Affinity chromatography of α-amylase from Bacillus licheniformis

被引：20
|
作者：
Mendu, DR
Ratnam, BVV
Purnima, A
Ayyanna, C
机构：
[1] Johns Hopkins Univ, Sch Med, Dept Pediat, Div Infect Dis, Baltimore, MD 21093 USA
[2] Univ Calif San Diego, San Diego Supercomp Ctr, La Jolla, CA 92093 USA
[3] Andhra Univ, Ctr Biotechnol, Dept Chem Engn, Visakhapatnam 530003, Andhra Pradesh, India
来源：
ENZYME AND MICROBIAL TECHNOLOGY | 2005年 / 37卷 / 07期
关键词：
alpha-amylase; affinity chromatography; Bacillus licheniformis; immunological characterization;
D O I：
10.1016/j.enzmictec.2005.04.015
中图分类号：
Q81 [生物工程学（生物技术）]; Q93 [微生物学];
学科分类号：
071005 ; 0836 ; 090102 ; 100705 ;
摘要：
An affinity chromatographic method with a novel eluant from Bacillus licheniformis is described. alpha-amylase was bound to starch, starch-celite, starch-Sepharose columns and the bound alpha-amylase was rapidly eluted with 2% (w/v) white dextrin. The binding capacity of a-amylase to starch column is 380 mu mol/g of starch. The purified enzyme showed a single polypeptide on SDS-polyacrylamide gel electrophoresis with a molecular weight of 58 kD. The specificity of purified enzyme was confirmed by immunodiffusion, immunoelectrophoresis. Single radial immunodiffusion and western blotting studies analyzed the synthesis of enzyme at different time points. (c) 2005 Elsevier Inc. All rights reserved.
引用
收藏
页码：712 / 717
页数：6
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