Affordable Access

Domain E of Bacillus macerans cyclodextrin glucanotransferase: An independent starch-binding domain.

Authors
  • Dalmia, B K
  • Schütte, K
  • Nikolov, Z L
Type
Published Article
Journal
Biotechnology and bioengineering
Publication Date
Sep 05, 1995
Volume
47
Issue
5
Pages
575–584
Identifiers
PMID: 18623437
Source
Medline
License
Unknown

Abstract

The starch-binding domains of glucoamylase I (SBD of GA-I) from Aspergillus awamori and of cyclodextrin glucanotransferase (domain E of CGTase) from Bacillus macerans were fused to the C-terminus of beta-galactosidase (beta-gal) The majority of the fusion proteins produced in Escherichia coli were found as inclusion bodies. Active fusion proteins were purified by partial solubilization of the inclusion bodies with 2 M urea followed by affinity chromatography. Adsorption isotherms of purified fusion proteins on corn starch and cross-linked amylose were generated. The beta-gal fusion proteins had similar affinities for cross-linked amylose and corn starch but significantly different saturation capacities on corn starch. The adsorption and elution data from the potato starch column as well as the adsorption isotherms of p-gal-domain E fusion protein (BDE109) on corn starch and cross-linked amylose demonstrated that domain E of CGTase is an independent domain, which retained its starch-binding activity when separated from the other four (A-D) domains in CGTase. (c) 1995 John Wiley & Sons Inc.

Report this publication

Statistics

Seen <100 times