CN1128221C - 编码碱性液化α-淀粉酶的基因 - Google Patents

编码碱性液化α-淀粉酶的基因 Download PDF

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CN1128221C
CN1128221C CN96194754A CN96194754A CN1128221C CN 1128221 C CN1128221 C CN 1128221C CN 96194754 A CN96194754 A CN 96194754A CN 96194754 A CN96194754 A CN 96194754A CN 1128221 C CN1128221 C CN 1128221C
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秦田勇二
尾崎克也
荒胜俊
川合修次
伊藤进
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Abstract

本发明提供一种编码碱性液化α-淀粉酶的DNA片段、包括该DNA片段的重组DNA、含有该重组DNA的转化的微生物和一种利用转化子生产碱性液化α-淀粉酶的方法。本发明的方法能够大规模生产作为一种洗涤剂的成分有用的碱性液化α-淀粉酶。

Description

编码碱性液化α-淀粉酶的基因
技术领域
本发明涉及编码碱性液化α-淀粉酶的基因和其片段,还涉及重组DNA和带有该基因或该基因的片段的转化子。
背景技术
长久以来α-淀粉酶一直被用于多个领域。例如,在发酵业中它一直被用于谷物和马铃薯的糖化,在纺织业中用作淀粉糊去除剂,在制药业中用作助消化药,而在食品业中用于制造粘稠的麦芽糖浆。α-淀粉酶是一种作用于淀粉相关多糖如直链淀粉和支链淀粉,单一地水解多糖分子中α-1,4-糖苷键的酶。自从1833年当时Payen和Persoz首次发现这种酶开始,已经从包括细菌、真菌、植物种子和动物消化腺等许多不同的来源中获得了α-淀粉酶的晶体样品或电泳上均质的样品。
发明内容
本发明的发明者们最近发现当将α-淀粉酶和支链淀粉酶都掺入洗碗剂和衣物洗涤剂中时,洗碗剂和衣物洗涤剂的效能可被大大提高,特别是对淀粉污渍(日本专利申请公开(kokai)2-132192号)。然而,以前在自然界中发现的大部分α-淀粉酶在中性到酸性pH范围内表现出最大且稳定的酶切活性,但在pH9-10的碱性溶液中却很少发挥作用。已知只有少数的淀粉酶在碱性的pH范围内表现最大的活性(所谓的碱性α-淀粉酶和耐碱α-淀粉酶)。这些碱性α-淀粉酶和耐碱α-淀粉酶包括由芽孢杆菌属sp.A-40-2产生的一种酶〔Horikoshi,K.等,《农业与生物化学》(Agric.Biol.Chem.),35,1783(1971)〕,由芽孢杆菌属sp.NRRL B-3881产生的一种酶〔Boyer,E.等,《细菌学杂志》(J.Bacteriol.),110,992(1972)〕,由链霉菌属sp.KSM-9产生的一种酶(日本专利申请公开(kokai)61-209528号),由芽孢杆菌属sp.H-167产生的一种酶(日本专利申请公开(kokai)62-208278号),由嗜热碱性芽孢杆菌sp.A3-8产生的一种酶(日本专利申请公开(kokai)2-49584号)以及由嗜盐碱球菌属sp.AH-36产生的一种酶(日本专利申请公开(kokai)4-211369号)。
这里所用的,术语“碱性α-淀粉酶”指最适pH落在碱性pH范围中的α-淀粉酶,而术语“耐碱α-淀粉酶”指最适pH在中性至酸性范围内但其在碱性范围内的活性与在最适pH时的活性类似且在碱性范围内保持其稳定性的淀粉酶。术语“中性范围”意指低于8且不小于6的pH范围,而“碱性”表示高于“中性范围”的pH。
这些碱性α-淀粉酶和耐碱α-淀粉酶的大部分是将淀粉或淀粉相关多糖分解为葡萄糖、麦芽糖或麦芽三糖的所谓的糖化α-淀粉酶。据此,虽然它们被有效地用于制糖业中,但如果将它们用作洗涤剂的酶却会产生问题。因此,仍然需要对用于洗涤剂中的表面活化剂具有抗性并以一种高度随机的方式分解淀粉或淀粉相关多糖的所谓的碱性液化α-淀粉酶。本发明者们持续深入地寻找产生适于作为洗涤剂成分的碱性α-淀粉酶的微生物,并发现其生长最适pH在碱性范围内的嗜碱芽孢杆菌sp.KSM-AP1378菌株产生一种表现碱性液化α-淀粉酶活性的酶。他们证明这种酶作为用于洗碗和厨房用具的洗涤剂组合物以及用于洗衣的洗涤剂组合物中的一种添加剂是有效的(WO94/26881)。
通过改善用于产碱性α-淀粉酶微生物芽孢杆菌sp.KSM-AP1378的培养方法或通过利用突变可以有效增加所产生的酶的量。然而,为了以一种工业化的规模有利地生产这种酶,必需采取其它方法。
利用一种基因工程的方法可以提高所生产的酶的量,另外,利用一种基因工程方法通过改变编码酶的基因提高酶的催化活性。然而,仍未获得编码一种碱性液化α-淀粉酶的基因。
相应地,本发明的一个目的是提供编码碱性液化α一淀粉酶的基因和其片段、一种含有包括该基因的重组DNA的转化子和一种用于利用该转化子生产碱性液化α-淀粉酶的方法。
编码碱性液化α-淀粉酶基因的DNA进一步可被用来制备用于从其它微生物中分离其它的同源碱性液化α-淀粉酶基因的探针。因此,本发明的另一目的是提供一种筛选和分离其它碱性液化α-淀粉酶的方法。
本发明者们试图从一种嗜碱芽孢杆菌菌株的染色体DNA中分离一种含有编码碱性液化α-淀粉酶基因的DNA片段,结果,他们成功分离了一个大约1.8kb的编码一种碱性液化α-淀粉酶的DNA片段。当他们利用被连至一合适载体的该DNA片段转化一种宿主微生物时,证实了所获的重组微生物产生一种碱性液化α-淀粉酶。此外,发现所编码的碱性液化α-淀粉酶的氨基酸序列与以前已知的淀粉酶不同。基于这个发现完成了本发明。
相应地,本发明提供编码一种碱性液化α-淀粉酶的DNA片段。
本发明还提供一种含有上述的编码碱性液化α-淀粉酶的DNA片段的重组DNA。
本发明还提供一种包含上述的含有编码碱性液化α-淀粉酶的DNA片段的重组DNA的转化的微生物。
本发明进一步提供一种用于通过培养上述的转化的微生物产生一种碱性液化α-淀粉酶并收集酶的方法。
附图说明
图1表现编码一种碱性液化淀粉酶的基因片段的限制性酶图谱。
图2是一个描述利用编码一种碱性液化淀粉酶的基因片段构建pAML100的图。
图3表现所用引物的核苷酸序列。
图4是一个由芽孢杆菌sp.KSM-AP1378产生的一种碱性液化α-淀粉酶的pH曲线。
在本发明中,用作一种碱性液化α-淀粉酶基因供体的一个有效的微生物例如可以是芽孢杆菌sp.KSM-AP1378(FERM BP-3048,1989年7月24日寄存于发酵研究所(Fermentation Research Institute),工业科学和技术代理处(Agency of Industrial Science and Technology)1-3,Higashi 1-chome,Tsukuba-shi,Ibaraki,305日本),它是一种嗜碱芽孢杆菌菌株。这种菌株是由本发明者在日本Tochigi县的Tochigi城附近从土壤中分离到并鉴定为一种产生显著量的碱性液化α-淀粉酶的菌株。该菌株在1990年8月8日以FERM BP-3048(最初于1989年7月24日保存为P-10886)保存在发酵研究所,工业科学和技术代理处(1-3,Higashi 1-chome,Tsukuba-shi,Ibaraki-ken,305,日本)。
为了从供体微生物中获得染色体DNA,可利用由Marmur,J.(《分子生物学杂志》(J.Mol.Biol.),3,208(1961))建议的方法或由Saito,H.和Miura,K.(《生物化学与生物物理学学报》(Biochem.Biophys.Acta),72,619(1963))建议的方法。也可使用其它类似的方法。
通过利用限制性酶切割所获的染色体DNA制备含有碱性液化α-淀粉酶基因的DNA片段。对于可使用的限制性酶只要不切割该基因则并无特殊限制。也可通过PCR获得碱性液化α-淀粉酶的基因(Mullis,K.B.和Faloona,F.A.,《酶学方法》(Methods Enzymol.),155,355(1987);Saiki,R.K.等,《科学》(Science),239,487(1988))。例如,根据在序列号2中描述的核苷酸序列通过合成具有与那些在核心区域的5’-末端的上游和3’-末端的下游序列相应的序列的引物,随后通过将产一种碱性液化α-淀粉酶的微生物的染色体DNA用作模板进行PCR可以获得基因。另外,可通过利用任何方法从产一种碱性液化α-淀粉酶的微生物中首先获得碱性液化α-淀粉酶基因的一个片段,随后通过PCR扩增该片段基因的上游和下游区。
然后将所制备的基因片段进行克隆。只要宿主细菌表达本发明的碱性液化α-淀粉酶基因,重组DNA分子在宿主菌中可被复制并且整合的基因可被稳定地保留,则对可利用的宿主/载体系统并无特殊限制。例如,宿主是大肠杆菌K-12的EK系统的成员和宿主为Marburg枯草芽孢杆菌的BS系统的成员都可以使用。利用包含许多种载体并且遗传学上被深入地研究过的EK系统可获得良好的结果,因而是优选的。宿主细菌的特定的例子包括EK系统的HB101、C600和JM109,以及BS系统的BD170、MI112和ISW1214。载体的特定的例子包括用于EK系统pBR322和pUC18,以及用于BS系统的pUB110和pHY300PLK。
通过用一限制性酶切割一种载体随后与上述的染色体或PCR扩增的DNA片段连接产生一种重组质粒DNA分子。例如通过利用一种DNA连接酶可以实现连接。
对利用一重组DNA分子转化宿主细菌的方法并无特殊的限制。例如,在EK系统宿主的情况下可用氯化钙法(Mandel,M.和Higa,A.,《分子生物学杂志》,53,159(1970)),而在BS系统宿主的情况下可用原生质体法(Chang,C.和Cohen,S.N.,《分子遗传学与普通遗传学》(Mol.Gen.Genet.),168,111(1978))。按照下面的方法进行重组子微生物的筛选。首先,利用一种未由外源染色体DNA片段的插入而失活的特性作为一种指标如载体DNA上编码的对抗生素的抗性,来筛选用含有载体衍生的DNA片段转化的微生物。例如,在一利用EK系统的pBR322作为载体并将染色体DNA的一个HindIII片段插入pBR322的HindIII切割位点中的特定例子中,四环素抗性基因失活,所以可以通过在氨苄青霉素基因中不带有HindIII切割位点而赋予氨苄青霉素抗性的转化子的生长进行初次筛选。随后,将所选的转化子利用如影印方法转移至含有淀粉的琼脂平板上,然后进行培养以便形成菌落。因为靶重组子微生物在集落周围分解淀粉,所以通过利用一种含碘溶液对在含有淀粉的琼脂平板中所含的淀粉染色可以对其进行筛选。
利用制备质粒或噬菌体DNA的标准程序可以提取由所获的重组微生物包含的重组DNA分子(Maniatis,T.等,《分子克隆》(MolecularCloning),冷泉港实验室,纽约(1982))。在利用电泳分析通过利用各种限制性酶所获得的切割模式时,证实重组DNA分子是载体DNA分子和一个含有碱性液化α-淀粉酶的DNA片段的连接产物。
在图1的限制性酶切图谱中所表现的一个大约2.1kb的DNA片段内含有编码一种碱性液化α-淀粉酶的基因,并存在于由白色带表示的大约1.6kb的片段中。该基因具有一个显示在序列号2中的核苷酸序列。在此序列中,5’末端和3’末端分别对应于显示在序列2中的大约2.1kb片段的左手侧和右手侧。在此序列中观察到一个在第145个核苷酸ATG处开始并编码一个由序列号1中所描述的516个氨基酸残基组成的序列的开放阅读框架(ORF)。ORF上游13个碱基(13b)处存在一个与枯草芽孢杆菌16S核糖体RNA的3’末端序列高度互补的AAGGAG序列(McLaughlin,J.R.等,《生物学和化学杂志》(J.Biol.Chem.),256,11283(1981))。在核苷酸由9延伸至36的更加上游的区域中,存在一个与一种σA-型启动子的共有序列具有高度同源性的TTGAAA……16b……TATGGT序列(Gitt,M.A.等,《生物学与化学杂志》,260,7178(1985))。类似地,在从95到125的核苷酸中发现另一个σA-型启动子序列。从芽孢杆菌sp.KSM-AP1378培养物纯化的碱性液化α-淀粉酶中氨基末端侧的10个氨基酸残基的氨基酸序列与由该DNA片段的核苷酸序列所推导的第37个氨基酸延伸的序列(序列号2中的37-46号氨基酸)一致。
当将本发明中基因的核苷酸序列和所推导的氨基酸序列与那些目前已知的α-淀粉酶相比较时,证实该基因包括一种新型核苷酸序列,所推导的由该基因编码的氨基酸序列与那些其它α-淀粉酶如由解淀粉芽孢杆菌产生的一种液化α-淀粉酶(Takkinen,K.等,《生物学与化学杂志》,258,1007(1983))、由嗜热脂肪芽孢杆菌产生的一种液化α-淀粉酶(Nakajima,R.等,《细菌学杂志》(J.Bacteriol.),163,401(1985))、由地衣芽孢杆菌产生的一种液化α-淀粉酶(Yuuki,T.等,《生物化学杂志》(J.Biochem.),98,1147(1985))或由芽孢杆菌sp.707产生的一种液化α-淀粉酶(Tsukamoto,A.等,《生物化学与生物物理学研究通讯》(Biochem.Biophys.Res.Commun.),151,25(1988))不同。
含有碱性液化α-淀粉酶基因完整区域的一个优选的重组DNA分子的例子是质粒pAML100(图2)。这个重组质粒大小为4.4kb并形成一个含有包括碱性液化α-淀粉酶基因和pUC19的一个1.8kb片段的片段。包含该重组DNA分子的一个优选的重组微生物是一种大肠杆菌HB101(pAML100)菌株。通过用重组质粒pAML100以一种标准的转化方法转化大肠杆菌HB101获得该菌株。当用一种常规用来培养大肠杆菌的培养基培养该菌株时,它产生一种碱性液化α-淀粉酶。所产生的酶的最适反应pH为pH8-9。这与对由该基因的供体细菌菌株芽孢杆菌sp.KSM-AP1378产生的碱性液化α-淀粉酶所确定的活性-pH关系曲线(图4)非常一致。
本发明的DNA片段,只要它们编码一种表现所需酶切活性的的蛋白质,则不一定仅限于那些编码在下述的序列表中所列氨基酸序列的DNA,这包括编码一种其中一个或多个氨基酸被置换、增加、缺失、倒位或插入的氨基酸序列的DNA片段。这种DNA的一个例子是一个编码一种等价于在序列号1中所描述的氨基酸序列而N-末端有多至32个氨基酸已缺失的氨基酸序列的DNA。
为了利用本发明中被转化的微生物生产一种碱性液化α-淀粉酶,将一种被转化的含有本发明中前面提到的DNA片段的微生物进行培养。另外,可将该DNA片段整合入许多表达载体来获得具有提高了表达能力的被转化的微生物,随后培养所获的转化子。此外,根据微生物的特性可在不同的条件下培养被转化的微生物。因此,可以使用适于宿主的培养条件。为了从所获的培养物中收集一种碱性液化α-淀粉酶,可使用一种常规的方法(如在WO94/26881中所描述的方法)。
可以进一步将本发明中的DNA片段用作探针用于从其它生物中分离同源的碱性液化α-淀粉酶基因。
具体实施方式
实施例
下面将要通过实施例更详细地描述本发明,这些实施例不应被认为是将本发明限定于此。在实施例中的浓度都是以重量的%为基础。
实施例1:
将产生一种碱性液化α-淀粉酶的芽孢杆菌sp.KSM-AP1378接种在5ml培养基A(表1)中并在30℃进行振荡培养24小时。将1ml培养物接种于100ml同样的培养基中,然后在30℃再次振荡培养12小时。随后,通过离心收集细胞并按照由Saito和Miura推荐的方法(Saito,H.和Miura,K.,《生物化学与生物物理学学报》(Biochem.Biophys.Acta),72,619(1963))获得大约1mg的染色体DNA。
                               表1
                         培养基A的组成
             可溶性淀粉                   1.0%
             多聚蛋白胨                   1.0%
             酵母提取物                   0.5%
             KH2PO4                     0.1%
             Na2HPO4·12H2O            0.25%
             MgSO4·7H2O                0.02%
             CaCl2·2H2O                0.02%
             FeSO4·7H2O                0.001%
             MnCl2·4H2O                0.0001%
             Na2CO3                     1.0%(单独灭菌)
实施例2:
已知淀粉酶家族的许多成员具有氨基酸序列高度保守的I-IV区(Nakajima,R.等,《应用微生物学与生物技术》(Appl.Microbiol.Biotechnol.),23,355(1986))。因而,根据在已知的碱性液化α-淀粉酶的I到IV区中非常保守的II区和IV区的氨基酸序列合成与II区和IV区相应的引物1和2(图1和3)。利用所合成的引物和KSM-AP1378的染色体DNA(用作模板)进行PCR(1个循环=94℃×1min+42℃×1min+60℃×2min,30个循环)。获得了在图1中所示的一个大约0.3kb的基因片段(片段A),并测定了该片段的核苷酸序列。结果,发现该片段编码一种表现出与已知液化淀粉酶的从II区延伸到IV区的氨基酸序列具有一种不可忽视水平同源性的氨基酸序列。
实施例3:
利用片段A作为一个探针,对经XbaI消化的KSM-AP1378的染色体DNA进行Southern杂交。结果,证实在大约1.0kb位置处杂交有一条带。利用从片段A的末端序列合成的引物(在II区侧:引物3;在IV区侧:引物4)和通过分子内连接XbaI消化的KSM-AP1378的染色体DNA(图1)而获得的DNA作为模板,通过一种反向PCR方法(Triglia,T.等,《核酸研究》(Nucleic Acids Res.),16,81(1988))获得一个大约0.7kb的扩增片段(片段B)。对片段B测定其核苷酸序列,其序列揭示该片段含有一段IV区下游的大约0.6kb区域的序列。该片段含有一个ORF的终止密码子,推测其归因于碱性液化α-淀粉酶。
实施例4:
基于来自KSM-AP1378菌株的碱性液化α-淀粉酶的N-末端氨基酸序列(7个氨基酸)(图3)设计并合成一个引物。利用所得的引物(引物5)联合前面所述的引物3(图3)并以KSM-AP1378的染色体DNA作为模板,进行PCR获得一个大约0.7kb的片段(片段C,图1),然后测定其核苷酸序列。
实施例5:
合成一个含有21个碱基、在编码所纯化的酶N-末端氨基酸序列的核苷酸序列的下游直接延伸的引物(引物6)。利用引物6和7(图1和3)并以通过分子内连接HindIII消化的KSM-AP1378染色体DNA所获的DNA(图1)为模板,进行反向PCR,获得一个其中在HindIII位点将一个上游的0.8kb片段(片段D)和一个下游的PstI-HindIII 0.4kb片段连接起来的1.2kb片段。对片段D区的核苷酸序列进行测定,揭示了一个由31个氨基酸组成的信号序列MKLHNRIISVLLTLLLAVAVLFPYMTEPAQA(从序列号2的第1到第31位)、一个推导的由AAGGAG组成的SD序列(核苷酸127-132;McLaughlin,J.R.等,《生物学与化学杂志》,260,7178(1985))和两种推导的启动子序列(-35序列,TTGAAA;-10序列,TATGGT和-35序列,TTGACT;-10序列,TAAATT)的存在。
实施例6:
利用定位于启动子序列上游大约0.1kb处的引物A、定位于中止密码子下游79b处的引物B并以KSM-AP1378的染色体DNA作为模板,通过PCR扩增在引物间的大约1.8kb的片段。将所获的扩增片段插入pUC19的SmaI位点,然后引入大肠杆菌HB101。转化子可以在含有0.4%的淀粉天青和15ug/ml氨苄青霉素的LB琼脂培养基上生长。分离在周围形成透明晕环的集落作为产生液化α-淀粉酶的大肠杆菌菌株。从该转化子中制备重组质粒,并制备质粒的限制性酶切图谱。在图谱中,证实含有一个在图1中所示的大约1.8kb的DNA片段(片段E)。这个重组质粒被定名为质粒pAML100(图2)。
实施例7:
将在实施例6中获得的重组大肠杆菌于5ml含有50ug/ml氨苄青霉素的LB液体培养基中振荡培养12小时。将1ml培养物接种于100ml LB培养基(含有氨苄青霉素)中,然后在37℃振荡培养24小时。将通过离心分离收集的细胞悬于Tris-HCl缓冲液(pH8.0)中,并通过超声处理破坏细胞。细胞被超声处理后,通过离心分离清除细胞碎片,并将所获的上清用作一种无细胞提取物。作为对照,以一种相似的方式分别制备HB101(pUC19)菌株的无细胞提取物。首先通过在一含有50mM甘氨酸-NaCl-NaOH缓冲液(pH10)和可溶性淀粉的反应混合物中于50℃反应15分钟,然后通过利用3,5-二硝基水杨酸方法定量测定所产生的还原糖来检测这些提取物中的α-淀粉酶活性(WO94/26881)。将1个单位的酶活性定义为每分钟产生还原糖的量等价于1μmol葡萄糖的蛋白质的量。因而,在菌株HB101(pAML100)的无细胞提取物中检测α-淀粉酶的活性。发现α-淀粉酶的最适工作pH落在8到9之间pH范围中。这个结果与由芽孢杆菌sp.KSM-AP1378产生的液化α-淀粉酶的最适pH非常一致(图4)。对于酶活性的测定,利用下面表2中所示的缓冲液(各为40mM)。
                                 表2
           pH 3.5-5.5:             醋酸盐缓冲液
           pH 5.5-8.5:             Tris-马来酸缓冲液
           pH 8.5-10.5:            甘氨酸-NaCl-
                                    NaOH缓冲液
           pH 10.5-11.0:           Na2CO3-NaHCO3
                                    缓冲液
根据本发明,获得一个编码在碱性pH范围内表现最大活性的碱性液化α-淀粉酶的基因和含有这种基因的微生物是可能的。利用它们便于碱性液化α-淀粉酶的大量生产。
                                 序列表序列号1的资料:(i)序列特征:
(A)长度:516个氨基酸
(B)类型:氨基酸
(D)拓扑结构:线性(ii)分子类型:肽(xi)序列描述:序列号1:Met Lys Leu His Asn Arg Ile Ile Ser Val Leu Leu Thr Leu Leu Leu1               5                  10                  15Ala Val Ala Val Leu Phe Pro Tyr Met Thr Glu Pro Ala Gln Ala His
         20                  25                  30His Asn Gly Thr Asn Gly Thr Met Met Gln Tyr Phe Glu Trp His Leu
     35                  40                  45Pro Asn Asp Gly Asn His Trp Asn Arg Leu Arg Asp Asp Ala Ala Asn
 50                  55                  60Leu Lys Ser Lys Gly Ile Thr Ala Val Trp Ile Pro Pro Ala Trp Lys65                  70                  75                  80Gly Thr Ser Gln Asn Asp Val Gly Tyr Gly Ala Tyr Asp Leu Tyr Asp
             85                  90                  95Leu Gly Glu Phe Asn Gln Lys Gly Thr Val Arg Thr Lys Tyr Gly Thr
        100                 105                 110Arg Ser Gln Leu Gln Gly Ala Val Thr Ser Leu Lys Asn Asn Gly Ile
    115                 120                 125Gln Val Tyr Gly Asp Val Val Met Asn His Lys Gly Gly Ala Asp Gly
130                 135                 140Thr Glu Met Val Asn Ala Val Glu Val Asn Arg Ser Asn Arg Asn Gln145                 150                 155                 160Glu Ile Ser Gly Glu Tyr Thr Ile Glu Ala Trp Thr Lys Phe Asp Phe
        165                 170                 175Pro Gly Arg Gly Asn Thr His Ser Asn Phe Lys Trp Arg Trp Tyr His
        180                 185                 190Phe Asp Gly Thr Asp Trp Asp Gln Ser Arg Gln Leu Gln Asn Lys Ile
    195                 200                 205Tyr Lys Phe Arg Gly Thr Gly Lys Ala Trp Asp Trp Glu Val Asp Ile
210                 215                 220Glu Asn Gly Asn Tyr Asp Tyr Leu Met Tyr Ala Asp Ile Asp Met Asp225                 230                 235                 240His Pro Glu Val Ile Asn Glu Leu Arg Asn Trp Gly Val Trp Tyr Thr
            245                 250                 255Asn Thr Leu Asn Leu Asp Gly Phe Arg Ile Asp Ala Val Lys His Ile
        260                 265                 270Lys Tyr Ser Tyr Thr Arg Asp Trp Leu Thr His Val Arg Asn Thr Thr
    275                 280                 285Gly Lys Pro Met Phe Ala Val Ala Glu Phe Trp Lys Asn Asp Leu Ala
290                 295                 300Ala Ile Glu Asn Tyr Leu Asn Lys Thr Ser Trp Asn His Ser Val Phe305                 310                 315                 320Asp Val Pro Leu His Tyr Asn Leu Tyr Asn Ala Ser Asn Ser Gly Gly
            325                 330                 335Tyr Phe Asp Met Arg Asn Ile Leu Asn Gly Ser Val Val Gln Lys His
        340                 345                 350Pro Ile His Ala Val Thr Phe Val Asp Asn His Asp Ser Gln Pro Gly
    355                 360                 365Glu Ala Leu Glu Ser Phe Val Gln Ser Trp Phe Lys Pro Leu Ala Tyr
370                 375                 380Ala Leu Ile Leu Thr Arg Glu Gln Gly Tyr Pro Ser Val Phe Tyr Gly385                 390                 395                 400Asp Tyr Tyr Gly Ile Pro Thr His Gly Val Pro Ser Met Lys Ser Lys
            405                 410                 415Ile Asp Pro Leu Leu Gln Ala Arg Gln Thr Tyr Ala Tyr Gly Thr Gln
        420                 425                 430His Asp Tyr Phe Asp His His Asp Ile Ile Gly Trp Thr Arg Glu Gly
    435                 440                 445Asp Ser Ser His Pro Asn Ser Gly Leu Ala Thr Ile Met Ser Asp Gly
450                 455                 460Pro Gly Gly Asn Lys Trp Met Tyr Val Gly Lys His Lys Ala Gly Gln465                 470                 475                 480Val Trp Arg Asp Ile Thr Gly Asn Arg Ser Gly Thr Val Thr Ile Asn
            485                 490                 495Ala Asp Gly Trp Gly Asn Phe Thr Val Asn Gly Gly Ala Val Ser Val
        500                 505                 510Trp Val Lys Gln
        516序列号2的资料:(i)序列特征:
(A)长度:1776个碱基对
(B)类型:核酸
(C)成链类型:双链
(D)拓扑结构:线性(ii)分子类型:DNA(基因组)(vi)来源:
(A)生物体:芽孢杆菌属
(B)菌株:  KSM-AP1378(xi)序列描述:序列号2:ATATAAATTT GAAATGAACA CCTATGAAAA TATGGTAGCG ATTGCGCGAC GAGAAAAAAC     60TTGGGAGTTA GGAAGTGATA TTAAAGGATT TTTTTTGACT TGTTGTGAAA ACGCTTGCAT    120AAATTGAAGG AGAGGGTGCT TTTT ATG AAA CTT CAT AAC CGT ATA ATT AGC GTA   174
                       Met Lys Leu His Asn Arg Ile Ile Ser Val
                         1               5                  10CTA TTA ACA CTA TTG TTA GCT GTA GCT GTT TTG TTT CCA TAT ATG ACG      222Leu Leu Thr Leu Leu Leu Ala Val Ala Val Leu Phe Pro Tyr Met Thr
             15                  20                  25GAA CCA GCA CAA GCC CAT CAT AAT GGG ACG AAT GGG ACC ATG ATG CAG      270Glu Pro Ala Gln Ala His His Asn Gly Thr Asn Gly Thr Met Met Gln
         30                  35                  40TAT TTT GAA TGG CAT TTG CCA AAT GAC GGG AAC CAC TGG AAC AGG TTA      318Tyr Phe Glu Trp His Leu Pro Asn Asp Gly Asn His Trp Asn Arg Leu
     45                  50                  55CGA GAT GAC GCA GCT AAC TTA AAG AGT AAA GGG ATT ACC GCT GTT TGG      366Arg Asp Asp Ala Ala Asn Leu Lys Ser Lys Gly Ile Thr Ala Val Trp
 60                  65                  70ATT CCT CCT GCA TGG AAG GGG ACT TCG CAA AAT GAT GTT GGG TAT GGT      414Ile Pro Pro Ala Trp Lys Gly Thr Ser Gln Asn Asp Val Gly Tyr Gly75                  80                  85                  90GCC TAT GAT TTG TAC GAT CTT GGT GAG TTT AAC CAA AAG GGA ACC GTC      462Ala Tyr Asp Leu Tyr Asp Leu Gly Glu Phe Asn Gln Lys Gly Thr Val
             95                 100                 105CGT ACA AAA TAT GGC ACA AGG AGT CAG TTG CAA GGT GCC GTG ACA TCT      510Arg Thr Lys Tyr Gly Thr Arg Ser Gln Leu Gln Gly Ala Val Thr Ser
        110                 115                 120TTG AAA AAT AAC GGG ATT CAA GTT TAT GGG GAT GTC GTG ATG AAT CAT      558Leu Lys Asn Asn Gly Ile Gln Val Tyr Gly Asp Val Val Met Asn His
    125                 130                 135AAA GGT GGA GCA GAC GGG ACA GAG ATG GTA AAT GCG GTG GAA GTG AAC      606Lys Gly Gly Ala Asp Gly Thr Glu Met Val Asn Ala Val Glu Val Asn
140                 145                 150CGA AGC AAC CGA AAC CAA GAA ATA TCA GGT GAA TAC ACC ATT GAA GCA      654Arg Ser Asn Arg Asn Gln Glu Ile Ser Gly Glu Tyr Thr Ile Glu Ala155                 160                 165                 170TGG ACG AAA TTT GAT TTC CCT GGA AGA GGA AAT ACC CAT TCC AAC TTT      702Trp Thr Lys Phe Asp Phe Pro Gly Arg Gly Asn Thr His Ser Asn Phe
            175                 180                 185AAA TGG CGC TGG TAT CAT TTT GAT GGG ACA GAT TGG GAT CAG TCA CGT      750Lys Trp Arg Trp Tyr His Phe Asp Gly Thr Asp Trp Asp Gln Ser Arg
        190                 195                 200CAG CTT CAG AAC AAA ATA TAT AAA TTC AGA GGT ACC GGA AAG GCA TGG      798Gln Leu Gln Asn Lys Ile Tyr Lys Phe Arg Gly Thr Gly Lys Ala Trp
    205                 210                 215GAC TGG GAA GTA GAT ATA GAG AAC GGC AAC TAT GAT TAC CTT ATG TAT      846Asp Trp Glu Val Asp Ile Glu Asn Gly Asn Tyr Asp Tyr Leu Met Tyr
220                 225                 230GCA GAC ATT GAT ATG GAT CAT CCA GAA GTA ATC AAT GAA CTT AGA AAT      894Ala Asp Ile Asp Met Asp His Pro Glu Val Ile Asn Glu Leu Arg Asn235                 240                 245                 250TGG GGA GTT TGG TAT ACA AAT ACA CTT AAT CTA GAT GGA TTT AGA ATC      942Trp Gly Val Trp Tyr Thr Asn Thr Leu Asn Leu Asp Gly Phe Arg Ile
            255                 260                 265GAT GCT GTG AAA CAT ATT AAA TAC AGC TAT ACG AGA GAT TGG CTA ACA      990Asp Ala Val Lys His Ile Lys Tyr Ser Tyr Thr Arg Asp Trp Leu Thr
        270                 275                 280CAT GTG CGT AAC ACC ACA GGT AAA CCA ATG TTT GCA GTT GCA GAA TTT     1038His Val Arg Asn Thr Thr Gly Lys Pro Met Phe Ala Val Ala Glu Phe
    285                 290                 295TGG AAA AAT GAC CTT GCT GCA ATC GAA AAC TAT TTA AAT AAA ACA AGT     1086Trp Lys Asn Asp Leu Ala Ala Ile Glu Asn Tyr Leu Asn Lys Thr Ser
300                 305                 310TGG AAT CAC TCC GTG TTC GAT GTT CCT CTT CAT TAT AAT TTG TAC AAT     1134Trp Asn His Ser Val Phe Asp Val Pro Leu His Tyr Asn Leu Tyr Asn315                 320                 325                 330GCA TCT AAT AGT GGT GGC TAT TTT GAT ATG AGA AAT ATT TTA AAT GGT     1182Ala Ser Asn Ser Gly Gly Tyr Phe Asp Met Arg Asn Ile Leu Asn Gly
            335                 340                 345TCT GTC GTA CAA AAA CAC CCT ATA CAT GCA GTC ACA TTT GTT GAT AAC     1230Ser Val Val Gln Lys His Pro Ile His Ala Val Thr Phe Val Asp Asn
        350                 355                 360CAT GAC TCT CAG CCA GGA GAA GCA TTG GAA TCC TTT GTT CAA TCG TGG     1278His Asp Ser Gln Pro Gly Glu Ala Leu Glu Ser Phe Val Gln Ser Trp
    365                 370                 375TTC AAA CCA CTG GCA TAT GCA TTG ATT CTG ACA AGG GAG CAA GGT TAC     1326Phe Lys Pro Leu Ala Tyr Ala Leu Ile Leu Thr Arg Glu Gln Gly Tyr
380                 385                 390CCT TCC GTA TTT TAC GGT GAT TAC TAC GGT ATA CCA ACT CAT GGT GTT     1374Pro Ser Val Phe Tyr Gly Asp Tyr Tyr Gly Ile Pro Thr His Gly Val395                 400                 405                 410CCT TCG ATG AAA TCT AAA ATT GAT CCA CTT CTG CAG GCA CGT CAA ACG     1422Pro Ser Met Lys Ser Lys Ile Asp Pro Leu Leu Gln Ala Arg Gln Thr
            415                 420                 425TAT GCC TAC GGA ACC CAA CAT GAT TAT TTT GAT CAT CAT GAT ATT ATC    1470Tyr Ala Tyr Gly Thr Gln His Asp Tyr Phe Asp His His Asp Ile Ile
        430                 435                 440GGC TGG ACG AGA GAA GGG GAC AGC TCC CAC CCA AAT TCA GGA CTT GCA    1518Gly Trp Thr Arg Glu Gly Asp Ser Ser His Pro Asn Ser Gly Leu Ala
    445                 450                 455ACT ATT ATG TCC GAT GGG CCA GGG GGT AAT AAA TGG ATG TAT GTC GGG    1566Thr Ile Met Ser Asp Gly Pro Gly Gly Asn Lys Trp Met Tyr Val Gly
460                 465                 470AAA CAT AAA GCT GGC CAA GTA TGG AGA GAT ATC ACC GGA AAT AGG TCT    1614Lys His Lys Ala Gly Gln Val Trp Arg Asp Ile Thr Gly Asn Arg Ser475                 480                 485                 490GGT ACC GTC ACC ATT AAT GCA GAT GGT TGG GGG AAT TTC ACT GTA AAC    1662Gly Thr Val Thr Ile Asn Ala Asp Gly Trp Gly Asn Phe Thr Val Asn
            495                 5005                505GGA GGG GCA GTT TCG GTT TGG GTG AAG CAA TAAATAAGGA ACAAGAGGCG      1712Gly Gly Ala Val Ser Val Trp Val Lys Gln
        510                 515AAAATTACTT TCCTACATGC AGAGCTTTCC GATCACTCAT ACACCCAATA TAAATTGGAA  1772GCTT                                                               1776

Claims (12)

1.一种编码碱性液化α-淀粉酶活性的DNA分子,它编码在序列号1中所描述的氨基酸序列。
2.权利要求1的DNA分子,其中进一步包括一个调节基因表达的核苷酸序列。
3.一种DNA分子,它编码一种表现碱性液化α-淀粉酶活性的蛋白质并具有一个在序列号1中所描述的其中一个或多个氨基酸被置换、增加、缺失、倒位或插入的氨基酸序列。
4.权利要求3的DNA分子,其中进一步包括一个调节基因表达的核苷酸序列。
5.一种重组载体,它含有权利要求1或3的DNA分子。
6.权利要求5的重组载体,其中进一步包括一个调节基因表达的核苷酸序列。
7.一种含有权利要求5的重组载体的转化的微生物。
8.权利要求7的微生物,其中所述DNA分子进一步包括一个调节基因表达的核苷酸序列。
9.一种用于生产碱性液化α-淀粉酶的方法,包括培养权利要求7的转化的微生物和分离由该微生物产生的碱性液化α-淀粉酶。
10.权利要求9的方法,其中所述DNA分子进一步包括一个调节基因表达的核苷酸序列。
11.重组DNA质粒pAML100。
12.包含pAML100的重组大肠杆菌菌株HB101。
CN96194754A 1995-06-14 1996-06-14 编码碱性液化α-淀粉酶的基因 Expired - Fee Related CN1128221C (zh)

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