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Bacillus agaradhaerens LS-3C cyclodextrin glycosyltransferase: activity and stability features.

Martins, Rita LU and Hatti-Kaul, Rajni LU (2003) In Enzyme and Microbial Technology 33(6). p.819-827
Abstract
Activity and stability characteristics of an alkaline active cyclodextrin glycosyltransferase (CGTase) enzyme from the alkaliphilic Bacillus agaradhaerens LS-3C strain are reported. The enzyme displays unusually high amylolytic activity in relation to the cyclization activity. Disproportionation activity of the CGTase was optimal with maltose as the acceptor substrate. The product of cyclization reaction was predominantly -cyclodextrin (CD) along with -CD as a minor product, however, the CDs profile was influenced by the reaction conditions. At pH 10, -CD was replaced by -CD formation. Cyclization reaction and -CD formation were significantly promoted in the presence of CaCl2. The salt allowed the cyclization reaction to be performed at... (More)
Activity and stability characteristics of an alkaline active cyclodextrin glycosyltransferase (CGTase) enzyme from the alkaliphilic Bacillus agaradhaerens LS-3C strain are reported. The enzyme displays unusually high amylolytic activity in relation to the cyclization activity. Disproportionation activity of the CGTase was optimal with maltose as the acceptor substrate. The product of cyclization reaction was predominantly -cyclodextrin (CD) along with -CD as a minor product, however, the CDs profile was influenced by the reaction conditions. At pH 10, -CD was replaced by -CD formation. Cyclization reaction and -CD formation were significantly promoted in the presence of CaCl2. The salt allowed the cyclization reaction to be performed at higher temperature. Increase in CDs production was also seen in the presence of 1 M sorbitol and 10% (w/v) PEG 3000, respectively. The enzyme stability was greatly enhanced with sorbitol, while alcohols had a highly negative effect on enzyme stability and hence on CDs production. -CD and maltose brought about significant inhibition of the cyclization reaction. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Bacillus agaradhaerens, Cyclodextrin glycosyltransferase, Cyclodextrin production, Starch hydrolysis, Disproportionation, Stability, Product inhibition
in
Enzyme and Microbial Technology
volume
33
issue
6
pages
819 - 827
publisher
Elsevier
external identifiers
  • wos:000185696100008
  • scopus:0141745541
ISSN
0141-0229
DOI
language
English
LU publication?
yes
id
434e9782-8925-45d0-a922-c267635fee00 (old id 129221)
date added to LUP
2007-07-02 13:43:29
date last changed
2018-05-29 10:45:10
@article{434e9782-8925-45d0-a922-c267635fee00,
  abstract     = {Activity and stability characteristics of an alkaline active cyclodextrin glycosyltransferase (CGTase) enzyme from the alkaliphilic Bacillus agaradhaerens LS-3C strain are reported. The enzyme displays unusually high amylolytic activity in relation to the cyclization activity. Disproportionation activity of the CGTase was optimal with maltose as the acceptor substrate. The product of cyclization reaction was predominantly -cyclodextrin (CD) along with -CD as a minor product, however, the CDs profile was influenced by the reaction conditions. At pH 10, -CD was replaced by -CD formation. Cyclization reaction and -CD formation were significantly promoted in the presence of CaCl2. The salt allowed the cyclization reaction to be performed at higher temperature. Increase in CDs production was also seen in the presence of 1 M sorbitol and 10% (w/v) PEG 3000, respectively. The enzyme stability was greatly enhanced with sorbitol, while alcohols had a highly negative effect on enzyme stability and hence on CDs production. -CD and maltose brought about significant inhibition of the cyclization reaction.},
  author       = {Martins, Rita and Hatti-Kaul, Rajni},
  issn         = {0141-0229},
  keyword      = {Bacillus agaradhaerens,Cyclodextrin glycosyltransferase,Cyclodextrin production,Starch hydrolysis,Disproportionation,Stability,Product inhibition},
  language     = {eng},
  number       = {6},
  pages        = {819--827},
  publisher    = {Elsevier},
  series       = {Enzyme and Microbial Technology},
  title        = {Bacillus agaradhaerens LS-3C cyclodextrin glycosyltransferase: activity and stability features.},
  url          = {http://dx.doi.org/},
  volume       = {33},
  year         = {2003},
}