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球形芽孢杆菌环糊精酶基因的克隆、序列分析及其在大肠杆菌中的表达

Cloning and sequence analysis of the cyclomaltodextrinase gene from Bacillus sphaericus and expression in Escherichia coli cells.

作者信息

Oguma T, Matsuyama A, Kikuchi M, Nakano E

机构信息

Noda Institute for Scientific Research, Chiba Pref., Japan.

出版信息

Appl Microbiol Biotechnol. 1993 May;39(2):197-203. doi: 10.1007/BF00228606.

DOI:10.1007/BF00228606
PMID:7763728
Abstract

The gene for cyclomaltodextrinase (CDase; EC 3.2.1.54) from Bacillus sphaericus E-244 was cloned in the recombinant plasmid pCD629. Sequencing a portion of pCD629 revealed a unique open reading frame of 1,773 nucleotides coding for a 591-amino-acid polypeptide. The deduced polypeptide sequence showed about 50% homology with that of a neopullulanase, and was slightly homologous to those of the cyclodextrin glucanotransferases and the alpha-amylases. The optimum pH, specific activity and Km value for beta-cyclodextrin of the CDase that has been produced in Escherichia coli cells were 8.0, 16.4 units/mg protein, and 0.41 mM, respectively. These values were almost identical to those from B. sphaericus E-244.

摘要

来自球形芽孢杆菌E - 244的环麦芽糊精酶（CDase；EC 3.2.1.54）基因被克隆到重组质粒pCD629中。对pCD629的一部分进行测序，发现了一个1773个核苷酸的独特开放阅读框，编码一个591个氨基酸的多肽。推导的多肽序列与新普鲁兰酶的序列显示出约50%的同源性，并且与环糊精葡糖基转移酶和α -淀粉酶的序列有轻微同源性。在大肠杆菌细胞中产生的CDase的最适pH、比活性和β -环糊精的Km值分别为8.0、16.4单位/毫克蛋白质和0.41 mM。这些值与来自球形芽孢杆菌E - 244的值几乎相同。

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