Purification and characterization of β-amylase from Bacillus polymyxa No. 26-1

Cited 12 time in scopus
Metadata Downloads
Title
Purification and characterization of β-amylase from Bacillus polymyxa No. 26-1
Author(s)
C B Sohn; S M lee; M H Kim; Jung Hun Koh; K S Kim; J E Chang; Y K Ahn; C H Kim
Bibliographic Citation
Journal of Food Science, vol. 61, no. 1, pp. 230-234
Publication Year
1996
Abstract
An extracellular β-amylase, which was easily adsorbable onto raw corn starch, was purified 22.5-fold from a new isolate of Bacillus polymyxa No 26-1 with a Mr of 53 kDa and pI of 9.1. The optimum temperature was 45°C and pH 5.5 for raw corn starch. Thermal stability at 40°C and pH stability at 5.0-8.5 were shown. The degradation ofraw starch by β-amylase was greatly stimulated by pullulanase addition. Scanning electron micrographs revealed that starch granule degradation by the enzyme alone occured at the equatorial grooves of lecticular granules. Corn starch granules hydrolyzed by β-amylase had large holes on granule surfaces.
Keyword
β-amylaseRaw starch saccharifying enzymeBacillus polymyxa No. 26-1
ISSN
0022-1147
Publisher
Wiley
DOI
http://dx.doi.org/10.1111/j.1365-2621.1996.tb14767.x
Type
Article
Appears in Collections:
Synthetic Biology and Bioengineering Research Institute > Genome Editing Research Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.