CN101087887A - 发酵产品方法 - Google Patents
发酵产品方法 Download PDFInfo
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- CN101087887A CN101087887A CNA2005800442665A CN200580044266A CN101087887A CN 101087887 A CN101087887 A CN 101087887A CN A2005800442665 A CNA2005800442665 A CN A2005800442665A CN 200580044266 A CN200580044266 A CN 200580044266A CN 101087887 A CN101087887 A CN 101087887A
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Abstract
本发明涉及用于从粒状淀粉产生乙醇产品的方法。
Description
发明领域
本发明涉及用于从粒状淀粉产生发酵产品的方法。使用酶的新组合促进了高干燥固体糖化醪(high dry solid mash)的加工。
发明背景
用于将粒状淀粉转化成发酵产品,例如乙醇产品的方法,在WO03/066826、WO 04/080923和WO 04/081193中公开。为了使这种方法有利可图,存在对于能够加工高干燥固体糖化醪的新方法的需求。本发明的目的是提供这种改进的方法,其用于将粒状淀粉转化成发酵产品。
发明概述
本发明人令人惊讶地发现,在粒状淀粉的液化和糖化中,使用包含糖结合模块(CBM)的酸性α-淀粉酶促进高干燥固体糖化醪的加工。
本发明人还令人惊讶地发现,在粒状淀粉的液化和糖化中,使用包含糖结合模块(CBM)的酸性α-淀粉酶与降粘酶(viscosity reducing enzyme),例如木聚糖酶和β-葡聚糖酶的组合,促进高干燥固体糖化醪的加工,即使当粗磨谷粉(grit)包含具有高木聚糖和β-葡聚糖含量的干磨的(dry milled)大麦、黑麦或小麦和其他谷物类型时。通过包含CBM的酸性α-淀粉酶的优良的原淀粉降解能力的效果和/或降粘酶的作用,加工较高干燥固体糖化醪,能够获得较高的乙醇收率以及由此获得较高的生产力(productivity)和处理量(throughput)。
在本发明的方法中,应用降粘酶例如β-葡聚糖酶和木聚糖酶降解葡聚糖和木聚糖,由此减少糖化醪的粘度。粘度减少导致液化糖化醪的流率(flow rate)增加,由此增加生产工厂的生产能力。此外,本发明提供简化的方法,其中能够将单独的降粘步骤省略。
对先前水解非淀粉多糖如***糖基木聚糖和β-葡聚糖的蒸馏加工的效果,是总体提高的生产能力,以及更好的热传递和相转移。
对先前水解非淀粉多糖以及更完全水解淀粉多糖的副产品如蒸馏器的干酒糟(distiller’s dry grain)的效果,是整体改进的进料转化,以及更好的营养物消化吸收率(digestivity),所述营养物如矿物质、蛋白质、脂质和残余淀粉。
因此本发明提供用于从粒状淀粉产生乙醇产品的方法,该方法没有所述淀粉的预先糊化(prior gelatinization)。在第一个方面,本发明提供包含如下步骤的方法,a)提供包含水和粒状淀粉的浆液,b)在下列物质存在下保持所述浆液:i)包含糖结合模块的酸性α-淀粉酶,和ii)发酵生物,以产生发酵产品和,c)任选地回收发酵产品。所述发酵生物优选为酵母,并且所述发酵产品优选乙醇。
在第二个方面,本发明提供组合物,其包含i)包含CBM的酸性α-淀粉酶和,ii)木聚糖酶,和/或iii)β-葡聚糖酶,和/或iv)葡糖淀粉酶。
发明详述
通过本发明的方法,能够将粒状淀粉水解成麦芽糖、葡萄糖或特制糖浆(specialty syrup),其用于作为甜味剂或作为其它糖类例如果糖的前体。还可以将麦芽糖和/或葡萄糖发酵成乙醇产品或其它发酵产品,例如柠檬酸、谷氨酸单钠(monosodium glutamate)、葡萄糖酸、葡萄糖酸钠、葡萄糖酸钙、葡萄糖酸钾、葡糖酸-δ-内酯或异抗坏血酸钠(sodium erythorbate)、衣康酸(itaconicacid)、乳酸、葡萄糖酸;酮;氨基酸、谷氨酸(谷氨酸单钠)、青霉素、四环素;酶;维生素,例如核黄素(riboflavin)、B12、β-胡萝卜素或激素。
术语“乙醇产品”的意思是包含乙醇的产品,例如燃料乙醇、饮用和工业乙醇。然而,所述乙醇产品还可以是啤酒,该啤酒可以是任何类型的啤酒。优选的啤酒类型包含爱儿啤酒(ale)、烈性黑啤酒(stout)、钵尔透黑啤酒(porter)、陈贮啤酒(lager)、苦味酒(bitter)、麦芽酒(malt liquor)、happoushu、高醇啤酒(high-alcohol beer)、低醇啤酒(low-alcohol beer)、低热量啤酒(low-calorie beer)或清淡啤酒(light beer)。
术语“粒状淀粉”的意思是未加工的生的淀粉,即以其天然形式存在于谷类(cereal)、块茎或谷粒(grain)中的淀粉。淀粉在植物细胞中形成为不溶于水的微小颗粒。当置于冷水中时,淀粉颗粒可以吸收少量的液体并且膨胀。在高达50℃-75℃的温度,所述膨胀可以是可逆的。然而,在更高的温度开始不可逆的膨胀,其称为糊化。
术语“起始糊化温度(initial gelatinization temperature)”的意思是淀粉糊化开始的最低温度。在水中加热的淀粉在50℃和75℃之间开始糊化;糊化的精确温度取决于具体的淀粉,并且能够容易地由熟练技术人员测定。因此,所述起始糊化温度可根据植物物种,根据植物物种的具体种类以及随生长条件而变化。在本发明的上下文中,给定淀粉的起始糊化温度是所述淀粉颗粒的双折射(birefringence)失去5%的温度,其使用由Gorinstein.S.和Lii.C.,Starch/Strke,Vol.44(12)pp.461-466(1992)所述的方法。
多肽“同源性”的意思是两种氨基酸序列之间的同一性程度。同源性可以由本领域已知的计算机程序合适地测定,例如,GCG程序包中提供的GAP(Program Manual for the Wisconsin Package,Version 8,August 1994,GeneticsComputer Group,575 Science Drive,Madison,Wisconsin,USA 53711)(Needleman,S.B.and Wunsch,C.D.,(1970),Journal of Molecular Biology,48,443-453)。使用下列用于多肽序列比较的设置:GAP产生罚分(creation penalty)3.0和GAP延伸罚分0.1。
术语“酸性α-淀粉酶”的意思是以有效量加入的α-淀粉酶活性(E.C.3.2.1.1),其在pH3.0-7.0的范围内,优选3.5-6.0,或更优选4.0-5.0具有活性。
酶
包含CBM的酸性α-淀粉酶:包含CBM的酸性α-淀粉酶是在EC 3.2.1.1之内的多肽,其具有酸性α-淀粉酶活性,并且包含糖结合模块,优选所述CBM是淀粉结合域(SBD),并且优选家族CBM20的CBM。用于本发明的包含CBM的酸性α-淀粉酶可以是杂合体酶(hydrid enzyme),或所述多肽可以是野生型酶,其已经包含具有α-淀粉酶活性的催化模块和糖结合模块。用于本发明的方法包含CBM的酸性α-淀粉酶还可以是这种野生型酶的变体。可以通过融合编码第一氨基酸序列的第一DNA序列和编码第二氨基酸的第二DNA序列来产生所述杂合体,或可将所述杂合体作为基于合适的CBM、接头和催化域的氨基酸序列的知识完全合成的基因产生。本文使用术语“杂合体酶”来表征多肽,所述多肽是包含CBM的酸性α-淀粉酶,该多肽包含第一氨基酸序列和第二氨基酸序列,所述第一氨基酸序列包含具有α-淀粉酶活性的催化模块,而所述第二氨基酸序列包含至少一个糖结合模块,其中所述第一和第二源自不同的来源。将术语“来源”理解为,但不限于,例如亲本多肽,例如酶,例如淀粉酶或葡糖淀粉酶,或具有其它催化活性、包含合适的催化模块和/或合适的CBM和/或合适的接头的酶。所述CBM的亲本多肽和酸性α-淀粉酶活性可以源自相同的菌株,和/或源自相同菌种或其可以源自相同菌种的不同菌株或源自不同菌种的菌株。真菌的和细菌的亲本多肽二者均为优选的,以及真菌的和细菌的野生型和野生型的变体。
本发明优选的是包含CBM的任何酸性α-淀粉酶,包括但不限于源自真菌的杂合体酶和野生型变体,其公开于PCT/US2004/020499[NZ10490]中和与本申请在同一日提交的丹麦专利申请[NZ10729]中,以及源自细菌的杂合体、野生型或野生型变体,其公开于与本申请在同一日提交的丹麦专利申请[NZ10753]中。更优选的是具有酸性α-淀粉酶活性并且包含CBM的酶,该酶具有如SEQ ID NO:1(JA001)公开的氨基酸序列,所述序列包含与黑曲霉酸性α-淀粉酶相同的催化域和与川地曲霉(A.kawachii)α-淀粉酶CBM相同的CBM,如SEQ ID NO:2(JA126)公开的序列或如SEQ ID NO:3(JA129)公开的序列或包含CBM的酸性α-淀粉酶,该酸性α-淀粉酶具有的氨基酸序列与任何前述氨基酸序列具有至少50%、60%、70%、80%、85%、90%或甚至至少95%同一性。
含有CBM的杂合体酶,以及其制备和纯化的详细描述,是本领域已知的[参见,例如WO 90/00609、WO 94/24158和WO 95/16782,以及Greenwoodet al.Biotechnology and Bioengineering 44(1994)pp.1295-1305]。
不包含CBM的α-淀粉酶:在本发明的方法的过程中还可以存在不包含CBM的α-淀粉酶,例如真菌酸性α-淀粉酶,如源自黑曲霉(Aspergillus niger)的酸性真菌α-淀粉酶和/或如细菌α-淀粉酶,例如源自芽孢杆菌属的菌种(Bacillussp.)的α-淀粉酶。
不包含CBM的α-淀粉酶可以作为来自DSM(Gist Brochades)的分枝菌酶(Mycolase)、BANTM、TERMAMYLTM SC、FUNGAMYLTM、LIQUOZYMETMX和SANTM SUPER、SANTM EXTRA L(Novozymes A/S)和澄解酶(Clarase)L-40,000、DEX-LOTM、Spezyme FRED、SPEZYMETM AA和SPEZYMETMDELTA AA(Genencor Int.)。
β-葡聚糖酶(E.C.3.2.1.4):可以在有效量的合适的β-葡聚糖酶存在下进行本发明的方法。所述β-葡聚糖酶可以是微生物来源的,例如可以源自细菌(例如芽孢杆菌属)的菌株,或可以源自丝状真菌(例如,曲霉属、木霉属(Trichoderma)、腐质霉属(Humicola)、镰孢属(Fusarium))。优选的是源自木霉属的菌种的β-葡聚糖酶,例如具有SEQ ID NO:8(WO200014206)中所示序列的β-葡聚糖酶,优选T.reesei例如具有SEQ ID NO:6中所示序列的β-葡聚糖酶,或绿色木霉(T.viride)例如具有SEQ ID NO:7中所示序列的β-葡聚糖酶。
用于本发明的方法的β-葡聚糖酶可以是内切葡聚糖酶,例如内-1,4-β-葡聚糖酶。商业上可得到的可使用的β-葡聚糖酶制剂包括CELLUCLAST、CELLUZYME、CEREFLO和ULTRAFLO(可由Novozymes A/S获得)、GC 880、LAMINEXTM和SPEZYMECP(可获得自Genencor Int.)和ROHAMENT7069 W(可由Rhm,Germany获得)。优选的是CEREFLO。
可以将β-葡聚糖酶以0.01-5000BGU/kg干固体的量,优选地以0.1-500BGU/kg干固体的量,并且最优选1-50BGU/kg干固体的量加入,并且在液化步骤(下游糖化醪)以1.0-5000BGU/kg干固体的量,并且最优选10-500BGU/kg干固体的量加入。
木聚糖酶(EC 3.2.1.8和其它):可以在有效量的合适的木聚糖酶存在下进行本发明的方法,所述木聚糖酶可以源自多种生物体,其包括真菌的和细菌的生物体,例如曲霉属、Disporotrichum属、青霉属(Penicilluum)、脉孢菌属(Neurospora)、镰孢属和木霉属。
合适的木聚糖酶的实例包括源自以下菌种的木聚糖酶:H.insolens(WO92/17573);塔宾曲霉(Aspergillus tubigensis)(WO 92/01793);黑曲霉(Shei et al.,1985,Biotech.和Bioeng.Vol.XXVII,pp.533-538,和Foumier et al.,1985,Bio-tech.Bioeng.Vol.XXVII,pp.539-546;WO 91/19782和EP 463 706);棘孢曲霉(Aspergillus aculeatus)(WO 94/21785)。
所述木聚糖酶还可以是1,3-β-D-木聚糖木聚糖水解酶(1,3-beta-D-xylanxylanohydrolase)(EC.3.2.1.32)。
优选地,木聚糖酶是家族10木聚糖酶,并且更加优选地所述木聚糖酶源自曲霉属的菌种。在具体的实施方案中,所述木聚糖酶是棘孢曲霉的木聚糖酶II,其公开于WO 94/21785,并且示于SEQ ID NO:4,或所述木聚糖酶是Trichoderma reesei的木聚糖酶,其具有SEQ ID NO:5(SWISSPROT Q9P973)中所示的序列。
预期的商业上可得到的包含木聚糖酶的组合物包括SHEARZYME200L、SHEARZYME500L、BIOFEED WHEAT和PULPZYMETM HC(来自Novozymes)和GC 880、SPEZYMECP(来自Genencor Int)。
可以将木聚糖酶以1.0-1000FXU/kg干固体的量加入,优选5-500FXU/kg干固体,优选5-100FXU/kg干固体,并且最优选10-100FXU/kg干固体。
葡糖淀粉酶:可以将葡糖淀粉酶(E.C.3.2.1.3)用在所述方法中。优选的是真菌来源的葡糖淀粉酶,例如曲霉属葡糖淀粉酶,具体为黑曲霉G1或G2葡糖淀粉酶(Boel et al.(1984),EMBO J.3(5),p.1097-1102)。同样优选的是其变体,例如WO92/00381和WO00/04136中公开的;泡盛曲霉(A.awamori)葡糖淀粉酶(WO84/02921)、米曲霉(A.oryzae)(Agric.Biol.Chem.(1991),55(4),p.941-949),或它们的变体或片段。优选的葡糖淀粉酶包括源自黑曲霉的葡糖淀粉酶,例如与WO00/04136和SEQ ID NO:13中所列氨基酸序列具有50%、55%、60%、65%、70%、75%、80%、85%或甚至90%同源性的葡糖淀粉酶。同样优选的是源自米曲霉的葡糖淀粉酶,例如与WO00/04136 SEQ ID NO:2所列氨基酸序列具有50%、55%、60%、65%、70%、75%、80%、85%或甚至90%同源性的葡糖淀粉酶。
其它葡糖淀粉酶包括踝节菌属(Talaromyces)葡糖淀粉酶,具体地源自Talaromyces emersonii(WO99/28448)、Talaromyces leycettanus(美国专利号Re.32,153)、Talaromyces duponti、嗜热踝节菌(Talaromyces thermophilus)(美国专利号4,587,215),梭菌属(Clostridium)葡糖淀粉酶,具体为嗜热解淀粉梭菌(C.thermoamylolyticum) (EP135,138)和热硫化氢梭菌(C.thermohydrosulfuricum)(WO86/01831)。
商业上可得到的包含葡糖淀粉酶的组合物包括AMG 200L;AMG300 L;SANTM SUPER、SAN EXTRA L和AMGTM E(来自Novozymes A/S);OPTIDEXTM 300(来自Genencor Int.);AMIGASETM和AMIGASETM PLUS(来自DSM);G-ZYMETM G900、G-ZYMETM和G990 ZR(来自Genencor Int.)。
肌醇六磷酸酶:可以用于本发明的方法中的额外的酶是肌醇六磷酸酶。所述肌醇六磷酸酶可以是能够从植酸(肌醇六磷酸(myo-inositolhexakisphosphate))或从它的任何盐(植酸盐)实现无机磷酸盐的释放的任何酶。肌醇六磷酸酶能够根据它们在初始水解步骤中的特异性,即根据哪个磷酸酯基团首先被水解来分类。用于本发明中的肌醇六磷酸酶可以具有任何特异性,例如,作为3-肌醇六磷酸酶(E.C.3.1.3.8)、6-肌醇六磷酸酶(E.C.3.1.3.26)或5-肌醇六磷酸酶(无E.C.编号)。
根据本发明优选的商业上可得到的肌醇六磷酸酶包括BIO-FEEDPHYTASETM、PHYTASE NOVOTM CT或L(NovozymesA/S),或NATUPHOSTMNG 5000(DSM)。
另一种酶可以是脱支酶,例如异淀粉酶(E.C.3.2.1.68)或支链淀粉酶(E.C.3.2.1.41)。异淀粉酶水解β-极限糊精和支链淀粉中的α-1,6-D-糖苷分支键(alpha-1,6-D-glucosidic branch linkage),并且能够凭借异淀粉酶不能攻击支链淀粉,和凭借对α-极限糊精的有限作用区别于支链淀粉酶。可以将脱支酶以本领域的技术人员熟知的有效量加入。
在第一个优选的实施方案中,本发明提供用于产生乙醇的方法,包含下列步骤:(a)提供包含水和粒状淀粉的浆液,(b)在下列物质存在下在30℃-35℃之间的温度温育所述浆液:i)包含CBM的酸性α-淀粉酶和ii)发酵生物,例如酵母,以产生发酵产品,和,(c)任选地回收所述发酵产品,例如乙醇。所述步骤(a)、(b)和(c)可以顺序进行;然而,所述方法可以包含未在本文描述中详细说明的额外的步骤,其可以在步骤(a)、(b)和(c)的任一项之前、之间或之后进行。优选地步骤(b)的温度是28℃-36℃之间,优选29℃-35℃,更优选30℃-34℃,例如大约32℃,并且将所述浆液保持与以下物质接触一段时间:i)包含CBM的酸性α-淀粉酶和ii)发酵生物,例如酵母,所述时间足以在步骤(b)的过程中使淀粉水解和释放的糖类发酵,优选25至190小时的时间,优选30-180小时,更优选40-170小时,甚至更优选50-160小时,还更优选60-150小时,甚至还更优选70-140小时,并且最优选80-130小时,例如85-110小时。在又一个优选的实施方案中,在步骤b)的过程中还存在木聚糖酶和/或β-葡聚糖酶。
在优选的实施方案中,在步骤b)之前将所述浆液在低于起始糊化温度0-30℃的温度,例如在低于起始糊化温度0-20℃,优选0-10,更优选5-10℃的温度温育。优选在步骤b)之前将所述浆液在低于起始糊化温度0-30℃的温度,例如在30℃-45℃、40℃-50℃,或45℃-55℃温育。
将包含CBM的酸性α-淀粉酶以有效量加入,该有效量是对于想要达到的目的来说足够的酸性α-淀粉酶(活性)的浓度,所述目的是将淀粉浆液中的粒状淀粉转化成糊精。优选所述包含CBM的酸性α-淀粉酶以10-10000AFAU/kg的DS的量,以500-2500AFAU/kg的DS的量,或更优选以100-1000AFAU/kg的DS的量,例如大约500AFAU/kg的DS的量存在。当以AAU单位测量时,所述酸性α-淀粉酶活性优选以5-500000AAU/kg的DS的量,以500-50000AAU/kg的DS的量,或更优选以100-10000AAU/kg的DS,例如500-1000AAU/kg的DS的量存在。
将所述葡糖淀粉酶以有效量加入,该有效量是对于想要达到的目的来说足够的葡糖淀粉酶的浓度,所述目的是降解由酸性α-淀粉酶处理淀粉浆液产生的糊精。优选所述葡糖淀粉酶活性以20-200AGU/kg的DS的量,优选100-1000AGU/kg的DS,或更优选以200-400AGU/kg的DS,例如250AGU/kgDS的量存在。当以AGI单位测量时,所述葡糖淀粉酶活性优选以10-100000AGI/kg的DS,50-50000AGI/kg的DS,优选100-10000AGI/kg的DS,或更优选以200-5000AGI/kg的DS的量存在。
优选将酸性α-淀粉酶活性和葡糖淀粉酶活性以0.3-5.0AFAU/AGU的比例加入所述浆液中。更优选酸性α-淀粉酶活性和葡糖淀粉酶活性之间的比例是至少0.35、至少0.40、至少0.50、至少0.60、至少0.7、至少0.8、至少0.9、至少1.0、至少1.1、至少1.2、至少1.3、至少1.4、至少1.5、至少1.6、至少1.7、至少1.8、至少1.85或甚至至少1.9AFAU/AGU。然而,酸性α-淀粉酶活性和葡糖淀粉酶活性之间的比例应该优选少于4.5、少于4.0、少于3.5、少于3.0、少于2.5或甚至少于2.25AFAU/AGU。以AUU/AGI表示的酸性α-淀粉酶和葡糖淀粉酶的活性优选以0.4-6.5AUU/AGI的比例存在。更优选地,酸性α-淀粉酶活性和葡糖淀粉酶活性之间的比例是至少0.45、至少0.50、至少0.60、至少0.7、至少0.8、至少0.9、至少1.0、至少1.1、至少1.2、至少1.3、至少1.4、至少1.5、至少1.6、至少1.7、至少1.8、至少1.9、至少2.0、至少2.1、至少2.2、至少2.3、至少2.4或甚至至少2.5AUU/AGI。然而,酸性α-淀粉酶活性和葡糖淀粉酶活性之间的比例优选少于6.0、少于5.5、少于4.5、少于4.0、少于3.5或甚至少于3.0AUU/AGI。
在本发明的第一个方面,木聚糖酶可优选以1-50000FXU/kg DS,优选5-5000FXU/kgDS,或更优选10-500FXU/kg DS的量存在,并且所述β-葡聚糖酶可以0.01-500000EGU/kg DS,优选0.1-10000EGU/kgDS,优选1-5000EGU/kg DS,更优选10-500EGU/kg DS,并最优选100-250EGU/kgDS的量存在。
所述酶活性可优选以本发明第二个方面所述的组合物的形式配制,并且优选地该组合物包含的前文所述酶的浓度在浓度上(in strength)等于在所述浆液中浓度的10倍、100倍、1000倍或甚至10000倍。
在优选的实施方案中,所述淀粉浆液包含水和5-60%DS(干固体)粒状淀粉,优选10-50%DS粒状淀粉,更优选15-40%DS,特别是大约20-25%DS粒状淀粉。在本发明的方法中待加工的粒状淀粉具体可以得自块茎(tuber)、根、茎、玉米芯(cob)、豆类、谷类或整谷粒(whole grain)。更具体地,所述粒状淀粉可以得自玉米、玉米芯、小麦、大麦、黑麦、买罗高粱(milo)、西米(sago)、木薯(cassava)、木薯淀粉(tapioca)、高粱(sorghum)、稻、豌豆(pea)、豆类(bean)、香蕉或马铃薯。优选的是蜡质或非蜡质两种类型的玉米和大麦。最优选的是谷类,特别是小麦、大麦和/或黑麦。所述待加工的粒状淀粉可优选源自磨碎的整谷粒。优选地将包含所述粒状淀粉的原料磨碎以打开结构并且用于进一步的加工。所述粒状淀粉优选是干磨的谷粒,例如小麦、大麦和/或黑麦。因为小麦、大麦和/或黑麦包含非常大量的β-葡聚糖和木聚糖,包含这些谷粒种类的干磨谷物(dry milled grist)能够在常规方法中导致高糖化醪粘度,所述常规方法包含未糊化的粒状淀粉的液化和/或糖化。因此源自干磨小麦、大麦和/或黑麦的粒状淀粉对于本发明的方法是特别优选的。
在经过本发明所述第一个方面的方法之后,将至少85%、86%、87%、88%、89%、90%、91%、92%、93%、94%、95%、96%、97%、98%或优选99%的所述粒状淀粉的干固体转化成乙醇。
所述发酵的浆液包含至少7%、至少8%、至少9%、至少10%例如至少11%、至少12%、至少13%、至少14%、至少15%例如至少16%的乙醇。
在发酵之后可以将乙醇任选地回收。所述乙醇回收可以通过任何常规方式,比如蒸馏来进行,并且可将其用作燃料乙醇和/或饮用乙醇和/或工业乙醇。
材料和方法
酸性α-淀粉酶活性
当根据本发明使用时,可以以AFAU(酸性真菌α-淀粉酶单位)测量任何酸性α-淀粉酶活性。可替换地,可以以AAU(酸性α-淀粉酶单位)测量酸性α-淀粉酶的活性。
酸性α-淀粉酶单位(AAU)
所述酸性α-淀粉酶活性能够以AAU(酸性α-淀粉酶单位)测量,其是绝对方法。一个酸性淀粉酶单位(AAU)是每小时将1g淀粉(100%的干固体)在标准化条件下转化成产物的酶量,所述产品在与已知浓度的碘溶液反应之后在620nm具有的透射(transmission)等于颜色参比(color reference)之一。
标准条件/反应条件:
底物:可溶淀粉。浓度约为20g DS/L.
缓冲液:柠檬酸盐,约0.13M,pH=4.2
碘溶液:40.176g碘化钾+0.088g碘/L
城市水 15°-20°dH(德国硬度(German degree hardness))
pH:4.2
温育温度:30℃
反应时间:11分钟
波长:620nm
酶浓度:0.13-0.19AAU/mL
酶工作范围:0.13-0.19AAU/mL
所述淀粉应该是Lintner淀粉,其是轻沸的(thin-boiling)淀粉,在实验室中用作比色指示剂。Lintner淀粉通过稀释盐酸处理的天然淀粉获得,因而其深持了与碘变为蓝色的能力。进一步的细节可见于EP0140410B2,通过引用将其公开包括在本文中。
酸性α-淀粉酶活性(AFAU)
可以以AFAU(酸性真菌α-淀粉酶单位)测量酸性α-淀粉酶活性,其相对于酶标准测定。将1FAU定义为在下述标准条件下每小时降解5.260mg淀粉干固体的酶量。
酸性α-淀粉酶,内-α-淀粉酶(1,4-α-D-葡聚糖-葡聚糖水解酶(1,4-alpha-D-glucan-glucanohydrolase),E.C.3.2.1.1)水解淀粉分子内部区域的α-1,4-糖苷键以形成具有不同链长的低聚糖和糊精。与碘形成的颜色强度与淀粉浓度成正比例。使用反向比色法(reverse colorimetry),测定在特定分析条件下淀粉浓度的降低作为淀粉酶活性。
λ=590nm
蓝色/紫色 t=23秒 脱色
标准条件/反应条件:
底物:可溶淀粉,约0.17g/L
缓冲液:柠檬酸盐,约0.03M
碘(I2):0.03g/L
CaCl2:1.85mM
pH:2.50±0.05
温育温度:40℃
反应时间:23秒
波长:590nm
酶浓度:0.025AFAU/mL
酶工作范围:0.01-0.04AFAU/mL
更详细描述这种分析方法的文件夹EB-SM-0259.02/01可以根据向Novozymes A/S,Denmark要求而获得,通过引用将该文件夹包括在本文中。
细菌α-淀粉酶活性(KNU)
可以使用马铃薯淀粉作为底物测定细菌α-淀粉酶活性。这种方法基于通过酶分解改性的马铃薯淀粉,并将淀粉/酶溶液的样品与碘溶液混合来跟踪该反应。最初,形成黑蓝色(blackish blue),但在分解淀粉的过程中蓝色变弱,并且逐渐转变成红棕色(reddish brown),其与有色玻璃标准(colored glassstandard)比较。
将一千Novo α-淀粉酶单位(KNU)定义为在标准条件(即,在37℃+/-0.05;0.0003M Ca2+;和pH5.6)下将5260mg淀粉干物质Merck Amylum solu-bile糊精化的酶量。
更详细描述这种分析方法的文件夹EB-SM-0009.02/01可以根据向Novozymes A/S,Denmark要求而获得,通过引用将该文件夹包括在本文中。
葡糖淀粉酶活性
可以以AGI单位或以淀粉葡萄糖苷酶单位(AGU)测量葡糖淀粉酶活性。
葡糖淀粉酶活性(AGI)
葡糖淀粉酶(等同于淀粉葡萄糖苷酶(amyloglucosidase))将淀粉转化为葡萄糖。此处通过用于活性测定的葡萄糖氧化酶方法测定葡萄糖的量。该方法在“Approved methods of the American Association of Cereal Chemists”.Vol.1-2AACC,from American Association of Cereal Chemists,(2000);ISBN:1-891127-12-8中的76-11节Starch-Glucoamylase Method with SubsequentMeasurement of Glucose with Glucose Oxidase中有所描述。
一个葡糖淀粉酶单位(AGI)是在所述方法的标准条件下每分钟将形成1微摩尔葡萄糖的酶量。
标准条件/反应条件:
底物:可溶淀粉,浓度约16g干固体/L.
缓冲液:醋酸盐,约0.04M,pH=4.3
pH:4.3
温育温度:60℃
反应时间:15分钟
终止反应:NaOH达到约0.2g/L(pH~9)的浓度
酶浓度:0.15-0.55AAU/mL.
所述淀粉应该是Lintner淀粉,其是轻沸的淀粉,在实验室中用作比色指示剂。Lintner淀粉通过稀释盐酸处理天然淀粉来获得,因而其保持了与碘变为蓝色的能力。
葡糖淀粉酶活性(AGU)
将Novo葡糖淀粉酶单位(AGU)定义为在标准条件下每分钟水解1微摩尔麦芽糖的酶量,所述标准条件是37℃,pH4.3,底物:麦芽糖23.2mM,缓冲液:醋酸盐0.1M,反应时间5分钟。
可以使用自动分析器***。将变旋酶(mutarotase)加入到葡萄糖脱氢酶试剂中,从而将存在的任何α-D-葡萄糖转变成β-D-葡萄糖。在上述反应中葡萄糖脱氢酶与β-D-葡萄糖特异地反应,形成NADH作为原始葡萄糖浓度的量度,所述NADH是使用光度计在340nm测定的。
AMG温育:
底物:麦芽糖23.2mM
缓冲液:醋酸盐0.1M
pH:4.30±0.05
温育温度:37℃±1
反应时间:5分钟
酶工作范围:0.5-4.0AGU/mL
显色反应:
GlucDH:430U/L
变旋酶:9U/L
NAD:0.21mM
缓冲液:磷酸盐0.12M;0.15M NaCl
pH:7.60±0.05
温育温度:37℃±1
反应时间:5分钟
波长:340nm
更详细描述这种分析方法的文件夹(EB-SM-0131.02/01)可以根据向Novozymes A/S,Denmark要求而获得,通过引用将该文件夹包括在本文中。
木聚糖水解(Xylanolytic)活性
木聚糖水解活性可以以FXU单位表示,用remazol-木聚糖(用RemazolBrilliant Blue R,Fluka染色的4-O-甲基-D-葡萄糖醛酸-D-木聚糖(4-O-methyl-D-glucurono-D-xylan))作为底物在pH6.0测定。
将木聚糖酶样品与remazol-木聚糖底物一起温育。将未降解的染色的底物背景通过乙醇沉淀。上清液中残余的蓝颜色(如通过分光光度法在585nm测定)与木聚糖酶活性成比例,然后相对于标准反应条件下的酶标准测定木聚糖酶单位,所述标准反应条件即在50.0℃,pH6.0,以及30分钟反应时间。
更详细描述这种分析方法的文件夹EB-SM-352.02/01可以根据向Novozymes A/S,Denmark要求而获得,通过引用将该文件夹包括在本文中。
纤维素水解(Cellulytic)活性
可以以内-葡聚糖酶单位(EGU)测量纤维素水解活性,其在pH6.0用羧甲基纤维素(CMC)作为底物测定。制备底物溶液,其在pH6.0的0.1M磷酸盐缓冲液中含有34.0g/l CMC(Hercules 7 LFD)。将所述待分析的酶样品溶于相同的缓冲液中。将5ml底物溶液和0.15ml酶溶液混合,并且转移到振动粘度计(vibration viscosimeter)(例如MIVI 3000,来自Sofraser,France)中,于40℃恒温30分钟。将一个EGU定义为在这些条件下将粘度减少至一半的酶量。应调节酶样品的量以在所述反应混合物中提供0.01-0.02EGU/ml。将主要标准物(arch standard)定义为880EGU/g。
更详细描述这种分析方法的文件夹EB-SM-0275.02/01可以根据向Novozymes A/S,Denmark要求而获得,通过引用将该文件夹包括在本文中。
酶制剂
使用下列酶制剂:
细菌α-淀粉酶;包含多肽的酶制剂,所述多肽具有源自嗜热脂肪芽孢杆菌(B.stearothermophilus)的α-淀粉酶活性(E.C.3.2.1.1),并且具有如WO99/19467中SEQ.NO:4公开的氨基酸序列。活性:120KNU/g(密度=1.20-1.25g/mL)。
包含酸性真菌α-淀粉酶和一些葡糖淀粉酶的组合物,所述酸性真菌α-淀粉酶包含具有SEQ ID NO:1中所示序列的CBM。活性:329AFAU/g,31AGU/g(密度=1.2g/mL)。
源自黑曲霉的葡糖淀粉酶组合物,其包含葡糖淀粉酶和一些酸性真菌α-淀粉酶。活性:363AGU/g,86AFAU/g(密度=1.2g/mL)。
源自遗传修饰的黑曲霉微生物(Spirizyme Fuel)的葡糖淀粉酶组合物,其包含葡糖淀粉酶和一些酸性真菌α-淀粉酶。活性:750AGU/g,30AFAU/g。
源自遗传修饰的黑曲霉微生物(Spirizyme Plus)的葡糖淀粉酶组合物,其包含葡糖淀粉酶和一些酸性真菌α-淀粉酶。活性:363AGU/g,86AFAU/g。
酶组合物(Novozym 50024),其包含木聚糖酶和纤维素酶活性,所述活性分别源自Trichoderma reesei和棘孢曲霉。活性:300FXU/g+350EGU/g(密度=1.2g/mL)。
酵母:来自De Danske Spritfabrikker A/S(Danish Distillers)的干的面包酵母(Dried baker’s yeast)。
实施例1
本实施例说明了使用包含CBM的酸性α-淀粉酶的本发明的方法。在室温的自来水中制备磨碎小麦的20%D.S.浆液。对每个处理,将2×250g浆液分配到500mL蓝盖瓶中。使用6N HCl将pH调节至4.5。根据表6配制酶活性,并且将所述瓶在55℃振荡水浴中温育一小时。将所述瓶冷却至32℃并添加0.25g干的面包酵母。将所述瓶置于32℃水浴72小时。记录重量损失数据。在50和72.5小时将所述瓶称重,并且测量CO2重量损失用于监测该发酵进程。所用的CO2损失量和乙醇重量之间的关系是:CO2损失(g)×1.045=EtOH(g)。
表1.小麦;50小时和72小时的重量损失(g)。葡糖淀粉酶(AGU)、包含CBM的酸性α-淀粉酶(AFAU) | ||||
AGU/kg DS | 0.3 | 0.3 | 0.3 | 0.3 |
AFAU/kg DS | 0 | 0.05 | 0.17 | 0.3 |
重量损失(g),50小时 | 10.98 | 12.98 | 14.37 | 15.18 |
重量损失(g),72.5小时 | 12.90 | 15.49 | 16.69 | 17.79 |
乙醇%w/w,50小时* | 4.80 | 5.73 | 6.37 | 6.76 |
乙醇%w/w,72小时* | 5.69 | 6.90 | 7.48 | 8.01 |
乙醇%w/w,100小时** | 6.26 | 7.57 | 7.82 | 8.25 |
*基于50和72小时的重量损失,CO2损失(g)×1.045=EtOH(g),**基于100小时的HPLC。
实施例2
将使用被称作不加压蒸煮(non-pressure cooking)(NPC)的传统预液化的常规乙醇方法与本发明的方法进行比较。用于产生饮用乙醇的传统不加压批式(batch)蒸煮方法在题为“Use of Novozymes enzymes in alcohol production”的Novozymes公开No.2001-10782-01中有所描述。
在室温(RT)自来水中制备磨碎大麦的20%D.S.浆液。使用HAAKEViscotester VT02型粘度计测量粘度。
常规乙醇方法的NPC预处理在6×1升的桶(tub)中伴随搅拌进行。添加细菌α-淀粉酶并且将所述桶置于65℃水浴。当糖化醪中的温度达到55℃时,增加加热以将该糖化醪加热至90℃历经60分钟。随后将温度调节至32℃,并且将3×250g糖化醪分配到带有气塞(air lock)的500mL蓝盖瓶中。向所有瓶中添加0.25g干面包酵母(对应于5百万-1千万活细胞/g糖化醪)。根据下列表格添加酶活性,并将每个瓶称重。将所述瓶置于32℃振荡水浴中。在72小时将所述瓶称重,并且测量CO2重量损失用于监测该发酵进程。所用的CO2损失量和乙醇重量之间的关系是:CO2损失(g)×1.045=EtOH(g)。
对于本发明的方法,在室温(RT)自来水中制备磨碎大麦的30%D.S.浆液。将每个装有250g浆液的500mL蓝盖发酵瓶装上气塞。使用4.0摩尔H2SO4将pH调节至5.0,并且使用HAAKE Viscotester VT02型粘度计测量粘度。将木聚糖酶、纤维素酶、葡糖淀粉酶和包含CBM的酸性α-淀粉酶根据表2配制。然后将温度调节至32℃,将所述瓶保持在磁力搅拌下,并且如上所述监测使用0.25g干的面包酵母的发酵(对应于在发酵开始时5百万-1千万活细胞/g糖化醪)。本发明的时间从接种开始计算。
表2.大麦,72小时和91小时的重量损失(g)。根据本表添加细菌α-淀粉酶(KNU),包含CBM的酸性α-淀粉酶(AFAU)和葡糖淀粉酶(AGU)活性。 | ||
传统不加压蒸煮 | 本发明的方法 | |
%DS | 20 | 30 |
发酵前粘度,cP | 2000 | 8000 |
FXU/kg DS | 0 | 300 |
EGU/kg DS | 0 | 350 |
KNU/kg DS | 36 | 0 |
AFAU/kg DS | 0 | 280 |
AGU/kg DS | 163 | 470 |
AFAU/AGU | 0 | 0.60 |
重量损失(g),72小时 | 12.2 | 15 |
重量损失(g),91小时 | 14.0 | 16.7 |
最终粘度cP | <30 | <30 |
乙醇%w/w,72小时 | 5.1 | 6.7 |
乙醇%w/w,91小时 | 6.2 | 7.5 |
实施例3
本实施例说明了使用多种原料的本发明的方法。在室温自来水中制备磨碎谷类的30%D.S.浆液。对于每个处理,将2×250g分配到500mL蓝盖瓶中。然后将温度调节至32℃,并且如上所述进行和监测使用0.25g干的面包酵母的发酵(对应于在发酵开始时5百万-1千万活细胞/g糖化醪)。时间从接种计算。
使用4.0摩尔H2SO4将pH调节至5.0,并使用HAAKE Viscotester VT02型粘度计测量粘度。将木聚糖酶、纤维素酶、葡糖淀粉酶和酸性α-淀粉酶根据表3配制。将所述瓶调节至32℃并且添加0.25g干的面包酵母。将所述瓶在32℃水浴中在磁力搅拌下保持91小时。
表3.小麦和黑麦,91小时的重量损失(g)。根据本表添加包含CBM的酸性α-淀粉酶(AFAU),和葡糖淀粉酶(AGU)活性。 | ||
谷类 | 小麦 | 黑麦 |
%DS | 30 | 30 |
发酵前粘度,cP | 950 | 16500 |
FXU/kgDS | 300 | 300 |
EGU/kgDS | 350 | 350 |
AFAU/kgDS | 280 | 280 |
AGU/kgDS | 470 | 470 |
AFAU/AGU | 0.60 | 0.60 |
重量损失(g),91小时 | 17.2 | 17.1 |
发酵后粘度,cP | <30 | <30 |
乙醇w/w%,91小时 | 7.7 | 7.7 |
*基于91小时的重量损失,CO2损失(g)×1.045=EtOH(g)。
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Val Gly Arg Tyr Lys Gly Lys Ile Arg Ala Trp Asp Val Val Asn Glu
165 170 175
Ile Phe Asn Glu Asp Gly Thr Leu Arg Ser Ser Val Phe Ser Arg Leu
180 185 190
Leu Gly Glu Glu Phe Val Ser Ile Ala Phe Arg Ala Ala Arg Asp Ala
195 200 205
Asp Pro Ser Ala Arg Leu Tyr Ile Asn Asp Tyr Asn Leu Asp Arg Ala
210 215 220
Asn Tyr Gly Lys Val Asn Gly Leu Lys Thr Tyr Val Ser Lys Trp Ile
225 230 235 240
Ser Gln Gly Val Pro Ile Asp Gly Ile Gly Ser Gln Ser His Leu Ser
245 250 255
Gly Gly Gly Gly Ser Gly Thr Leu Gly Ala Leu Gln Gln Leu Ala Thr
260 265 270
Val Pro Val Thr Glu Leu Ala Ile Thr Glu Leu Asp Ile Gln Gly Ala
275 280 285
Pro Thr Thr Asp Tyr Thr Gln Val Val Gln Ala Cys Leu Ser Val Ser
290 295 300
Lys Cys Val Gly Ile Thr Val Trp Gly Ile Ser Asp Lys Asp Ser Trp
305 310 315 320
Arg Ala Ser Thr Asn Pro Leu Leu Phe Asp Ala Asn Phe Asn Pro Lys
325 330 335
Pro Ala Tyr Asn Ser Ile Val Gly Ile Leu Gln
340 345
<210>6
<211>419
<212>PRT
<213>Beta-葡聚糖酶 木霉属的菌种
<220>
<221>mat_肽
<222>(1)..(419)
<400>6
Met Asn Lys Pro Met Ser Ser Leu Leu Leu Ala Ala Thr Leu Leu Ala
1 5 10 15
Gly Gly Ser Ile Ala Gln Gln Thr Val Trp Gly Gln Cys Gly Gly Gln
20 25 30
Gly Trp Ser Gly Pro Thr Ser Cys Val Ala Gly Ser Ala Cys Ser Thr
35 40 45
Leu Asn Pro Tyr Tyr Ala Gln Cys Ile Pro Gly Ala Thr Thr Met Ser
50 55 60
Thr Thr Thr Lys Pro Thr Ser Val Ser Ala Ser Thr Thr Arg Ala Ser
65 70 75 80
Ala Thr Ser Ser Ala Thr Pro Pro Pro Ser Ser Gly Leu Thr Arg Phe
85 90 95
Ala Gly Val Asn Ile Ala Gly Phe Asp Phe Gly Cys Gly Thr Asp Gly
100 105 110
Thr Cys Val Thr Ser Lys Val Tyr Pro Pro Leu Lys Asn Tyr Ala Gly
115 120 125
Thr Asn Asn Tyr Pro Asp Gly Val Gly Gln Met Gln His Phe Val Asn
130 135 140
Asp Asp Lys Leu Thr Ile Phe Arg Leu Pro Val Gly Trp Gln Tyr Leu
145 150 155 160
Val Asn Asn Asn Leu Gly Gly Thr Leu Asp Ser Asn Asn Phe Gly Lys
165 170 175
Tyr Asp Gln Leu Val Gln Ala Cys Leu Ser Leu Gly Val Tyr Cys Ile
180 185 190
Val Asp Ile His Asn Tyr Ala Arg Trp Asn Gly Gly Ile Ile Gly Gln
195 200 205
Gly Gly Pro Thr Asn Asp Gln Phe Thr Ser Leu Trp Ser Gln Leu Ala
210 215 220
Gln Lys Tyr Ala Ser Gln Ser Lys Val Trp Phe Gly Ile Met Asn Glu
225 230 235 240
Pro His Asp Val Asn Ile Asn Thr Trp Ala Thr Thr Val Gln Ala Val
245 250 255
Val Thr Ala Ile Arg Asn Ala Gly Ala Thr Ser Gln Phe Ile Ser Leu
260 265 270
Pro Gly Asn Asp Trp Gln Ser Ala Gly Ala Phe Ile Ser Asp Gly Ser
275 280 285
Ala Ala Ala Leu Ser Gln Val Lys Asn Pro Asp Gly Ser Thr Pro Asn
290 295 300
Leu Ile Phe Asp Leu His Lys Tyr Leu Asp Ser Asp Asn Ser Gly Thr
305 310 315 320
His Ala Asp Cys Val Thr Asn Asn Val Asn Asp Ala Phe Ser Pro Val
325 330 335
Ala Thr Trp Leu Arg Gln Asn Asn Arg Gln Ala Ile Leu Thr Glu Thr
340 345 350
Gly Gly Gly Asn Thr Gln Ser Cys Ile Gln Tyr Leu Cys Gln Gln Phe
355 360 365
Gln Tyr Ile Asn Gln Asn Ser Asp Val Tyr Leu Gly Tyr Val Gly Trp
370 375 380
Gly Ala Gly Ser Phe Asp Ser Thr Tyr Ile Leu Thr Glu Thr Pro Thr
385 390 395 400
Gly Ser Gly Ser Ser Trp Thr Asp Thr Ser Leu Val Ser Ser Cys Ile
405 410 415
Ser Arg Lys
<210>7
<211>459
<212>PRT
<213>Beta-葡聚糖酶 绿色木霉(Trichoderma viride)
<220>
<221>mat_肽
<222>(1)..(459)
<400>7
Met Ala Pro Ser Val Thr Leu Pro Leu Thr Thr Ala Ile Leu Ala Ile
1 5 10 15
Ala Arg Leu Val Ala Ala Gln Gln Pro Gly Thr Ser Thr Pro Glu Val
20 25 30
His Pro Lys Leu Thr Thr Tyr Lys Cys Thr Lys Ser Gly Gly Cys Val
35 40 45
Ala Gln Asp Thr Ser Val Val Leu Asp Trp Asn Tyr Arg Trp Met His
50 55 60
Asp Ala Asn Tyr Asn Ser Cys Thr Val Asn Gly Gly Val Asn Thr Thr
65 70 75 80
Leu Cys Pro Asp Glu Ala Thr Cys Gly Lys Asn Cys Phe Ile Glu Gly
85 90 95
Val Asp Tyr Ala Ala Ser Gly Val Thr Thr Ser Gly Ser Ser Leu Thr
100 105 110
Met Asn Gln Tyr Met Pro Ser Ser Ser Gly Gly Tyr Ser Ser Val Ser
115 120 125
Pro Arg Leu Tyr Leu Leu Asp Ser Asp Gly Glu Tyr Val Met Leu Lys
130 135 140
Leu Asn Gly Gln Glu Leu Ser Phe Asp Val Asp Leu Ser Ala Leu Pro
145 150 155 160
Cys Gly Glu Asn Gly Ser Leu Tyr Leu Ser Gln Met Asp Glu Asn Gly
165 170 175
Gly Ala Asn Gln Tyr Asn Thr Ala Gly Ala Asn Tyr Gly Ser Gly Tyr
180 185 190
Cys Asp Ala Gln Cys Pro Val Gln Thr Trp Arg Asn Gly Thr Leu Asn
195 200 205
Thr Ser His Gln Gly Phe Cys Cys Asn Glu Met Asp Ile Leu Glu Gly
210 215 220
Asn Ser Arg Ala Asn Ala Leu Thr Pro His Ser Cys Thr Ala Thr Ala
225 230 235 240
Cys Asp Ser Ala Gly Cys Gly Phe Asn Pro Tyr Gly Ser Gly Tyr Lys
245 250 255
Ser Tyr Tyr Gly Pro Gly Asp Thr Val Asp Thr Ser Lys Thr Phe Thr
260 265 270
Ile Ile Thr Gln Phe Asn Thr Asp Asn Gly Ser Pro Ser Gly Asn Leu
275 280 285
Val Gly Ile Thr Arg Lys Tyr Gln Gln Asn Gly Val Asp Ile Pro Ser
290 295 300
Ala Gln Pro Gly Gly Asp Thr Ile Ser Ser Cys Pro Ser Ala Ser Ala
305 310 315 320
Tyr Gly Gly Leu Ala Thr Met Gly Lys Ala Leu Ser Ser Gly Met Val
325 330 335
Leu Val Phe Ser Ile Trp Asn Asp Asn Ser Gln Tyr Met Asn Trp Leu
340 345 350
Asp Ser Gly Asn Ala Gly Pro Cys Ser Ser Thr Glu Gly Asn Pro Ser
355 360 365
Asn Ile Leu Ala Asn Asn Pro Asn Thr His Val Val Phe Ser Asn Ile
370 375 380
Arg Trp Gly Asp Ile Gly Ser Thr Thr Asn Ser Thr Ala Pro Pro Pro
385 390 395 400
Pro Pro Ala Ser Ser Thr Thr Phe Ser Thr Thr Arg Arg Ser Ser Thr
405 410 415
Thr Ser Ser Ser Pro Ser Cys Thr Gln Thr His Trp Gly Gln Cys Gly
420 425 430
Gly Ile Gly Tyr Ser Gly Cys Lys Thr Cys Thr Ser Gly Thr Thr Cys
435 440 445
Gln Tyr Ser Asn Asp Tyr Tyr Ser Gln Cys Leu
450 455
<210>8
<21l>232
<212>PRT
<213>Beta-葡聚糖酶EG III木霉属的菌种
<220>
<221>mat_肽
<222>(1)..(232)
<400>8
Met Lys Phe Leu Gln Val Leu Pro Ala Leu Ile Pro Ala Ala Leu Ala
1 5 10 15
Gln Thr Ser Cys Asp Gln Trp Ala Thr Phe Thr Gly Asn Gly Tyr Thr
20 25 30
Val Ser Asn Asn Leu Trp Gly Ala Ser Ala Gly Ser Gly Phe Gly Cys
35 40 45
Val Thr Ala Val Ser Leu Ser Gly Gly Ala His Ala Asp Trp Gln Trp
50 55 60
Ser Gly Gly Gln Asn Asn Val Lys Ser Tyr Gln Asn Ser Gln Ile Ala
65 70 75 80
Ile Pro Gln Lys Arg Thr Val Asn Ser Ile Ser Ser Met Pro Thr Thr
85 90 95
Ala Ser Trp Ser Tyr Ser Gly Ser Asn Ile Arg Ala Asn Val Ala Tyr
100 105 110
Asp Leu Phe Thr Ala Ala Asn Pro Asn His Val Thr Tyr Ser Gly Asp
115 120 125
Tyr Glu Leu Met Ile Trp Leu Gly Lys Tyr Gly Asp Ile Gly Pro Ile
130 135 140
Gly Ser Ser Gln Gly Thr Val Asn Val Gly Gly Gln Ser Trp Thr Leu
145 150 155 160
Tyr Tyr Gly Tyr Asn Gly Ala Met Gln Val Tyr Ser Phe Val Ala Gln
165 170 175
Thr Asn Thr Thr Asn Tyr Ser Gly Asp Val Lys Asn Phe Phe Asn Tyr
180 185 190
Leu Arg Asp Asn Lys Gly Tyr Asn Ala Ala Gly Gln Tyr Val Leu Ser
195 200 205
Tyr Gln Phe Gly Thr Glu Pro Phe Thr Gly Ser Gly Thr Leu Asn Val
210 215 220
Ala Ser Trp Thr Ala Ser Ile Asn
225 230
Claims (24)
1.包括下列步骤的方法:
(a)提供包含水和粒状淀粉的浆液;
(b)在下列物质存在下保持所述浆液以产生发酵产品:i)包含糖结合模块的酸性α-淀粉酶,和和/或ii)发酵生物,和,
(c)任选地回收所述发酵产品。
2.根据权利要求1的方法,其中所述发酵生物是酵母。
3.根据权利要求1-2任一项的方法,其中步骤b进一步包含iii)木聚糖酶,iv)β-葡聚糖酶的存在。
4.根据权利要求1-3任一项的方法,其中步骤b进一步包含葡糖淀粉酶的存在,其优选来自曲霉属的菌种,并且更优选来自黑曲霉。
5.根据权利要求1-4任一项的方法,其中将所述浆液在步骤b)之前,在低于起始糊化温度0-30℃的温度,例如在35℃至45℃、40℃至50℃或45℃至55℃温育。
6.根据权利要求1-5任一项的方法,其中所述发酵产品是燃料乙醇、饮用乙醇和/或工业乙醇,例如燃料乙醇。
7.根据权利要求1-6任一项的方法,其中所述发酵浆液包含至少7%、至少8%、至少9%、至少10%例如至少11%、至少12%、至少13%、至少14%、至少15%例如至少16%的乙醇。
8.根据权利要求1-7任一项的方法,其中在步骤(b)中的温度是28℃-36℃,例如29℃-35℃,例如30℃-34℃,例如大约32℃。
9.根据权利要求1-8任一项的方法,其中所述包含CBM的酸性α-淀粉酶是多肽,所述多肽与下组中的任何氨基酸序列具有至少50%的同源性:SEQID NO:1、SEQ ID NO:2和SEQ ID NO:3。
10.根据权利要求1-9任一项的方法,其中包含CBM的酸性α-淀粉酶是包含氨基酸序列的α-淀粉酶,所述氨基酸序列与选自下组的任何序列具有至少70%,优选至少75%、80%、85%或至少90%,例如至少95%、至少97%、至少98%,或至少99%的同源性:SEQ ID NO:1、SEQ ID NO:2和SEQ ID NO:3。
11.权利要求1-10任一项的方法,其中所述木聚糖酶源自曲霉属的菌种的菌株,优选源自棘孢曲霉的菌株,并且更优选所述木聚糖酶具有SEQ IDNO:4中所示的氨基酸序列。
12.权利要求1-11任一项的方法,其中所述β-葡聚糖酶源自木霉属的菌种的菌株,优选源自T.reesei的菌株。
13.根据权利要求1-12任一项的方法,其中所述酸性α-淀粉酶活性以50-500 AFAU/kg的DS的量存在。
14.根据权利要求1-13任一项的方法,其中所述葡糖淀粉酶活性以20-200AGU/kg的DS的量存在。
15.根据权利要求1-14任一项的方法,其中所述酸性α-淀粉酶活性和葡糖淀粉酶活性的比例是0.35-5.00 AFAU/AGU。
16.权利要求1-15任一项的方法,其中所述淀粉浆液具有5-60%DS粒状淀粉,优选10-50%DS粒状淀粉,更优选20-40%DS,特别是大约30%,例如至少31%,例如至少32%,例如至少33%,例如至少34%,例如至少35%,或甚至例如至少36%DS粒状淀粉。
17.权利要求1-16任一项的方法,其中步骤b过程中的乙醇含量达到至少7%、至少8%、至少9%、至少10%、至少11%、至少12%、至少13%、至少14%至少16%,至少17%(w/w)。
18.权利要求1-17任一项的方法,其中步骤(b)过程中的pH在3.0-7.0的范围内,优选3.5至6.0,或更优选4.0至5.0,例如4.3至4.6。
19.权利要求1-18任一项的方法,其中所述粒状淀粉得自块茎、根、茎、果实、种子、谷类和/或整谷粒。
20.权利要求1-19任一项的方法,其中所述粒状淀粉得自谷类,优选得自小麦、大麦和/或黑麦。
21.权利要求1-20任一项的方法,其中所述粒状淀粉得自玉米。
22.权利要求1-21任一项的方法,其中所述粒状淀粉得自整谷粒的干磨。
23.组合物,其包含:i)含有CBM的酸性α-淀粉酶和ii)葡糖淀粉酶和/或iii)β-葡聚糖酶,和/或iv)木聚糖酶。
24,根据权利要求23的组合物,其中所述含有CBM的酸性α-淀粉酶是杂合体。
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EP (1) | EP1831383A1 (zh) |
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US20040219649A1 (en) | 2003-03-10 | 2004-11-04 | Novozymes A/S | Alcohol product processes |
US8841091B2 (en) | 2004-12-22 | 2014-09-23 | Novozymes Als | Enzymes for starch processing |
AU2005319074B2 (en) * | 2004-12-22 | 2011-03-24 | Novozymes A/S | Enzymes for starch processing |
WO2008150880A1 (en) * | 2007-06-01 | 2008-12-11 | Syngenta Participations Ag | Process for starch liquefaction and fermentation |
BRPI0912291A2 (pt) * | 2008-05-29 | 2015-08-04 | Danisco Us Inc | Processo para produção de coproduto e álcool a partir de sorgo em grão |
WO2010129287A2 (en) | 2009-04-27 | 2010-11-11 | The Board Of Trustees Of The University Of Illinois | Hemicellulose-degrading enzymes |
WO2012149275A1 (en) * | 2011-04-29 | 2012-11-01 | Danisco Us Inc. | Use of cellulase and glucoamylase to improve ethanol yields from fermentation |
JP6084617B2 (ja) | 2011-09-14 | 2017-02-22 | デュポン ニュートリション バイオサイエンシーズ エーピーエス | 酵素 |
BR112015001767A2 (pt) | 2012-08-03 | 2017-08-08 | Dupont Nutrition Biosci Aps | enzimas |
US9334516B2 (en) | 2013-03-14 | 2016-05-10 | Abengoa Bioenergy New Technologies, Inc. | Method for adding enzymes to obtain high ethanol yield from cereal mash |
EP3017706A1 (en) | 2014-11-05 | 2016-05-11 | Dupont Nutrition Biosciences ApS | Enzymes for malting |
CN114717217A (zh) | 2014-12-19 | 2022-07-08 | 诺维信公司 | 包括具有木聚糖酶活性的多肽和具有***呋喃糖苷酶活性的多肽的组合物 |
HUE061031T2 (hu) | 2015-11-26 | 2023-05-28 | Novozymes As | Õrlési eljárás |
CA3006992A1 (en) | 2015-12-22 | 2017-06-29 | Novozymes A/S | Processes for improving fermentation product yield using phospholipase c |
EA037907B1 (ru) | 2016-05-02 | 2021-06-04 | Карлсберг Брюириз А/С | Напитки, содержащие -глюкан ячменя |
CN109641973B (zh) | 2016-11-25 | 2022-03-08 | 诺维信公司 | Gh10木聚糖酶、gh62***呋喃糖苷酶、研磨方法以及其他应用 |
MX2020011244A (es) * | 2018-04-25 | 2021-01-20 | Carlsberg As | Bebidas a base de cebada. |
CN115747262A (zh) * | 2021-09-03 | 2023-03-07 | 国投生物科技投资有限公司 | 利用小麦生产乙醇的方法 |
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US20040115779A1 (en) * | 2002-03-19 | 2004-06-17 | Olsen Hans Sejr | Fermentation process |
BRPI0408215B1 (pt) * | 2003-03-10 | 2015-11-03 | Broin And Associates Inc | processo para a produção de etanol usando amido bruto |
US20040219649A1 (en) * | 2003-03-10 | 2004-11-04 | Novozymes A/S | Alcohol product processes |
WO2004087889A1 (en) * | 2003-04-04 | 2004-10-14 | Novozymes A/S | Mash viscosity reduction |
US20080113418A1 (en) * | 2004-01-16 | 2008-05-15 | Novozymes A/S | Processes for Producing a Fermantation Product |
AU2005319074B2 (en) * | 2004-12-22 | 2011-03-24 | Novozymes A/S | Enzymes for starch processing |
-
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- 2005-12-16 CN CNA2005800442665A patent/CN101087887A/zh active Pending
- 2005-12-16 US US11/720,098 patent/US20090117630A1/en not_active Abandoned
- 2005-12-16 EP EP05821060A patent/EP1831383A1/en not_active Withdrawn
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WO2006066582A1 (en) | 2006-06-29 |
US20090117630A1 (en) | 2009-05-07 |
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