Affinity chromatography of α-amylase from Bacillus licheniformis

Damodara Rao Mendu; B. V.V. Ratnam; A. Purnima; C. Ayyanna

doi:10.1016/j.enzmictec.2005.04.015

Affinity chromatography of α-amylase from Bacillus licheniformis

Damodara Rao Mendu, B. V.V. Ratnam, A. Purnima, C. Ayyanna

Research output: Contribution to journal › Article › peer-review

26 Scopus citations

Abstract

An affinity chromatographic method with a novel eluant from Bacillus licheniformis is described. α-amylase was bound to starch, starch-celite, starch-Sepharose columns and the bound α-amylase was rapidly eluted with 2% (w/v) white dextrin. The binding capacity of α-amylase to starch column is 380 μmol/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.

Original language	English (US)
Pages (from-to)	712-717
Number of pages	6
Journal	Enzyme and Microbial Technology
Volume	37
Issue number	7
DOIs	https://doi.org/10.1016/j.enzmictec.2005.04.015
State	Published - Dec 1 2005
Externally published	Yes

Keywords

Affinity chromatography
Bacillus licheniformis
Immunological characterization
α-Amylase

ASJC Scopus subject areas

Biotechnology
Bioengineering
Biochemistry
Applied Microbiology and Biotechnology

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10.1016/j.enzmictec.2005.04.015

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title = "Affinity chromatography of α-amylase from Bacillus licheniformis",

abstract = "An affinity chromatographic method with a novel eluant from Bacillus licheniformis is described. α-amylase was bound to starch, starch-celite, starch-Sepharose columns and the bound α-amylase was rapidly eluted with 2% (w/v) white dextrin. The binding capacity of α-amylase to starch column is 380 μmol/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.",

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T1 - Affinity chromatography of α-amylase from Bacillus licheniformis

AU - Mendu, Damodara Rao

AU - Ratnam, B. V.V.

AU - Purnima, A.

AU - Ayyanna, C.

PY - 2005/12/1

Y1 - 2005/12/1

N2 - An affinity chromatographic method with a novel eluant from Bacillus licheniformis is described. α-amylase was bound to starch, starch-celite, starch-Sepharose columns and the bound α-amylase was rapidly eluted with 2% (w/v) white dextrin. The binding capacity of α-amylase to starch column is 380 μmol/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.

AB - An affinity chromatographic method with a novel eluant from Bacillus licheniformis is described. α-amylase was bound to starch, starch-celite, starch-Sepharose columns and the bound α-amylase was rapidly eluted with 2% (w/v) white dextrin. The binding capacity of α-amylase to starch column is 380 μmol/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.

KW - Affinity chromatography

KW - Bacillus licheniformis

KW - Immunological characterization

KW - α-Amylase

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DO - 10.1016/j.enzmictec.2005.04.015

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JO - Enzyme and Microbial Technology

JF - Enzyme and Microbial Technology

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ER -

Affinity chromatography of α-amylase from Bacillus licheniformis

Abstract

Keywords

ASJC Scopus subject areas

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