三胺、三亚乙基四胺或四亚乙基五胺)都可以用于氨化。相应的基于聚丙烯的添加剂尤其在WO94/24231中已经描述了。
其他优选的包括单氨基(a)的添加剂是由平均聚合度P=10-100的聚异丁烯与氮氧化物或氮氧化物/氧气的混合物反应所形成产品的氢化产物,尤其正如WO97/03946描述的。
其他优选的包括单氨基(a)的添加剂是由聚异丁烯环氧化物与胺反应, 随后脱水并以氨基醇还原后获得的化合物,尤其正如DE-A 196 20 262描述的。
包括硝基(b)且适用的情况下与羟基组合的添加剂优选由平均聚合度P=5-100或10-100的聚异丁烯与氮氧化物或氮氧化物/氧气的混合物反应所形成的产物,尤其正如WO96/03367和WO 96/03479描述的。这些反应产物通常是纯硝基聚异丁烯(如α,β-二硝基聚异丁烯)并混杂有羟基硝基聚异丁烯(如α-硝基-β-羟基聚异丁烯)的混合物。
包括与单氨基或多氨基组合的羟基(c)的添加剂优选通过具有双键[优选主要位于末端的双键]并且Mn=300-5000的聚异丁烯获得的聚异丁烯环氧化物与氨或一元胺或多元胺的反应产物,尤其正如EP-A 0 476 485描述的。
包括羧基或其碱金属/碱土金属盐(d)的添加剂优选马来酐的C2-C40烯烃的共聚物,所述共聚物的总分子量在500至20 000,并且其全部或部分羧基反应形成碱金属或碱土金属盐,其余的羰基与醇或胺反应。这些添加剂已经公开了,尤其在EP-A 0 307 815中。这些性质的添加剂主要用来防护阀座磨损,并且如WO87/01126中描述的,最好与常规燃料去污剂如聚(异)丁烯胺或聚醚胺一起使用。
包括磺酸基或其碱金属/碱土金属盐(e)的添加剂优选烷基磺基琥珀酸酯的碱金属或碱土金属盐,尤其正如EP-A 0 639 632描述的。
该性质的添加剂主要用来防护阀座磨损,优选与常规燃料去污剂如聚(异)丁烯胺或聚醚胺一起使用。
包括聚C2-C4氧化烯基团(f)的添加剂优选聚醚或聚醚胺,所述聚醚或聚醚胺可通过C2-C60烷醇、C6-C30烷二醇、单/双-C2-C30烷胺、C1-C30烷基环己醇或C1-C30-烷基酚与每羟基或氨基1-30mol的环氧乙烷和/或环氧丙烷和/或环氧丁烷反应获得,对于聚醚胺,随后与氨、一元胺或多元胺进行还原氨化。尤其在EP-A 0 310 875,EP-A 0 356 725,EP-A 0 700 985和US 4,877,416中已经描述了该性质的产物。对于聚醚,这些产物也达到浮选油质量的要求。在这点上一般的例子是十三烷醇或异十三烷醇丁氧基 化物(isotridecanol butoxylates)、异壬基酚丁氧基化物(isononylphenolbutoxylates)及聚异丁烯醇丁氧基化物(polyisobutenol butoxylates)和丙氧基化物(propoxylates)以及它们与氨反应的相应产物。
包括羧酸酯基(g)的添加剂优选具有长链烷醇或多元醇的单-、双-或三羧酸酯类,尤其优选在100℃时,最小粘度为2mm2/s,尤其正如DE-A38 38918描述的。脂肪酸或芳香酸可以用作单-、双-或三羧酸,而合适的酯醇(ester alcohol)或多元醇尤其为长链如6-24 C原子的酯醇或多元醇。异辛醇、异壬醇、异癸醇、异十三烷醇的乙二酸酯、邻苯二甲酸酯、异邻苯二甲酸酯、对苯二酸酯和(偏)苯三酸酯都是酯类的一般代表。该性质的产物也达到浮选油质量的要求。
包括具有羟基和/或氨基和/或酰氨基和/或亚氨基的琥珀酐衍生基团(h)的添加剂优选聚异丁烯琥珀酐相应的衍生物,所述的衍生物可以利用Mn=300-5000的常规或高活性的聚异丁烯与马来酐通过加热或氯化聚异丁烯反应获得。在这方面,尤其关注的是脂肪族聚胺(例如乙二胺、二亚乙基三胺、三亚乙基四胺或四亚乙基五胺)衍生物。该性质的汽油添加剂尤其在US 4,849,572中已经描述了。
包括由取代酚与醛和一元胺或多元胺通过曼尼希反应产生的基团(i)的添加剂优选聚异丁烯取代的酚类与甲醛和一元胺或多元胺(例如乙二胺、二亚乙基三胺、三亚乙基四胺或四亚乙基五胺)反应的产物。所述的聚异丁烯取代的酚类可从Mn=300-5000的常规或高活性的聚异丁烯衍生获得。该性质的“聚异丁烯曼尼希碱” 尤其在EP-A 0 831 141中已经描述了。
为了更加明确地定义所列出的各个汽油添加剂,上述公开内容的现有技术文件在此明确引用作为参考。
在这方面,用于给定应用的所述的添加剂的使用量对于本领域技术人员是显而易见的。
除此之外,根据本发明的制剂也可以结合其他常规的组分和添加剂。没有任何显著去污效果的浮选油在此作为实例提及。
合适的矿物浮选油是在矿物油加工过程生成的馏分,例如光亮油、或 具有SN 500-2000型粘度的基础油,以及芳香烃、链烷烃和烷氧基烷醇(alkoxyalkanol)。精炼矿物油的过程中生成一种称为“加氢裂化油”的馏分同样适合本发明,所述“加氢裂化油”是在约360-500℃的范围内沸腾,从在高压条件下已经催化加氢、异构化并脱蜡的天然矿物油中获得的真空蒸馏切取馏分。上述矿物浮选油的混合物也是合适的。
可以用于本发明的合成浮选油的实施选自:聚烯烃(聚α烯烃或聚内烯烃)、(聚)酯、(聚)烷氧基化物、聚醚、脂肪族聚醚胺、烷基酚起始的聚醚、烷基酚起始的聚醚胺以及长链烯醇羧酸酯。
合适的聚烯烃的实例为Mn=400-1800,尤其是以聚丁烯或聚异丁烯为基础的烯烃聚合物(氢化的或非氢化的)。
合适的聚醚或聚醚胺的实例为,优选包括聚C2-C4氧化烯基团的化合物,所述聚醚或聚醚胺可通过C2-C60烷醇、C6-C30烷二醇、单/双-C2-C30烷基胺、C1-C30烷基环己醇或C1-C30烷基酚与每羟基或氨基1-30mol的环氧乙烷和/或环氧丙烷和/或环氧丁烷反应获得,对于聚醚胺,随后与氨、一元胺或多元胺进行还原氨基化。尤其在EP-A 0 310 875,EP-A 0 356 725,EP-A 0 700 985和US 4,877,416中已经描述了该性质的产物。可以利用的聚醚胺的实例为聚C2-C6氧化烯胺(poly-C2-C6-alkylene oxide amine)或其功能衍生物。在这点上一般的例子是十三烷醇或异十三烷醇丁氧基化物、异壬基酚丁氧基化物及聚异丁烯丁氧基化物和丙氧基化物以及它们与氢反应的相应产物。
长链烯醇的羧酸酯的实例为,优选具有长链烷醇或多元醇的单-、双-或三羧酸酯类,尤其正如DE-A38 38 918描述的。脂肪酸或芳香酸可以用作单-、双-或三羧酸,而合适的酯醇或多元醇尤其为长链如6-24C原子的酯醇或多元醇。异辛醇、异壬醇、异癸醇、异十三烷醇的乙二酸酯、邻苯二甲酸酯、异邻苯二甲酸酯、对苯二酸酯和(偏)苯三酸酯都是酯类的一般代表,例如双-(正-或异-十三烷基)邻苯二甲酸酯。
其他合适的浮选油系统的实例已在DE-A 38 26 608、DE-A 41 42 241、DE-A 43 09 074,EP-A 0 452 328和EP-A 0 548 617中描述,在此明确引用作 为参考。
尤其适合的合成浮选油的实例是具有约5-35个(例如约5-30个)C3-C6氧化烯单体的以醇起始的聚醚,所述氧化烯单体选自例如环氧丙烷、正环氧丁烷和异环氧丁烷单体,或其混合物。合适的起始醇的非限制实例是,具有长链烷基尤其是直链或支链C6-C18烷基的长链烷醇或长链烷基取代酚。
十三烷醇及壬基酚作为优选的实施例提及。
更多合适的合成的浮选油是烷氧基化的烷基酚,正如DE-A 10 102913.6所描述的那样。
在这方面,用于给定应用的所述浮选油的使用量对于本领域技术人员是显而易见的。
其他常规的添加剂为缓蚀剂,例如基于有机羧酸的铵盐,所述盐趋向形成膜,或者基于杂环芳香族化合物用于非铁金属腐蚀保护;抗氧化剂或稳定剂,例如基于胺(如对苯二胺、二环己基胺)或其衍生物,或基于酚(例如2,4-二-叔丁基苯酚或3,5-二-叔丁基-4-羟苯基丙酸);其他常规破乳剂;抗静电剂;茂金属(例如二茂铁);甲基环戊二烯三羰基锰(methylcyclopentadienyl manganese tricarbonyl);润滑添加剂(如某些脂肪酸、烯基琥珀酯、双(羟烷基)脂肪胺、羟乙酰胺或蓖麻油);以及染料(标记)。适用的情况下,为了降低燃料的pH值也添加胺。
通常,添加到燃料中的所述含极性基团(a)-(i)的去污添加剂的量为以重量计10-5000ppm,尤其为以重量计50-1000ppm。如果需要的话,为了该目的,所提及的其他成分和添加剂的添加量是常规的。
适合本发明的燃料和可燃物是本领域技术人员已知的任意燃料和可燃物,例如汽油,正如例如Ullmann’s Encyclopedia of Industrial Chemistry,第5版1990,卷A16,pp.719ff所描述的。根据本发明,柴油机燃料、煤油和喷气机燃料也是合适的燃料。
特别的,含有以体积计最多60%(例如最多42%)的芳香族化合物以及以重量计最多2000ppm(例如最多150ppm)的硫的汽油是合适的。
汽油中芳香族化合物的含量为,例如,以体积计在10-50%范围内,例如30-42%,优选以体积计32-40%。汽油中硫的含量为,例如,以重量计在2-500ppm范围内,例如5-150ppm,优选以重量计10-100ppm。
此外,合适的汽油可以是,例如,具有以体积计高达50%的烯烃,例如以体积计6-21%,优选以体积计7-18%;具有以体积计高达5%的苯,例如以体积计0.5-1.0%,优选以体积计0.6-0.9%;和/或具有以重量计高达25%的氧,例如,以重量计高达10%或以重量计1.0-2.7%,优选以重量计1.2-2.0%。
优选利用实例提及的汽油:同时具有的芳香族化合物的含量为以体积计最多38%、烯烃的含量为以体积计最多21%、硫的含量为以重量计最多50ppm、苯的含量为以体积计最多1.0%以及氧的含量以重量计1.0-2.7%。
汽油中醇和醚的含量在很大范围内变动。对于甲醇,以体积计通常的最大含量的实例为15%、对于乙醇,以体积计为65%、对于异丙醇,以体积计为20%、对于叔丁醇,以体积计为15%、对于异丁醇,以体积计为20%以及对于具有5个或更多C原子的醚,以体积计为30%。
适合本发明的汽油的Sommer蒸汽压通常为最多70kPa,尤其为60kPa(每种情况均为37℃)。
通常,汽油的RON为75至105。相应的MON的常规范围为65至95。
利用常规方法(DIN EN 228)确定所述标准。
以下实施例对本发明进行更详细的说明。
实施例
实施例1
克隆yaad-His6/yaaE-His6的初步工作
利用寡核苷酸Hal 570和Hal 571(Hal 572/Hal 573)实施聚合酶链式反应。所用的模板DNA为细菌枯草杆菌的基因组DNA。得到的PCR片段包括枯草杆菌yaaD/yaaE基因的编码序列,其末端分别为NcoI及BglII的限制性切割位点。纯化并利用限制性内切酶NcoI及BglII切割PCR片段。该DNA 片段用作插入物并克隆入Qiagen pQE60载体中,所述载体事先已经利用限制性内切酶NcoI及BgIII线性化。由此得到载体pQE60YAAD#2/pQE60YaaE#5,可用于表达分别由YAAD∷HIS6和YAAE∷HIS6组成的蛋白质。
Hal570:gcgcgcccatggctcaaacaggtactga
Hal571:gcagatctccagccgcgttcttgcatac
Hal572:ggccatgggattaacaataggtgtactagg
Hal573:gcagatcttacaagtgccttttgcttatattcc
实施例2
yaad疏水蛋白DewA-His6的克隆
利用寡核苷酸KaM 416和KaM 417实施聚合酶链式反应。所用的模板DNA为霉菌构巢曲霉的基因组DNA。得到的PCR片段包括疏水蛋白基因dewA的编码序列和编码N-末端Xa因子蛋白酶裂解位点的序列。纯化并用限制性核酸内切酶BamHI切割PCR片段。该DNA片段用作插入物并克隆入事先已经通过限制性核酸内切酶BamHI线性化的pQE60YAAD#2载体中。
由此得到的载体#508,可用于表达包含YAAD∷Xa∷dewA∷HIS6的融合蛋白质。
KaM416:
GCAGCCCATCAGGGATCCCTCAGCCTTGGTACCAGCGC
KaM417:
CCCGTAGCTAGTGGATCCATTGAAGGCCGCATGAAGTTCTCCGT
CTCCGC
实施例3
yaad-疏水蛋白RodA-His6的克隆
利用寡核苷酸KaM 434和KaM 435克隆质粒#513,方法与克隆质粒#508类似。
KaM434:
GCTAAGCGGATCCATTGAAGGCCGCATGAAGTTCTCCATTGCTG
C
KaM435:CCAATGGGGATCCGAGGATGGAGCCAAGGG
实施例4
yaad-疏水蛋白BASF1-His6的克隆
利用寡核苷酸KaM 417和KaM 418克隆质粒#507,方法与克隆质粒#508类似。
所用的模板DNA为人工合成的DNA序列,即疏水蛋白BASF1(见附录,SEQ ID NO.11和12)。
KaM417:
CCCGTAGCTAGTGGATCCATTGAAGGCCGCATGAAGTTCTCCGT
CTCCGC
KaM418:
CTGCCATTCAGGGGATCCCATATGGAGGAGGGAGACAG
实施例5
yaad-疏水蛋白BASF2-His6的克隆
利用寡核苷酸KaM 417和KaM 418克隆质粒#506,方法与克隆质粒#508类似。
所用的模板DNA为人工合成的DNA序列,即疏水蛋白BASF2(见附录,SEQ ID NO.13和14)。
KaM417:
CCCGTAGCTAGTGGATCCATTGAAGGCCGCATGAAGTTCTCCGT
CTCCGC
KaM418:
CTGCCATTCAGGGGATCCCATATGGAGGAGGGAGACAG
实施例6
yaad-疏水蛋白SC3-His6的克隆
利用寡核苷酸KaM 464和KaM 465克隆质粒#526,方法与克隆质粒#508类似。
所用的模板DNA为普通裂褶菌cDNA(见附录,SEQ ID NO.9和10)。
KaM464:CGTTAAGGATCCGAGGATGTTGATGGGGGTGC
KaM465:GCTAACAGATCTATGTTCGCCCGTCTCCCCGTCGT
实施例7
重组大肠杆菌菌株yaad-疏水蛋白DewA-His6的发酵
于15ml Greiner管中将表达yaad-疏水蛋白DewA-His6的大肠杆菌菌株接种于3ml LB液体培养基。37℃条件下在200rpm的振荡器中温育8小时。在每例中,用1ml预培养物接种2个包含250ml LB培养基(+100μg/ml氨苄青霉素)的1l具挡板的Erlenmeyer烧瓶,并在37℃于180rpm的振荡器中温育9小时。
在20 l的发酵罐中用0.5 l预培养物(相对水测得OD600nm 1∶10)接种于13.5 l LB培养基(+100μg/ml氨苄青霉素)。在OD60nm~3.5时加入140ml的100mM IPTG。3小时后,将发酵器冷却至10℃,并通过离心移除发酵液。细胞沉淀用于进一步纯化。
实施例8
重组疏水蛋白融合蛋白质的纯化
(具有C末端His6标签的疏水蛋白融合蛋白质的纯化)
将100g细胞沉淀(100-500mg疏水蛋白)溶于50mM磷酸钠缓冲液(pH7.5)中,至总体积为200ml并重悬所述细胞。用Ultraturrax T25型(Janke and Kunkel;IKA-Labortechnik)处理悬浮物10分钟,然后与500单位的benzonase核酸酶(Merck,Darmstadt;订货号:1.01697.0001)于室温温 育1小时,以降解核酸。在细胞破碎前,利用玻璃管(Cartridge)(P1)进行过滤。为破碎细胞并剪切残留的基因组DNA,进行两次1500bar匀浆(Microfluidizer M-110EH;Microfluidics Corp.)。离心匀浆物(SorvallRC-5B,GSA转子,250ml离心杯,60分钟,4℃,12 000rpm,23 000g),将上清液置于冰上并将沉淀重悬于100ml磷酸钠缓冲液(pH7.5)。重复离心及重悬步骤三次,其中第三次的磷酸钠缓冲液中包含1%SDS。重悬后,将混合物搅拌1小时,然后进行最终离心(Sorvall RC-5B,GSA转子,250ml离心杯,60分钟,4℃,12 000rpm,23 000g)。SDS-PAGE分析表明,在最终离心后,疏水蛋白存在于上清液中(图1)。该实验显示,疏水蛋白很可能以包涵体的形式存在于相应大肠杆菌的细胞中。将50ml含有疏水蛋白的上清液充填50ml镍-琼脂糖凝胶高效17-5268-02柱(Amersham),其中该柱用50mM Tris-Cl缓冲液(pH8.0)平衡。利用50mM Tris-Cl缓冲液(pH8.0)洗柱,然后利用含有200mM咪唑的50mM Tris-Cl缓冲液(pH8.0)洗脱疏水蛋白。为去除咪唑,用50mM Tris-Cl缓冲液(pH8.0)透析溶液。
图1显示了所制备的疏水蛋白的纯化:
泳道A:充填于镍-琼脂糖凝胶柱的物质(1∶10稀释)
泳道B:渗漏=洗涤步骤洗脱液
泳道C-E:OD 280峰值处的洗脱级分(WP1,WP2,WP3)
泳道F:显示所应用的分子量标准参照物
图1的疏水蛋白分子量约为53kD。某些较小的条带代表疏水蛋白的降解产物。
实施例9
应用测试;通过改变水滴在玻璃上的接触角对疏水蛋白进行表征底物:
玻璃(窗玻璃,Süddeutsche Glas,Mannheim,Germany):
使用如实施例8所述纯化的疏水蛋白。
-将玻璃板浸入该溶液过夜(温度80℃)
-此后,从该溶液中取出包被有疏水蛋白的玻璃板,并在蒸馏水中洗涤
-此后,温育,10分钟/80℃/1%SDS蒸馏水溶液
-蒸馏水洗涤
-此后,在80℃条件下温育10分钟/1%SDS蒸馏水溶液
-再次用蒸馏水洗涤
风干样品,室温确定已包被玻璃表面上5μl水滴的接触角(以度表示)。
在Dataphysics Contact Angle System OCA 15+,软件SCA 20.2.0(2002年11月)仪器确定接触角测量值。根据厂商的说明书进行测量。
未处理玻璃的接触角为30±5°;
以实施例8的疏水蛋白(yaad-dewA-his6)包被的玻璃板的接触角为75±5°。
==>接触角的增加:45°
实施例10
利用疏水蛋白浓缩物(yaad-Xa-dewA-His6)作为燃料的添加剂
实验原理:
现代燃料通常包含许多不同的添加剂(定义为添加剂包)。如果在燃料生产或销售过程中接触到水,这些添加剂能够显示出乳化作用,并导致不希望的燃料-水乳剂的形成。为了避免该结果,通常向燃料中添加破乳剂。
利用实施例8(SEQ ID NO.19和20)所描述的疏水蛋白浓缩物进行破乳化实验。
所述疏水蛋白浓缩物以乙醇稀释并添加到市场上可以购买到的Eurosuper燃料(与EN 228一致)中,所述燃料已含特效添加剂包A 725 mg/kg。该添加剂包主要包含聚异丁烯胺Kerocom PIBA、浮选油混合物、溶剂、缓蚀剂及摩擦改性剂。
制备含0.01、0.03、0.05、0.07、0.14和0.28mg疏水蛋白/kg的燃料样品。只添加A,不含疏水蛋白的燃料作为参比(10-V1)。在另一个对比实验(10-V2)中,使用市场上可以购买到的基于酚树脂(ADX 606,自Lubrizol)的破乳剂D 1.45mg/kg。
依照DIN51415使用每一个燃料样品进行乳化实验。在这方面,每例中80ml燃料和20ml水相互完全混合。此后,观察到依赖时间的分层过程。利用规范标准分析,1表征非常好的分层,较大的数代表越来越差的分层。所引用的DIN规范中包含所述细节。
表1总结了实验所获得的结果。该表列出各种情况下1分钟、5分钟、30分钟和60分钟后相分离层的评定。通常,1或1b评定值需要在5分钟后获得。
表1
No. | 1min. | 5min. | 30min. | 60min | |
10-V1(对照) | A | 4 | 4 | 2 | 1b |
10-V2(对照) | A+1.45mg D/kg | 1b | 1 | 1 | 1 |
10-1 | A+0.01mg H./kg | 1b | 1 | 1 | 1 |
10-2 | A+0.03mg H./kg | 1b | 1 | 1 | 1 |
10-3 | A+0.05mg H./kg | 1b | 1 | 1 | 1 |
10-4 | A+0.07mg H./kg | 1b | 1 | 1 | 1 |
10-5 | A+014mg H./kg | 1b | 1 | 1 | 1 |
10-6 | A+0.28mg H./kg | 1 | 1 | 1 | 1 |
注解:
当没有添加破乳剂时,仅仅观察到非常慢的破乳化作用。评定值4是不能接受的;形成稳定的乳剂。
甚至及其少量的疏水蛋白也显示出非常好的破乳化效果。0.01ppm的 疏水蛋白足可以在1分钟内导致可接受的结果。为了达到与0.07mg疏水蛋白/kg相同的效果,需要向每kg燃料中添加1.45mg市场上可以购买的基于酚树脂的破乳剂。因此,当使用疏水蛋白时,仅仅约常规破乳剂所需用量的1/20即可达到相同的效果。
比较实施例11
使用其他蛋白质作为燃料添加剂
利用与实施例10相似的方法,测试非疏水蛋白在燃料中的用途。
本实验利用牛血清白蛋白(BSA)和酪蛋白进行。这些蛋白质是市场上可以购买的。也利用如SEQ ID No.15和16所示的yaad,即没有连接疏水蛋白的融合配偶体本身。
分别添加各蛋白质到市场上可以购买的Eurosuper燃料(与EN 228一致)中,所述蛋白质的浓度为0.07mg/kg,所述燃料已含上述特效添加剂包A 1000mg/kg。只添加A,不含蛋白质的燃料作为参比。
如上所述,依照DIN51415使用每一燃料样品进行乳化实验。
表2
1min. | 5min. | 30min. | 60min. | ||
11-V3(对照) | A | 4 | 4 | 2 | 1b |
11-1 | A+0.07mg BSA/kg | 2 | 1 | 1 | 1 |
11-2 | A+0.07mg yaad/kg | 3 | 1 | 1 | 1 |
11-2 | A+0.07mg酪蛋白/kg | 3 | 1b | 1 | 1 |
注解:
当没有添加破乳剂时,乳剂分离的发生与实施例10一样慢。评定值4是不能接受的;形成稳定的乳剂。尽管所使用的蛋白质具有破乳化效果,但破乳化作用的速率低于使用疏水蛋白时的速率。
实施例12
利用疏水蛋白浓缩物(yaad-Xa-dewA-His6)作为原油的破乳剂
利用实施例8(SEQ ID NO.19和20)所描述的疏水蛋白浓缩物进行实验。
在该实验中,将不同量的疏水蛋白浓缩物添加到50ml原油中(样品exWintershall AG,Emlichheim,well 301;在常规破乳化作用后,残留的水含量约为3%)。原油中疏水蛋白的浓度为1ppm、10ppm和40ppm。在匀浆化处理后,2000rpm离心混合物10分钟。结果在表3中列出。
表3
添加的疏水蛋白 | 自由水相 | 乳剂相 |
未添加 | 0.4% | 2.4% |
1ppm | 0.8% | 2.0% |
10ppm | 2.4% | 0.4% |
40ppm | 2.4% | 0.4% |
添加10ppm和40ppm疏水蛋白浓缩物之后,自由水相构成主要组分。
实施例13
利用疏水蛋白浓缩物(yaad-Xa-dewA-His6)作为分级聚合物
利用实施例8(SEQ ID NO.19和20)所述的疏水蛋白浓缩物进行实验。
在每例中,开始加入150g钠盐形式的聚丙烯酸(SokalanCP 10 S;Mw 4000g/mol,依据DE 199 50 941 A1)到两个玻璃烧杯中,之后分别添加75g异丙醇。搅拌混合物5分钟,之后分别添加146g的异丙醇/水(1/1比率)并搅拌混合物5分钟。
添加50ppm疏水蛋白(1.64m,11.3mg/ml)到玻璃烧杯A中,并搅拌混合物5分钟。疏水蛋白在澄清的溶液中形成白色条带,5分钟后该条带完全溶解。两个玻璃烧杯中都添加19.75g 50%的NaOH,并搅拌混合物5分钟。
疏水蛋白存在时马上形成乳状溶液,而没有疏水蛋白时形成浓烈的不透明溶液。在搅拌15分钟后,分别转移玻璃烧杯中的内容物到500ml分液漏斗,轻摇漏斗,观察确定相分离所需要的时间长短。
对于包含疏水蛋白的样品,10分钟后可看到清楚的相分离;不含疏水蛋白时,最初形成泡沫状的“过渡层”;换句话说,没有形成清晰的相界面。不含疏水蛋白时,清晰的相界面在40分钟后才形成。
分离直到清晰的相界面出现的时间:
-有疏水蛋白:12分钟
-没有疏水蛋白:40分钟
实施例14,比较实施例15
55℃时,疏水蛋白融合蛋白(yaad-Xa-dewA-His
6
)及牛血清白蛋白(BSA)在油-水乳剂中作为破乳剂的用途
利用实施例8(SEQ ID NO.19和20)所述的疏水蛋白浓缩物以及利用市场上可以买到的牛血清白蛋白(BSA)溶液进行实验。
如下测试破乳化能力:
所使用的油为液压油。
开始在100ml量量筒中加入40ml蒸馏水,基于水量添加5ppm相关的蛋白质,或者基于总体系添加2.5ppm。然后加入40ml液压油,并在55℃水浴中平衡该体系。温度平衡时间为20分钟。此后,利用叶片式搅拌机在1500rpm使油和水乳化15分钟。使油在水相中乳化。此后,观察相分离。所给出的是每例中再分离的水相的量,以ml表示。
在一个实验组中,所使用的两种蛋白质的水性溶液是不经改变的。结果如图2中曲线图1所示。
在第二个实验组中,首先调节两种蛋白质溶液,在室温RT条件下,利用HCl调节pH值到1并在pH为1时放置24小时。此后,再一次利用NaOH调节pH值到7。结果如图2中曲线图2所示。
注解:
与没有破乳剂的样品相比,BSA仅能轻微提高油-水乳剂的破乳化速率。另一方面,当添加疏水蛋白时,可以观察到破乳化作用显著地加速。
序列表中DNA和多肽序列的命名
dewA DNA及多肽序列 | SEQ ID NO:1 |
dewA多肽序列 | SEQ ID NO:2 |
rodA DNA及多肽序列 | SEQ ID NO:3 |
rodA多肽序列 | SEQ ID NO:4 |
hypA DNA及多肽序列 | SEQ ID NO:5 |
hypA多肽序列 | SEQ ID NO:6 |
hypB DNA及多肽序列 | SEQ ID NO:7 |
hypB多肽序列 | SEQ ID NO:8 |
sc3DNA及多肽序列 | SEQ ID NO:9 |
sc3多肽序列 | SEQ ID NO:10 |
basf1 DNA及多肽序列 | SEQ ID NO:11 |
basf1 多肽序列 | SEQ ID NO:12 |
basf2 DNA及多肽序列 | SEQ ID NO:13 |
basf2多肽序列 | SEQ ID NO:14 |
yaad DNA及多肽序列 | SEQ ID NO:15 |
yaad多肽序列 | SEQ ID NO:16 |
yaae DNA及多肽序列 | SEQ ID NO:17 |
yaae多肽序列 | SEQ ID NO:18 |
yaad-Xa-dewA-his DNA及多肽序列 | SEQ ID NO:19 |
yaad-Xa-dewA-his多肽序列 | SEQ ID NO:20 |
yaad-Xa-rodA-his DNA及多肽序列 | SEQ ID NO:21 |
yaad-Xa-rodA-his多肽序列 | SEQ ID NO:22 |
yaad-Xa-basf1-his DNA及多肽序列 | SEQ ID NO:23 |
yaad-Xa-basf1-his多肽序列 | SEQ ID NO:24 |
序列表
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acc atc gcc gcc ggt ggc acg tgt act acg ggg tcg ctc tct tgc tgc 192
Thr Ile Ala Ala Gly Gly Thr Cys Thr Thr Gly Ser Leu Ser Cys Cys
50 55 60
aac cag gtt caa tcg gcg agc agc agc cct gtt acc gcc ctc ctc ggc 240
Asn Gln Val Gln Ser Ala Ser Ser Ser Pro Val Thr Ala Leu Leu Gly
65 70 75 80
ctg ctc ggc att gtc ctc agc gac ctc aac gtt ctc gtt ggc atc agc 288
Leu Leu Gly Ile Val Leu Ser Asp Leu Asn Val Leu Val Gly Ile Ser
85 90 95
tgc tct ccc ctc act gtc atc ggt gtc gga ggc agc ggc tgt tcg gcg 336
Cys Ser Pro Leu Thr Val Ile Gly Val Gly Gly Ser Gly Cys Ser Ala
100 105 110
cag acc gtc tgc tgc gaa aac acc caa ttc aac ggg ctg atc aac atc 384
Gln Thr Val Cys Cys Glu Asn Thr Gln Phe Asn Gly Leu Ile Asn Ile
115 120 125
ggt tgc acc ccc atc aac atc ctc 408
Gly Cys Thr Pro Ile Asn Ile Leu
130 135
<210>10
<211>136
<212>PRT
<213>basf-sc3
<400>10
Met Phe Ala Arg Leu Pro Val Val Phe Leu Tyr Ala Phe Val Ala Phe
1 5 10 15
Gly Ala Leu Val Ala Ala Leu Pro Gly Gly His Pro Gly Thr Thr Thr
20 25 30
Pro Pro Val Thr Thr Thr Val Thr Val Thr Thr Pro Pro Ser Thr Thr
35 40 45
Thr Ile Ala Ala Gly Gly Thr Cys Thr Thr Gly Ser Leu Ser Cys Cys
50 55 60
Asn Gln Val Gln Ser Ala Ser Ser Ser Pro Val Thr Ala Leu Leu Gly
65 70 75 80
Leu Leu Gly Ile Val Leu Ser Asp Leu Asn Val Leu Val Gly Ile Ser
85 90 95
Cys Ser Pro Leu Thr Val Ile Gly Val Gly Gly Ser Gly Cys Ser Ala
100 105 110
Gln Thr Val Cys Cys Glu Asn Thr Gln Phe Asn Gly Leu Ile Asn Ile
115 120 125
Gly Cys Thr Pro Ile Asn Ile Leu
130 135
<210>11
<211>483
<212>DNA
<213>basf-BASF1
<220>
<221>CDS
<222>(1)..(483)
<223>
<400>11
atg aag ttc tcc gtc tcc gcc gcc gtc ctc gcc ttc gcc gcc tcc gtc 48
Met Lys Phe Ser Val Ser Ala Ala Val Leu Ala Phe Ala Ala Ser Val
1 5 10 15
gcc gcc ctc cct cag cac gac tcc gcc gcc ggc aac ggc aac ggc gtc 96
Ala Ala Leu Pro Gln His Asp Ser Ala Ala Gly Asn Gly Asn Gly Val
20 25 30
ggc aac aag ttc cct gtc cct gac gac gtc acc gtc aag cag gcc acc 144
Gly Asn Lys Phe Pro Val Pro Asp Asp Val Thr Val Lys Gln Ala Thr
35 40 45
gac aag tgc ggc gac cag gcc cag ctc tcc tgc tgc aac aag gcc acc 192
Asp Lys Cys Gly Asp Gln Ala Gln Leu Ser Cys Cys Asn Lys Ala Thr
50 55 60
tac gcc ggc gac gtc ctc acc gac atc gac gag ggc atc ctc gcc ggc 240
Tyr Ala Gly Asp Val Leu Thr Asp Ile Asp Glu Gly Ile Leu Ala Gly
65 70 75 80
ctc ctc aag aac ctc atc ggc ggc ggc tcc ggc tcc gag ggc ctc ggc 288
Leu Leu Lys Asn Leu Ile Gly Gly Gly Ser Gly Ser Glu Gly Leu Gly
85 90 95
ctc ttc gac cag tgc gtc aag ctc gac ctc cag atc tcc gtc atc ggc 336
Leu Phe Asp Gln Cys Val Lys Leu Asp Leu Gln Ile Ser Val Ile Gly
100 105 110
atc cct atc cag gac ctc ctc aac cag gtc aac aag cag tgc aag cag 384
Ile Pro Ile Gln Asp Leu Leu Asn Gln Val Asn Lys Gln Cys Lys Gln
115 120 125
aac atc gcc tgc tgc cag aac tcc cct tcc gac gcc acc ggc tcc ctc 432
Asn Ile Ala Cys Cys Gln Asn Ser Pro Ser Asp Ala Thr Gly Ser Leu
130 135 140
gtc aac ctc ggc ctc ggc aac cct tgc atc cct gtc tcc ctc ctc cat 480
Val Asn Leu Gly Leu Gly Asn Pro Cys Ile Pro Val Ser Leu Leu His
145 150 155 160
atg 483
Met
<210>12
<211>161
<212>PRT
<213>basf-BASF1
<400>12
Met Lys Phe Ser Val Ser Ala Ala Val Leu Ala Phe Ala Ala Ser Val
1 5 10 15
Ala Ala Leu Pro Gln His Asp Ser Ala Ala Gly Asn Gly Asn Gly Val
20 25 30
Gly Asn Lys Phe Pro Val Pro Asp Asp Val Thr Val Lys Gln Ala Thr
35 40 45
Asp Lys Cys Gly Asp Gln Ala Gln Leu Ser Cys Cys Asn Lys Ala Thr
50 55 60
Tyr Ala Gly Asp Val Leu Thr Asp Ile Asp Glu Gly Ile Leu Ala Gly
65 70 75 80
Leu Leu Lys Asn Leu Ile Gly Gly Gly Ser Gly Ser Glu Gly Leu Gly
85 90 95
Leu Phe Asp Gln Cys Val Lys Leu Asp Leu Gln Ile Ser Val Ile Gly
100 105 110
Ile Pro Ile Gln Asp Leu Leu Asn Gln Val Asn Lys Gln Cys Lys Gln
115 120 125
Asn Ile Ala Cys Cys Gln Asn Ser Pro Ser Asp Ala Thr Gly Ser Leu
130 135 140
Val Asn Leu Gly Leu Gly Asn Pro Cys Ile Pro Val Ser Leu Leu His
145 150 155 160
Met
<210>13
<211>465
<212>DNA
<213>basf-BASF2
<220>
<221>CDS
<222>(1)..(465)
<223>
<400>13
atg aag ttc tcc gtc tcc gcc gcc gtc ctc gcc ttc gcc gcc tcc gtc 48
Met Lys Phe Ser Val Ser Ala Ala Val Leu Ala Phe Ala Ala Ser Val
1 5 10 15
gcc gcc ctc cct cag cac gac tcc gcc gcc ggc aac ggc aac ggc gtc 96
Ala Ala Leu Pro Gln His Asp Ser Ala Ala Gly Asn Gly Asn Gly Val
20 25 30
ggc aac aag ttc cct gtc cct gac gac gtc acc gtc aag cag gcc acc 144
Gly Asn Lys Phe Pro Val Pro Asp Asp Val Thr Val Lys Gln Ala Thr
35 40 45
gac aag tgc ggc gac cag gcc cag ctc tcc tgc tgc aac aag gcc acc 192
Asp Lys Cys Gly Asp Gln Ala Gln Leu Ser Cys Cys Asn Lys Ala Thr
50 55 60
tac gcc ggc gac gtc acc gac atc gac gag ggc atc ctc gcc ggc ctc 240
Tyr Ala Gly Asp Val Thr Asp Ile Asp Glu Gly Ile Leu Ala Gly Leu
65 70 75 80
ctc aag aac ctc atc ggc ggc ggc tcc ggc tcc gag ggc ctc ggc ctc 288
Leu Lys Asn Leu Ile Gly Gly Gly Ser Gly Ser Glu Gly Leu Gly Leu
85 90 95
ttc gac cag tgc gtc aag ctc gac ctc cag atc tcc gtc atc ggc atc 336
Phe Asp Gln Cys Val Lys Leu Asp Leu Gln Ile Ser Val Ile Gly Ile
100 105 110
cct atc cag gac ctc ctc aac cag cag tgc aag cag aac atc gcc tgc 384
Pro Ile Gln Asp Leu Leu Asn Gln Gln Cys Lys Gln Asn Ile Ala Cys
115 120 125
tgc cag aac tcc cct tcc gac gcc acc ggc tcc ctc gtc aac ctc ggc 432
Cys Gln Asn Ser Pro Ser Asp Ala Thr Gly Ser Leu Val Asn Leu Gly
130 135 140
aac cct tgc atc cct gtc tcc ctc ctc cat atg 465
Asn Pro Cys Ile Pro Val Ser Leu Leu His Met
145 150 155
<210>14
<211>155
<212>PRT
<213>basf-BASF2
<400>14
Met Lys Phe Ser Val Ser Ala Ala Val Leu Ala Phe Ala Ala Ser Val
1 5 10 15
Ala Ala Leu Pro Gln His Asp Ser Ala Ala Gly Asn Gly Asn Gly Val
20 25 30
Gly Asn Lys Phe Pro Val Pro Asp Asp Val Thr Val Lys Gln Ala Thr
35 40 45
Asp Lys Cys Gly Asp Gln Ala Gln Leu Ser Cys Cys Asn Lys Ala Thr
50 55 60
Tyr Ala Gly Asp Val Thr Asp Ile Asp Glu Gly Ile Leu Ala Gly Leu
65 70 75 80
Leu Lys Asn Leu Ile Gly Gly Gly Ser Gly Ser Glu Gly Leu Gly Leu
85 90 95
Phe Asp Gln Cys Val Lys Leu Asp Leu Gln Ile Ser Val Ile Gly Ile
100 105 110
ProIle Gln Asp Leu Leu Asn Gln Gln Cys Lys Gln Asn Ile Ala Cys
115 120 125
Cys Gln Asn Ser Pro Ser Asp Ala Thr Gly Ser Leu Val Asn Leu Gly
130 135 140
Asn Pro Cys Ile Pro Val Ser Leu Leu His Met
145 150 155
<210>15
<211>882
<212>DNA
<213>basf-yaad
<220>
<221>CDS
<222>(1)..(882)
<223>
<400>15
atg gct caa aca ggt act gaa cgt gta aaa cgc gga atg gca gaa atg 48
Met Ala Gln Thr Gly Thr Glu Arg Val Lys Arg Gly Met Ala Glu Met
1 5 10 15
caa aaa ggc ggc gtc atc atg gac gtc atc aat gcg gaa caa gcg aaa 96
Gln Lys Gly Gly Val Ile Met Asp Val Ile Asn Ala Glu Gln Ala Lys
20 25 30
atc gct gaa gaa gct gga gct gtc gct gta atg gcg cta gaa cgt gtg 144
Ile Ala Glu Glu Ala Gly Ala Val Ala Val Met Ala Leu Glu Arg Val
35 40 45
cca gca gat att cgc gcg gct gga gga gtt gcc cgt atg gct gac cct 192
Pro Ala Asp Ile Arg Ala Ala Gly Gly Val Ala Arg Met Ala Asp Pro
50 55 60
aca atc gtg gaa gaa gta atg aat gca gta tct atc ccg gta atg gca 240
Thr Ile Val Glu Glu Val Met Asn Ala Val Ser Ile Pro Val Met Ala
65 70 75 80
aaa gcg cgt atc gga cat att gtt gaa gcg cgt gtg ctt gaa gct atg 288
Lys Ala Arg Ile Gly His Ile Val Glu Ala Arg Val Leu Glu Ala Met
85 90 95
ggt gtt gac tat att gat gaa agt gaa gtt ctg acg ccg gct gac gaa 336
Gly Val Asp Tyr Ile Asp Glu Ser Glu Val Leu Thr Pro Ala Asp Glu
100 105 110
gaa ttt cat tta aat aaa aat gaa tac aca gtt cct ttt gtc tgt ggc 384
Glu Phe His Leu Asn Lys Asn Glu Tyr Thr Val Pro Phe Val Cys Gly
115 120 125
tgc cgt gat ctt ggt gaa gca aca cgc cgt att gcg gaa ggt gct tct 432
Cys Arg Asp Leu Gly Glu Ala Thr Arg ArgIle Ala Glu Gly Ala Ser
130 135 140
atg ctt cgc aca aaa ggt gag cct gga aca ggt aat att gtt gag gct 480
Met Leu Arg Thr Lys Gly Glu Pro Gly Thr Gly AsnIle Val Glu Ala
145 150 155 160
gtt cgc cat atg cgt aaa gtt aac gct caa gtg cgc aaa gta gtt gcg 528
Val Arg His Met Arg Lys Val Asn Ala Gln Val Arg Lys Val Val Ala
165 170 175
atg agt gag gat gag cta atg aca gaa gcg aaa aac cta ggt gct cct 576
Met Ser Glu Asp Glu Leu Met Thr Glu Ala Lys Asn Leu Gly Ala Pro
180 185 190
tac gag ctt ctt ctt caa att aaa aaa gac ggc aag ctt cct gtc gtt 624
Tyr Glu Leu Leu Leu Gln Ile Lys Lys Asp Gly Lys Leu Pro Val Val
195 200 205
aac ttt gcc gct ggc ggc gta gca act cca gct gat gct gct ctc atg 672
Asn Phe Ala Ala Gly Gly Val Ala Thr Pro Ala Asp Ala Ala Leu Met
210 215 220
atg cag ctt ggt gct gac gga gta ttt gtt ggt tct ggt att ttt aaa 720
Met Gln Leu Gly Ala Asp Gly Val Phe Val Gly Ser Gly Ile Phe Lys
225 230 235 240
tca gac aac cct gct aaa ttt gcg aaa gca att gtg gaa gca aca act 768
Ser Asp Asn Pro Ala Lys Phe Ala Lys Ala Ile Val Glu Ala Thr Thr
245 250 255
cac ttt act gat tac aaa tta atc gct gag ttg tca aaa gag ctt ggt 816
His Phe Thr Asp Tyr Lys Leu Ile Ala Glu Leu Ser Lys Glu Leu Gly
260 265 270
act gca atg aaa ggg att gaa atc tca aac tta ctt cca gaa cag cgt 864
Thr Ala Met Lys Gly Ile Glu Ile Ser Asn Leu Leu Pro Glu Gln Arg
275 280 285
atg caa gaa cgc ggc tgg 882
Met Gln Glu Arg Gly Trp
290
<210>16
<211>294
<212>PRT
<213>basf-yaad
<400>16
Met Ala Gln Thr Gly Thr Glu Arg Val Lys Arg Gly Met Ala Glu Met
1 5 10 15
Gln Lys Gly Gly Val Ile Met Asp Val Ile Asn Ala Glu Gln Ala Lys
20 25 30
Ile Ala Glu Glu Ala Gly Ala Val Ala Val Met Ala Leu Glu Arg Val
35 40 45
Pro Ala Asp Ile Arg Ala Ala Gly Gly Val Ala Arg Met Ala Asp Pro
50 55 60
Thr Ile Val Glu Glu Val Met Asn Ala Val Ser Ile Pro Val Met Ala
65 70 75 80
Lys Ala Arg Ile Gly His Ile Val Glu Ala Arg Val Leu Glu Ala Met
85 90 95
Gly Val Asp Tyr Ile Asp Glu Ser Glu Val Leu Thr Pro Ala Asp Glu
100 105 110
Glu Phe His Leu Asn Lys Asn Glu Tyr Thr Val Pro Phe Val Cys Gly
115 120 125
Cys Arg Asp Leu Gly Glu Ala Thr Arg Arg Ile Ala Glu Gly Ala Ser
130 135 140
Met Leu Arg Thr Lys Gly Glu Pro Gly Thr Gly Asn Ile Val Glu Ala
145 150 155 160
Val Arg His Met Arg Lys Val Asn Ala Gln Val Arg Lys Val Val Ala
165 170 175
Met Ser Glu Asp Glu Leu Met Thr Glu Ala Lys Asn Leu Gly Ala Pro
180 185 190
Tyr Glu Leu Leu Leu Gln Ile Lys Lys Asp Gly Lys Leu Pro Val Val
195 200 205
Asn Phe Ala Ala Gly Gly Val Ala Thr Pro Ala Asp Ala Ala Leu Met
210 215 220
Met Gln Leu Gly Ala Asp Gly Val Phe Val Gly Ser Gly Ile Phe Lys
225 230 235 240
Ser Asp Asn Pro Ala Lys Phe Ala Lys Ala Ile Val Glu Ala Thr Thr
245 250 255
His Phe Thr Asp Tyr Lys Leu Ile Ala Glu Leu Ser Lys Glu Leu Gly
260 265 270
Thr Ala Met Lys Gly Ile Glu Ile Ser Asn Leu Leu Pro Glu Gln Arg
275 280 285
Met Gln Glu Arg Gly Trp
290
<210>17
<211>591
<212>DNA
<213>basf-yaae
<220>
<221>CDS
<222>(1)..(591)
<223>
<400>17
atg gga tta aca ata ggt gta cta gga ctt caa gga gca gtt aga gag 48
Met Gly Leu Thr Ile Gly Val Leu Gly Leu Gln Gly Ala Val Arg Glu
1 5 10 15
cac atc cat gcg att gaa gca tgc ggc gcg gct ggt ctt gtc gta aaa 96
His Ile His Ala Ile Glu Ala Cys Gly Ala Ala Gly Leu Val Val Lys
20 25 30
cgt ccg gag cag ctg aac gaa gtt gac ggg ttg att ttg ccg ggc ggt 144
Arg Pro Glu Gln Leu Asn Glu Val Asp Gly Leu Ile Leu Pro Gly Gly
35 40 45
gag agc acg acg atg cgc cgt ttg atc gat acg tat caa ttc atg gag 192
Glu Ser Thr Thr Met Arg Arg Leu Ile Asp Thr Tyr Gln Phe Met Glu
50 55 60
ccg ctt cgt gaa ttc gct gct cag ggc aaa ccg atg ttt gga aca tgt 240
Pro Leu Arg Glu Phe Ala Ala Gln Gly Lys Pro Met Phe Gly Thr Cys
65 70 75 80
gcc gga tta att ata tta gca aaa gaa att gcc ggt tca gat aat cct 288
Ala Gly Leu Ile Ile Leu Ala Lys Glu Ile Ala Gly Ser Asp Asn Pro
85 90 95
cat tta ggt ctt ctg aat gtg gtt gta gaa cgt aat tca ttt ggc cgg 336
His Leu Gly Leu Leu Asn Val Val Val Glu Arg Asn Ser Phe Gly Arg
100 105 110
cag gtt gac agc ttt gaa gct gat tta aca att aaa ggc ttg gac gag 384
Gln Val Asp Ser Phe Glu Ala Asp Leu Thr Ile Lys Gly Leu Asp Glu
115 120 125
cct ttt act ggg gta ttc atc cgt gct ccg cat att tta gaa gct ggt 432
Pro Phe Thr Gly Val Phe Ile Arg Ala Pro His Ile Leu Glu Ala Gly
130 135 140
gaa aat gtt gaa gtt cta tcg gag cat aat ggt cgt att gta gcc gcg 480
Glu Asn Val Glu Val Leu Ser Glu His Asn Gly Arg Ile Val Ala Ala
145 150 155 160
aaa cag ggg caa ttc ctt ggc tgc tca ttc cat ccg gag ctg aca gaa 528
Lys Gln Gly Gln Phe Leu Gly Cys Ser Phe His Pro Glu Leu Thr Glu
165 170 175
gat cac cga gtg acg cag ctg ttt gtt gaa atg gtt gag gaa tat aag 576
Asp His Arg Val Thr Gln Leu Phe Val Glu Met Val Glu Glu Tyr Lys
180 185 190
caa aag gca ctt gta 591
Gln Lys Ala Leu Val
195
<210>18
<211>197
<212>PRT
<213>basf-yaae
<400>18
Met Gly Leu Thr Ile Gly Val Leu Gly Leu Gln Gly Ala Val Arg Glu
1 5 10 15
His Ile His Ala Ile Glu Ala Cys Gly Ala Ala Gly Leu Val Val Lys
20 25 30
Arg Pro Glu Gln Leu Asn Glu Val Asp Gly Leu Ile Leu Pro Gly Gly
35 40 45
Glu Ser Thr Thr Met Arg Arg Leu Ile Asp Thr Tyr Gln Phe Met Glu
50 55 60
Pro Leu Arg Glu Phe Ala Ala Gln Gly Lys Pro Met Phe Gly Thr Cys
65 70 75 80
Ala Gly Leu Ile Ile Leu Ala Lys Glu Ile Ala Gly Ser Asp Asn Pro
85 90 95
His Leu Gly Leu Leu Asn Val Val Val Glu Arg Asn Ser Phe Gly Arg
100 105 110
Gln Val Asp Ser Phe Glu Ala Asp Leu Thr Ile Lys Gly Leu Asp Glu
115 120 125
Pro Phe Thr Gly Val Phe Ile Arg Ala Pro His Ile Leu Glu Ala Gly
130 135 140
Glu Asn Val Glu Val Leu Ser Glu His Asn Gly Arg Ile Val Ala Ala
145 150 155 160
Lys Gln Gly Gln Phe Leu Gly Cys Ser Phe His Pro Glu Leu Thr Glu
165 170 175
Asp His Arg Val Thr Gln Leu Phe Val Glu Met Val Glu Glu Tyr Lys
180 185 190
Gln Lys Ala Leu Val
195
<210>19
<211>1329
<212>DNA
<213>basf-yaad-Xa-dewA-his
<220>
<221>CDS
<222>(1)..(1329)
<223>
<400>19
atg gct caa aca ggt act gaa cgt gta aaa cgc gga atg gca gaa atg 48
Met Ala Gln Thr Gly Thr Glu Arg Val Lys Arg Gly Met Ala Glu Met
1 5 10 15
caa aaa ggc ggc gtc atc atg gac gtc atc aat gcg gaa caa gcg aaa 96
Gln Lys Gly Gly Val Ile Met Asp Val Ile Asn Ala Glu Gln Ala Lys
20 25 30
atc gct gaa gaa gct gga gct gtc gct gta atg gcg cta gaa cgt gtg 144
Ile Ala Glu Glu Ala Gly Ala Val Ala Val Met Ala Leu Glu Arg Val
35 40 45
cca gca gat att cgc gcg gct gga gga gtt gcc cgt atg gct gac cct 192
Pro Ala Asp Ile Arg Ala Ala Gly Gly Val Ala Arg Met Ala Asp Pro
50 55 60
aca atc gtg gaa gaa gta atg aat gca gta tct atc ccg gta atg gca 240
Thr Ile Val Glu Glu Val Met Asn Ala Val Ser Ile Pro Val Met Ala
65 70 75 80
aaa gcg cgt atc gga cat att gtt gaa gcg cgt gtg ctt gaa gct atg 288
Lys Ala Arg Ile Gly His Ile Val Glu Ala Arg Val Leu Glu Ala Met
85 90 95
ggt gtt gac tat att gat gaa agt gaa gtt ctg acg ccg gct gac gaa 336
Gly Val Asp Tyr Ile Asp Glu Ser Glu Val Leu Thr Pro Ala Asp Glu
100 105 110
gaa ttt cat tta aat aaa aat gaa tac aca gtt cct ttt gtc tgt ggc 384
Glu Phe His Leu Asn Lys Asn Glu Tyr Thr Val Pro Phe Val Cys Gly
115 120 125
tgc cgt gat ctt ggt gaa gca aca cgc cgt att gcg gaa ggt gct tct 432
Cys Arg Asp Leu Gly Glu Ala Thr Arg Arg Ile Ala Glu Gly Ala Ser
130 135 140
atg ctt cgc aca aaa ggt gag cct gga aca ggt aat att gtt gag gct 480
Met Leu Arg Thr Lys Gly Glu Pro Gly Thr Gly Asn Ile Val Glu Ala
145 150 155 160
gtt cgc cat atg cgt aaa gtt aac gct caa gtg cgc aaa gta gtt gcg 528
Val Arg His Met Arg Lys Val Asn Ala Gln Val Arg Lys Val Val Ala
165 170 175
atg agt gag gat gag cta atg aca gaa gcg aaa aac cta ggt gct cct 576
Met Ser Glu Asp Glu Leu Met Thr Glu Ala Lys Asn Leu Gly Ala Pro
180 185 190
tac gag ctt ctt ctt caa att aaa aaa gac ggc aag ctt cct gtc gtt 624
Tyr Glu Leu Leu Leu Gln Ile Lys Lys Asp Gly Lys Leu Pro Val Val
195 200 205
aac ttt gcc gct ggc ggc gta gca act cca gct gat gct gct ctc atg 672
Asn Phe Ala Ala Gly Gly Val Ala Thr Pro Ala Asp Ala Ala Leu Met
210 215 220
atg cag ctt ggt gct gac gga gta ttt gtt ggt tct ggt att ttt aaa 720
Met Gln Leu Gly Ala Asp Gly Val Phe Val Gly Ser Gly Ile Phe Lys
225 230 235 240
tca gac aac cct gct aaa ttt gcg aaa gca att gtg gaa gca aca act 768
Ser Asp Asn Pro Ala Lys Phe Ala Lys Ala Ile Val Glu Ala Thr Thr
245 250 255
cac ttt act gat tac aaa tta atc gct gag ttg tca aaa gag ctt ggt 816
His Phe Thr Asp Tyr Lys Leu Ile Ala Glu Leu Ser Lys Glu Leu Gly
260 265 270
act gca atg aaa ggg att gaa atc tca aac tta ctt cca gaa cag cgt 864
Thr Ala Met Lys Gly Ile Glu Ile Ser Asn Leu Leu Pro Glu Gln Arg
275 280 285
atg caa gaa cgc ggc tgg aga tcc att gaa ggc cgc atg cgc ttc atc 912
Met Gln Glu Arg Gly Trp Arg Ser Ile Glu Gly Arg Met Arg Phe Ile
290 295 300
gtc tct ctc ctc gcc ttc act gcc gcg gcc acc gcg acc gcc ctc ccg 960
Val Ser Leu Leu Ala Phe Thr Ala Ala Ala Thr Ala Thr Ala Leu Pro
305 310 315 320
gcc tct gcc gca aag aac gcg aag ctg gcc acc tcg gcg gcc ttc gcc 1008
Ala Ser Ala Ala Lys Asn Ala Lys Leu Ala Thr Ser Ala Ala Phe Ala
325 330 335
aag cag gct gaa ggc acc acc tgc aat gtc ggc tcg atc gct tgc tgc 1056
Lys Gln Ala Glu Gly Thr Thr Cys Asn Val Gly Ser Ile Ala Cys Cys
340 345 350
aac tcc ccc gct gag acc aac aac gac agt ctg ttg agc ggt ctg ctc 1104
Asn Ser Pro Ala Glu Thr Asn Asn Asp Ser Leu Leu Ser Gly Leu Leu
355 360 365
ggt gct ggc ctt ctc aac ggg ctc tcg ggc aac act ggc agc gcc tgc 1152
Gly Ala Gly Leu Leu Asn Gly Leu Ser Gly Asn Thr Gly Ser Ala Cys
370 375 380
gcc aag gcg agc ttg att gac cag ctg ggt ctg ctc gct ctc gtc gac 1200
Ala Lys Ala Ser Leu Ile Asp Gln Leu Gly Leu Leu Ala Leu Val Asp
385 390 395 400
cac act gag gaa ggc ccc gtc tgc aag aac atc gtc gct tgc tgc cct 1248
His Thr Glu Glu Gly Pro Val Cys Lys Asn Ile Val Ala Cys Cys Pro
405 410 415
gag gga acc acc aac tgt gtt gcc gtc gac aac gct ggc gct ggt acc 1296
Glu Gly Thr Thr Asn Cys Val Ala Val Asp Asn Ala Gly Ala Gly Thr
420 425 430
aag gct gag gga tct cat cac cat cac cat cac 1329
Lys Ala Glu Gly Ser His His His His His His
435 440
<210>20
<211>443
<212>PRT
<213>basf-yaad-Xa-dewA-his
<400>20
Met Ala Gln Thr Gly Thr Glu Arg Val Lys Arg Gly Met Ala Glu Met
1 5 10 15
Gln Lys Gly Gly Val Ile Met Asp Val Ile Asn Ala Glu Gln Ala Lys
20 25 30
Ile Ala Glu Glu Ala Gly Ala Val Ala Val Met Ala Leu Glu Arg Val
35 40 45
Pro Ala Asp Ile Arg Ala Ala Gly Gly Val Ala Arg Met Ala Asp Pro
50 55 60
Thr Ile Val Glu Glu Val Met Asn Ala Val Ser Ile Pro Val Met Ala
65 70 75 80
Lys Ala Arg Ile Gly His Ile Val Glu Ala Arg Val Leu Glu Ala Met
85 90 95
Gly Val Asp Tyr Ile Asp Glu Ser Glu Val Leu Thr Pro Ala Asp Glu
100 105 110
Glu Phe His Leu Asn Lys Asn Glu Tyr Thr Val Pro Phe Val Cys Gly
115 120 125
Cys Arg Asp Leu Gly Glu Ala Thr Arg Arg Ile Ala Glu Gly Ala Ser
130 135 140
Met Leu Arg Thr Lys Gly Glu Pro Gly Thr Gly Asn Ile Val Glu Ala
145 150 155 160
Val Arg His Met Arg Lys Val Asn Ala Gln Val Arg Lys Val Val Ala
165 170 175
Met Ser Glu Asp Glu Leu Met Thr Glu Ala Lys Asn Leu Gly Ala Pro
180 185 190
Tyr Glu Leu Leu Leu Gln Ile Lys Lys Asp Gly Lys Leu Pro Val Val
195 200 205
Asn Phe Ala Ala Gly Gly Val Ala Thr Pro Ala Asp Ala Ala Leu Met
210 215 220
Met Gln Leu Gly Ala Asp Gly Val Phe Val Gly Ser Gly Ile Phe Lys
225 230 235 240
Ser Asp Asn Pro Ala Lys Phe Ala Lys Ala Ile Val Glu Ala Thr Thr
245 250 255
His Phe Thr Asp Tyr Lys Leu Ile Ala Glu Leu Ser Lys Glu Leu Gly
260 265 270
Thr Ala Met Lys Gly Ile Glu Ile Ser Asn Leu Leu Pro Glu Gln Arg
275 280 285
Met Gln Glu Arg Gly Trp Arg Ser Ile Glu Gly Arg Met Arg Phe Ile
290 295 300
Val Ser Leu Leu Ala Phe Thr Ala Ala Ala Thr Ala Thr Ala Leu Pro
305 310 315 320
Ala Ser Ala Ala Lys Asn Ala Lys Leu Ala Thr Ser Ala Ala Phe Ala
325 330 335
Lys Gln Ala Glu Gly Thr Thr Cys Asn Val Gly Ser Ile Ala Cys Cys
340 345 350
Asn Ser Pro Ala Glu Thr Asn Asn Asp Ser Leu Leu Ser Gly Leu Leu
355 360 365
Gly Ala Gly Leu Leu Asn Gly Leu Ser Gly Asn Thr Gly Ser Ala Cys
370 375 380
Ala Lys Ala Ser Leu Ile Asp Gln Leu Gly Leu Leu Ala Leu Val Asp
385 390 395 400
His Thr Glu Glu Gly Pro Val Cys Lys Asn Ile Val Ala Cys Cys Pro
405 410 415
Glu Gly Thr Thr Asn Cys Val Ala Val Asp Asn Ala Gly Ala Gly Thr
420 425 430
Lys Ala Glu Gly Ser His His His His His His
435 440
<210>21
<211>1395
<212>DNA
<213>basf-yaad-Xa-rodA-his
<220>
<221>CDS
<222>(1)..(1395)
<223>
<400>21
atg gct caa aca ggt act gaa cgt gta aaa cgc gga atg gca gaa atg 48
Met Ala Gln Thr Gly Thr Glu Arg Val Lys Arg Gly Met Ala Glu Met
1 5 10 15
caa aaa ggc ggc gtc atc atg gac gtc atc aat gcg gaa caa gcg aaa 96
Gln Lys Gly Gly Val Ile Met Asp Val Ile Asn Ala Glu Gln Ala Lys
20 25 30
atc gct gaa gaa gct gga gct gtc gct gta atg gcg cta gaa cgt gtg 144
Ile Ala Glu Glu Ala Gly Ala Val Ala Val Met Ala Leu Glu Arg Val
35 40 45
cca gca gat att cgc gcg gct gga gga gtt gcc cgt atg gct gac cct 192
Pro Ala Asp Ile Arg Ala Ala Gly Gly Val Ala Arg Met Ala Asp Pro
50 55 60
aca atc gtg gaa gaa gta atg aat gca gta tct atc ccg gta atg gca 240
Thr Ile Val Glu Glu Val Met Asn Ala Val Ser Ile Pro Val Met Ala
65 70 75 80
aaa gcg cgt atc gga cat att gtt gaa gcg cgt gtg ctt gaa gct atg 288
Lys Ala Arg Ile Gly His Ile Val Glu Ala Arg Val Leu Glu Ala Met
85 90 95
ggt gtt gac tat att gat gaa agt gaa gtt ctg acg ccg gct gac gaa 336
Gly Val Asp Tyr Ile Asp Glu Ser Glu Val Leu Thr Pro Ala Asp Glu
100 105 110
gaa ttt cat tta aat aaa aat gaa tac aca gtt cct ttt gtc tgt ggc 384
Glu Phe His Leu Asn Lys Asn Glu Tyr Thr Val Pro Phe Val Cys Gly
115 120 125
tgc cgt gat ctt ggt gaa gca aca cgc cgt att gcg gaa ggt gct tct 432
Cys Arg Asp Leu Gly Glu Ala Thr Arg Arg Ile Ala Glu Gly Ala Ser
130 135 140
atg ctt cgc aca aaa ggt gag cct gga aca ggt aat att gtt gag gct 480
Met Leu Arg Thr Lys Gly Glu Pro Gly Thr Gly Asn Ile Val Glu Ala
145 150 155 160
gtt cgc cat atg cgt aaa gtt aac gct caa gtg cgc aaa gta gtt gcg 528
Val Arg His Met Arg Lys Val Asn Ala Gln Val Arg Lys Val Val Ala
165 170 175
atg agt gag gat gag cta atg aca gaa gcg aaa aac cta ggt gct cct 576
Met Ser Glu Asp Glu Leu Met Thr Glu Ala Lys Asn Leu Gly Ala Pro
180 185 190
tac gag ctt ctt ctt caa att aaa aaa gac ggc aag ctt cct gtc gtt 624
Tyr Glu Leu Leu Leu Gln Ile Lys Lys Asp Gly Lys Leu Pro Val Val
195 200 205
aac ttt gcc gct ggc ggc gta gca act cca gct gat gct gct ctc atg 672
Asn Phe Ala Ala Gly Gly Val Ala Thr Pro Ala Asp Ala Ala Leu Met
210 215 220
atg cag ctt ggt gct gac gga gta ttt gtt ggt tct ggt att ttt aaa 720
Met Gln Leu Gly Ala Asp Gly Val Phe Val Gly Ser Gly Ile Phe Lys
225 230 235 240
tca gac aac cct gct aaa ttt gcg aaa gca att gtg gaa gca aca act 768
Ser Asp Asn Pro Ala Lys Phe Ala Lys Ala Ile Val Glu Ala Thr Thr
245 250 255
cac ttt act gat tac aaa tta atc gct gag ttg tca aaa gag ctt ggt 816
His Phe Thr Asp Tyr Lys Leu Ile Ala Glu Leu Ser Lys Glu Leu Gly
260 265 270
act gca atg aaa ggg att gaa atc tca aac tta ctt cca gaa cag cgt 864
Thr Ala Met Lys GlyIle Glu Ile Ser Asn Leu Leu Pro Glu Gln Arg
275 280 285
atg caa gaa cgc ggc tgg aga tct att gaa ggc cgc atg aag ttc tcc 912
Met Gln Glu Arg Gly Trp Arg SerIle Glu Gly Arg Met Lys Phe Ser
290 295 300
att gct gcc gct gtc gtt gct ttc gcc gcc tcc gtc gcg gcc ctc cct 960
Ile Ala Ala Ala Val Val Ala Phe Ala Ala Ser Val Ala Ala Leu Pro
305 310 315 320
cct gcc cat gat tcc cag ttc gct ggc aat ggt gtt ggc aac aag ggc 1008
Pro Ala His Asp Ser Gln Phe Ala Gly Asn Gly Val Gly Asn Lys Gly
325 330 335
aac agc aac gtc aag ttc cct gtc ccc gaa aac gtg acc gtc aag cag 1056
Asn Ser Asn Val Lys Phe Pro Val Pro Glu Asn Val Thr Val Lys Gln
340 345 350
gcc tcc gac aag tgc ggt gac cag gcc cag ctc tct tgc tgc aac aag 1104
Ala Ser Asp Lys Cys Gly Asp Gln Ala Gln Leu Ser Cys Cys Asn Lys
355 360 365
gcc acg tac gcc ggt gac acc aca acc gtt gat gag ggt ctt ctg tct 1152
Ala Thr Tyr Ala Gly Asp Thr Thr Thr Val Asp Glu Gly Leu Leu Ser
370 375 380
ggt gcc ctc agc ggc ctc atc ggc gcc ggg tct ggt gcc gaa ggt ctt 1200
Gly Ala Leu Ser Gly Leu Ile Gly Ala Gly Ser Gly Ala Glu Gly Leu
385 390 395 400
ggt ctc ttc gat cag tgc tcc aag ctt gat gtt gct gtc ctc att ggc 1248
Gly Leu Phe Asp Gln Cys Ser Lys Leu Asp Val Ala Val Leu Ile Gly
405 410 415
atc caa gat ctt gtc aac cag aag tgc aag caa aac att gcc tgc tgc 1296
Ile Gln Asp Leu Val Asn Gln Lys Cys Lys Gln Asn Ile Ala Cys Cys
420 425 430
cag aac tcc ccc tcc agc gcg gat ggc aac ctt att ggt gtc ggt ctc 1344
Gln Asn Ser Pro Ser Ser Ala Asp Gly Asn Leu Ile Gly Val Gly Leu
435 440 445
cct tgc gtt gcc ctt ggc tcc atc ctc gga tct cat cac cat cac cat 1392
Pro Cys Val Ala Leu Gly Ser Ile Leu Gly Ser His His His His His
450 455 460
cac 1395
His
465
<210>22
<211>465
<212>PRT
<213>basf-yaad-Xa-rodA-his
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Met Ala Gln Thr Gly Thr Glu Arg Val Lys Arg Gly Met Ala Glu Met
1 5 10 15
Gln Lys Gly Gly Val Ile Met Asp Val Ile Asn Ala Glu Gln Ala Lys
20 25 30
Ile Ala Glu Glu Ala Gly Ala Val Ala Val Met Ala Leu Glu Arg Val
35 40 45
Pro Ala Asp Ile Arg Ala Ala Gly Gly Val Ala Arg Met Ala Asp Pro
50 55 60
Thr Ile Val Glu Glu Val Met Asn Ala Val Ser Ile Pro Val Met Ala
65 70 75 80
Lys Ala Arg Ile Gly His Ile Val Glu Ala Arg Val Leu Glu Ala Met
85 90 95
Gly Val Asp Tyr Ile Asp Glu Ser Glu Val Leu Thr Pro Ala Asp Glu
100 105 110
Glu Phe His Leu Asn Lys Asn Glu Tyr Thr Val Pro Phe Val Cys Gly
115 120 125
Cys Arg Asp Leu Gly Glu Ala Thr Arg Arg Ile Ala Glu Gly Ala Ser
130 135 140
Met Leu Arg Thr Lys Gly Glu Pro Gly Thr Gly Asn Ile Val Glu Ala
145 150 155 160
Val Arg His Met Arg Lys Val Asn Ala Gln Val Arg Lys Val Val Ala
165 170 175
Met Ser Glu Asp Glu Leu Met Thr Glu Ala Lys Asn Leu Gly Ala Pro
180 185 190
Tyr Glu Leu Leu Leu Gln Ile Lys Lys Asp Gly Lys Leu Pro Val Val
195 200 205
Asn Phe Ala Ala Gly Gly Val Ala Thr Pro Ala Asp Ala Ala Leu Met
210 215 220
Met Gln Leu Gly Ala Asp Gly Val Phe Val Gly Ser Gly Ile Phe Lys
225 230 235 240
Ser Asp Asn Pro Ala Lys Phe Ala Lys Ala Ile Val Glu Ala Thr Thr
245 250 255
His Phe Thr Asp Tyr Lys Leu Ile Ala Glu Leu Ser Lys Glu Leu Gly
260 265 270
Thr Ala Met Lys Gly Ile Glu Ile Ser Asn Leu Leu Pro Glu Gln Arg
275 280 285
Met Gln Glu Arg Gly Trp Arg Ser Ile Glu Gly Arg Met Lys Phe Ser
290 295 300
Ile Ala Ala Ala Val Val Ala Phe Ala Ala Ser Val Ala Ala Leu Pro
305 310 315 320
Pro Ala His Asp Ser Gln Phe Ala Gly Asn Gly Val Gly Asn Lys Gly
325 330 335
Asn Ser Asn Val Lys Phe Pro Val Pro Glu Asn Val Thr Val Lys Gln
340 345 350
Ala Ser Asp Lys Cys Gly Asp Gln Ala Gln Leu Ser Cys Cys Asn Lys
355 360 365
Ala Thr Tyr Ala Gly Asp Thr Thr Thr Val Asp Glu Gly Leu Leu Ser
370 375 380
Gly Ala Leu Ser Gly Leu Ile Gly Ala Gly Ser Gly Ala Glu Gly Leu
385 390 395 400
Gly Leu Phe Asp Gln Cys Ser Lys Leu Asp Val Ala Val Leu Ile Gly
405 410 415
Ile Gln Asp Leu Val Asn Gln Lys Cys Lys Gln Asn Ile Ala Cys Cys
420 425 430
Gln Asn Ser Pro Ser Ser Ala Asp Gly Asn Leu Ile Gly Val Gly Leu
435 440 445
Pro Cys Val Ala Leu Gly Ser Ile Leu Gly Ser His His His His His
450 455 460
His
465
<210>23
<211>1407
<212>DNA
<213>basf-yaad-Xa-BASF1-his
<220>
<221>CDS
<222>(1)..(1407)
<223>
<400>23
atg gct caa aca ggt act gaa cgt gta aaa cgc gga atg gca gaa atg 48
Met Ala Gln Thr Gly Thr Glu Arg Val Lys Arg Gly Met Ala Glu Met
1 5 10 15
caa aaa ggc ggc gtc atc atg gac gtc atc aat gcg gaa caa gcg aaa 96
Gln Lys Gly Gly Val Ile Met Asp Val Ile Asn Ala Glu Gln Ala Lys
20 25 30
atc gct gaa gaa gct gga gct gtc gct gta atg gcg cta gaa cgt gtg 144
Ile Ala Glu Glu Ala Gly Ala Val Ala Val Met Ala Leu Glu Arg Val
35 40 45
cca gca gat att cgc gcg gct gga gga gtt gcc cgt atg gct gac cct 192
Pro Ala AspIle Arg Ala Ala Gly Gly Val Ala Arg Met Ala Asp Pro
50 55 60
aca atc gtg gaa gaa gta atg aat gca gta tct atc ccg gta atg gca 240
Thr Ile Val Glu Glu Val Met Asn Ala Val Ser Ile Pro Val Met Ala
65 70 75 80
aaa gcg cgt atc gga cat att gtt gaa gcg cgt gtg ctt gaa gct atg 288
Lys Ala Arg Ile Gly His Ile Val Glu Ala Arg Val Leu Glu Ala Met
85 90 95
ggt gtt gac tat att gat gaa agt gaa gtt ctg acg ccg gct gac gaa 336
Gly Val Asp Tyr Ile Asp Glu Ser Glu Val Leu Thr Pro Ala Asp Glu
100 105 110
gaa ttt cat tta aat aaa aat gaa tac aca gtt cct ttt gtc tgt ggc 384
Glu Phe His Leu Asn Lys Asn Glu Tyr Thr Val Pro Phe Val Cys Gly
115 120 125
tgc cgt gat ctt ggt gaa gca aca cgc cgt att gcg gaa ggt gct tct 432
Cys Arg Asp Leu Gly Glu Ala Thr Arg Arg Ile Ala Glu Gly Ala Ser
130 135 140
atg ctt cgc aca aaa ggt gag cct gga aca ggt aat att gtt gag gct 480
Met Leu Arg Thr Lys Gly Glu Pro Gly Thr Gly Asn Ile Val Glu Ala
145 150 155 160
gtt cgc cat atg cgt aaa gtt aac gct caa gtg cgc aaa gta gtt gcg 528
Val Arg His Met Arg Lys Val Asn Ala Gln Val Arg Lys Val Val Ala
165 170 175
atg agt gag gat gag cta atg aca gaa gcg aaa aac cta ggt gct cct 576
Met Ser Glu Asp Glu Leu Met Thr Glu Ala Lys Asn Leu Gly Ala Pro
180 185 190
tac gag ctt ctt ctt caa att aaa aaa gac ggc aag ctt cct gtc gtt 624
Tyr Glu Leu Leu Leu Gln Ile Lys Lys Asp Gly Lys Leu Pro Val Val
195 200 205
aac ttt gcc gct ggc ggc gta gca act cca gct gat gct gct ctc atg 672
Asn Phe Ala Ala Gly Gly Val Ala Thr Pro Ala Asp Ala Ala Leu Met
210 215 220
atg cag ctt ggt gct gac gga gta ttt gtt ggt tct ggt att ttt aaa 720
Met Gln Leu Gly Ala Asp Gly Val Phe Val Gly Ser Gly Ile Phe Lys
225 230 235 240
tca gac aac cct gct aaa ttt gcg aaa gca att gtg gaa gca aca act 768
Ser Asp Asn Pro Ala Lys Phe Ala Lys Ala Ile Val Glu Ala Thr Thr
245 250 255
cac ttt act gat tac aaa tta atc gct gag ttg tca aaa gag ctt ggt 816
His Phe Thr Asp Tyr Lys Leu Ile Ala Glu Leu Ser Lys Glu Leu Gly
260 265 270
act gca atg aaa ggg att gaa atc tca aac tta ctt cca gaa cag cgt 864
Thr Ala Met Lys Gly Ile Glu Ile Ser Asn Leu Leu Pro Glu Gln Arg
275 280 285
atg caa gaa cgc ggc tgg aga tct att gaa ggc cgc atg aag ttc tcc 912
Met Gln Glu Arg Gly Trp Arg Ser Ile Glu Gly Arg Met Lys Phe Ser
290 295 300
gtc tcc gcc gcc gtc ctc gcc ttc gcc gcc tcc gtc gcc gcc ctc cct 960
Val Ser Ala Ala Val Leu Ala Phe Ala Ala Ser Val Ala Ala Leu Pro
305 310 315 320
cag cac gac tcc gcc gcc ggc aac ggc aac ggc gtc ggc aac aag ttc 1008
Gln His Asp Ser Ala Ala Gly Asn Gly Asn Gly Val Gly Asn Lys Phe
325 330 335
cct gtc cct gac gac gtc acc gtc aag cag gcc acc gac aag tgc ggc 1056
Pro Val Pro Asp Asp Val Thr Val Lys Gln Ala Thr Asp Lys Cys Gly
340 345 350
gac cag gcc cag ctc tcc tgc tgc aac aag gcc acc tac gcc ggc gac 1104
Asp Gln Ala Gln Leu Ser Cys Cys Asn Lys Ala Thr Tyr Ala Gly Asp
355 360 365
gtc ctc acc gac atc gac gag ggc atc ctc gcc ggc ctc ctc aag aac 1152
Val Leu Thr Asp Ile Asp Glu Gly Ile Leu Ala Gly Leu Leu Lys Asn
370 375 380
ctc atc ggc ggc ggc tcc ggc tcc gag ggc ctc ggc ctc ttc gac cag 1200
Leu Ile Gly Gly Gly Ser Gly Ser Glu Gly Leu Gly Leu Phe Asp Gln
385 390 395 400
tgc gtc aag ctc gac ctc cag atc tcc gtc atc ggc atc cct atc cag 1248
Cys Val Lys Leu Asp Leu Gln Ile Ser Val Ile Gly Ile Pro Ile Gln
405 410 415
gac ctc ctc aac cag gtc aac aag cag tgc aag cag aac atc gcc tgc 1296
Asp Leu Leu Asn Gln Val Asn Lys Gln Cys Lys Gln Asn Ile Ala Cys
420 425 430
tgc cag aac tcc cct tcc gac gcc acc ggc tcc ctc gtc aac ctc ggc 1344
Cys Gln Asn Ser Pro Ser Asp Ala Thr Gly Ser Leu Val Asn Leu Gly
435 440 445
ctc ggc aac cct tgc atc cct gtc tcc ctc ctc cat atg gga tct cat 1392
Leu Gly Asn Pro Cys Ile Pro Val Ser Leu Leu His Met Gly Ser His
450 455 460
cac cat cac cat cac 1407
His His His His His
465
<210>24
<211>469
<212>PRT
<213>basf-yaad-Xa-BASF1-his
<400>24
Met Ala Gln Thr Gly Thr Glu Arg Val Lys Arg Gly Met Ala Glu Met
1 5 10 15
Gln Lys Gly Gly Val Ile Met Asp Val Ile Asn Ala Glu Gln Ala Lys
20 25 30
Ile Ala Glu Glu Ala Gly Ala Val Ala Val Met Ala Leu Glu Arg Val
35 40 45
Pro Ala Asp Ile Arg Ala Ala Gly Gly Val Ala Arg Met Ala Asp Pro
50 55 60
Thr Ile Val Glu Glu Val Met Asn Ala Val Ser Ile Pro Val Met Ala
65 70 75 80
Lys Ala Arg Ile Gly His Ile Val Glu Ala Arg Val Leu Glu Ala Met
85 90 95
Gly Val Asp Tyr Ile Asp Glu Ser Glu Val Leu Thr Pro Ala Asp Glu
100 105 110
Glu Phe His Leu Asn Lys Asn Glu Tyr Thr Val Pro Phe Val Cys Gly
115 120 125
Cys Arg Asp Leu Gly Glu Ala Thr Arg Arg Ile Ala Glu Gly Ala Ser
130 135 140
Met Leu Arg Thr Lys Gly Glu Pro Gly Thr Gly Asn Ile Val Glu Ala
145 150 155 160
Val Arg His Met Arg Lys Val Asn Ala Gln Val Arg Lys Val Val Ala
165 170 175
Met Ser Glu Asp Glu Leu Met Thr Glu Ala Lys Asn Leu Gly Ala Pro
180 185 190
Tyr Glu Leu Leu Leu Gln Ile Lys Lys Asp Gly Lys Leu Pro Val Val
195 200 205
Asn Phe Ala Ala Gly Gly Val Ala Thr Pro Ala Asp Ala Ala Leu Met
210 215 220
Met Gln Leu Gly Ala Asp Gly Val Phe Val Gly Ser Gly Ile Phe Lys
225 230 235 240
Ser Asp Asn Pro Ala Lys Phe Ala Lys Ala Ile Val Glu Ala Thr Thr
245 250 255
His Phe Thr Asp Tyr Lys Leu Ile Ala Glu Leu Ser Lys Glu Leu Gly
260 265 270
Thr Ala Met Lys Gly Ile Glu Ile Ser Asn Leu Leu Pro Glu Gln Arg
275 280 285
Met Gln Glu Arg Gly Trp Arg Ser Ile Glu Gly Arg Met Lys Phe Ser
290 295 300
Val Ser Ala Ala Val Leu Ala Phe Ala Ala Ser Val Ala Ala Leu Pro
305 310 315 320
Gln His Asp Ser Ala Ala Gly Asn Gly Asn Gly Val Gly Asn Lys Phe
325 330 335
Pro Val Pro Asp Asp Val Thr Val Lys Gln Ala Thr Asp Lys Cys Gly
340 345 350
Asp Gln Ala Gln Leu Ser Cys Cys Asn Lys Ala Thr Tyr Ala Gly Asp
355 360 365
Val Leu Thr Asp Ile Asp Glu Gly Ile Leu Ala Gly Leu Leu Lys Asn
370 375 380
Leu Ile Gly Gly Gly Ser Gly Ser Glu Gly Leu Gly Leu Phe Asp Gln
385 390 395 400
Cys Val Lys Leu Asp Leu Gln Ile Ser Val Ile Gly Ile Pro Ile Gln
405 410 415
Asp Leu Leu Asn Gln Val Asn Lys Gln Cys Lys Gln Asn Ile Ala Cys
420 425 430
Cys Gln Asn Ser Pro Ser Asp Ala Thr Gly Ser Leu Val Asn Leu Gly
435 440 445
Leu Gly Asn Pro Cys Ile Pro Val Ser Leu Leu His Met Gly Ser His
450 455 460
His His His His His
465
Claims (21)
1.至少一种疏水蛋白在改进组合物相分离中的用途,所述组合物包含至少两种不同密度的液相,且包含选自以下的至少一种液相:燃料、原油和水溶性聚合物的溶液,其中所述燃料选自汽油、柴油机燃料或汽轮机燃料。
2.权利要求1的用途,其中所述至少一种疏水蛋白作为破乳剂。
3.权利要求1或2的用途,其中所述至少一种疏水蛋白是疏水蛋白融合蛋白质。
4.权利要求3的用途,其中所述疏水蛋白融合蛋白质选自SEQ ID No:20、SEQ ID No:22及SEQ ID No:24中的至少一个。
5.权利要求1或2的用途,其中包含至少两种不同密度的液相的组合物选自:
-包含原油和水的组合物,
-包含燃料和水的组合物,其中所述燃料选自汽油、柴油机燃料或汽轮机燃料。
6.权利要求1或2的用途,其中所述至少一种疏水蛋白基于总组合物的使用量为0.0001ppm至1000ppm。
7.权利要求6的用途,其中组合物是原油-水组合物,所述至少一种疏水蛋白基于总组合物的使用量为1ppm至800ppm。
8.权利要求6的用途,其中组合物是燃料-水组合物,所述至少一种疏水蛋白基于总组合物的使用量为0.001ppm至10ppm。
9.权利要求1或2的用途,其中除了所述的至少一种疏水蛋白外,还使用至少一种能改进相分离的其他化合物。
10.分离包含至少两种不同密度的液相的组合物中至少两种不同密度的液相的方法,包括向所述组合物中添加至少一种疏水蛋白,其中所述组合物包含选自以下的至少一种液相:燃料、原油和水溶性聚合物的溶液,其中所述燃料选自汽油、柴油机燃料或汽轮机燃料。
11.权利要求10的方法,其中所述至少一种疏水蛋白是疏水蛋白融合蛋白质。
12.权利要求11的方法,其中所述疏水蛋白融合蛋白质选自SEQ IDNo:20、SEQ ID N0:22及SEQ ID No:24中的至少一个。
13.权利要求10至12任一项的方法,其中包含至少两种不同密度的液相的组合物选自:
-包含原油和水的组合物,
-包含燃料和水的组合物,其中所述燃料选自汽油、柴油机燃料或汽轮机燃料。
14.权利要求10至12任一项的方法,其中所述至少一种疏水蛋白基于总组合物的使用量为0.0001ppm至1000ppm。
15.权利要求14的方法,其中组合物是原油-水组合物,所述至少一种疏水蛋白基于总组合物的使用量为1ppm至800ppm。
16.权利要求14的方法,其中组合物是燃料-水组合物,所述至少一种疏水蛋白基于总组合物的使用量为0.001ppm至10ppm。
17.根权利要求10至12任一项的方法,其中所述方法包括在添加所述至少一种疏水蛋白之前或之后提高包含至少两种不同密度的液相组合物的温度。
18.一种制剂,包括至少一种组合物和至少一种疏水蛋白,所述组合物选自燃料、原油和水溶性聚合物的溶液,其中存在于制剂中的所述疏水蛋白基于总制剂的量为0.0001ppm至1000ppm,其中所述燃料选自汽油、柴油机燃料或汽轮机燃料。
19.权利要求18的制剂,其中所述制剂包括至少一种燃料,且疏水蛋白基于总制剂的量为0.001ppm至0.5ppm。
20.权利要求18或19的制剂,其中所述至少一种蛋白质是疏水蛋白融合蛋白质。
21.权利要求20的制剂,其中所述疏水蛋白融合蛋白选自SEQ ID No:20、SEQ ID N0:22及SEQ ID No:24中的至少一个。
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EP05007208.1 | 2005-04-01 | ||
EP05007208 | 2005-04-01 | ||
EP05016962 | 2005-08-04 | ||
EP05016962.2 | 2005-08-04 | ||
PCT/EP2006/061132 WO2006103251A1 (de) | 2005-04-01 | 2006-03-29 | Verwendung von proteinen als demulgatoren |
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CN101151081B true CN101151081B (zh) | 2012-02-29 |
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US (1) | US20100170142A1 (zh) |
EP (1) | EP1868698A1 (zh) |
KR (1) | KR20070118157A (zh) |
CN (1) | CN101151081B (zh) |
BR (1) | BRPI0609776A2 (zh) |
CA (1) | CA2599985C (zh) |
MX (1) | MX2007011125A (zh) |
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CA2596661C (en) | 2005-02-07 | 2013-12-10 | Basf Aktiengesellschaft | Novel hydrophobin fusion products, production and use thereof |
US8859106B2 (en) * | 2005-03-31 | 2014-10-14 | Basf Se | Use of polypeptides in the form of adhesive agents |
EP1868700A2 (de) | 2005-04-01 | 2007-12-26 | Basf Aktiengesellschaft | Verwendung von hydrophobin als phasen-stabilisator |
DK1869138T3 (da) | 2005-04-01 | 2010-03-01 | Basf Se | Borevæske indeholdende hydrophobin |
DE102005027139A1 (de) | 2005-06-10 | 2006-12-28 | Basf Ag | Neue Cystein-verarmte Hydrophobinfusionsproteine, deren Herstellung und Verwendung |
DE102005033002A1 (de) * | 2005-07-14 | 2007-01-18 | Basf Ag | Wässrige Monomeremulsionen enthaltend Hydrophobin |
DE102005048720A1 (de) * | 2005-10-12 | 2007-04-19 | Basf Ag | Verwendung von Proteinen als Antischaum-Komponente in Kraftstoffen |
ES2374320T3 (es) | 2006-08-15 | 2012-02-15 | Basf Se | Procedimiento para la producción de preparaciones de hidrofobina secas de flujo libre. |
US8173716B2 (en) | 2007-03-06 | 2012-05-08 | Basf Se | Open-cell foam modified with hydrophobines |
CN101679063A (zh) * | 2007-05-24 | 2010-03-24 | 巴斯夫欧洲公司 | 疏水蛋白在固体结晶中作为添加剂的用途 |
WO2009037061A2 (de) * | 2007-09-13 | 2009-03-26 | Basf Se | Verwendung von hydrophobin-polypeptiden als penetrationsverstärker |
EP2042155A1 (de) | 2007-09-28 | 2009-04-01 | Basf Se | Verfahren zum Entfernen von wasserunlöslichen Substanzen von Substratoberflächen |
WO2009047210A1 (de) | 2007-10-08 | 2009-04-16 | Basf Se | Verwendung von hyperverzweigten polyestern und/oder polyesteramiden zum spalten von öl-wasser-emulsionen |
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- 2006-03-29 CN CN2006800101415A patent/CN101151081B/zh not_active Expired - Fee Related
- 2006-03-29 WO PCT/EP2006/061132 patent/WO2006103251A1/de active Application Filing
- 2006-03-29 BR BRPI0609776-6A patent/BRPI0609776A2/pt not_active IP Right Cessation
- 2006-03-29 MX MX2007011125A patent/MX2007011125A/es unknown
- 2006-03-29 KR KR1020077025100A patent/KR20070118157A/ko not_active Application Discontinuation
- 2006-03-29 US US11/886,610 patent/US20100170142A1/en not_active Abandoned
- 2006-03-29 CA CA2599985A patent/CA2599985C/en not_active Expired - Fee Related
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2007
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Also Published As
Publication number | Publication date |
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US20100170142A1 (en) | 2010-07-08 |
EP1868698A1 (de) | 2007-12-26 |
CN101151081A (zh) | 2008-03-26 |
KR20070118157A (ko) | 2007-12-13 |
WO2006103251A1 (de) | 2006-10-05 |
BRPI0609776A2 (pt) | 2011-10-18 |
NO20074580L (no) | 2007-10-29 |
CA2599985C (en) | 2012-11-13 |
CA2599985A1 (en) | 2006-10-05 |
MX2007011125A (es) | 2007-10-23 |
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