Insoluble but enzymatically active α-amylase from Bacillus licheniformis

被引：8
|
作者：
Rashid, Naeem [1 ]
Farooq, Alia [1 ,2 ]
Ikram-ul-Haq [2 ]
Akhtar, Muhammad [1 ]
机构：
[1] Univ Punjab, Sch Biol Sci, Lahore 54590, Pakistan
[2] Govt Coll Univ, Inst Ind Biotechnol, Lahore 54000, Pakistan
来源：
BIOLOGIA | 2009年 / 64卷 / 04期
关键词：
Bacillus licheniformis; cloning; alpha-amylase; inclusion bodies; STARCH-BINDING DOMAIN; ESCHERICHIA-COLI; SIGNAL PEPTIDE; T7; PROMOTER; EXPRESSION; EVOLUTION; SECRETION; AMYLOLIQUEFACIENS; PURIFICATION; SUBTILIS;
D O I：
10.2478/s11756-009-0132-5
中图分类号：
Q [生物科学];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
The gene encoding thermostable alpha-amylase from Bacillus licheniformis consisting of 483 amino acid residues (mature protein) was cloned and expressed in Escherichia coli under the control of T7 promoter. The analysis of the soluble and insoluble fractions after lyzing the host cells revealed that recombinant alpha-amylase was produced in insoluble aggregates. Despite being produced in the insoluble aggregates the recombinant enzyme was highly active with a specific activity of 408 U/mg.
引用
收藏
页码：660 / 663
页数：4
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