Bacillus agaradhaerens LS-3C cyclodextrin glycosyltransferase: activity and stability features.
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/129221
- author
- Martins, Rita LU and Hatti-Kaul, Rajni LU
- organization
- publishing date
- 2003
- 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
- 10.1016/S0141-0229(03)00215-1
- language
- English
- LU publication?
- yes
- id
- 434e9782-8925-45d0-a922-c267635fee00 (old id 129221)
- date added to LUP
- 2016-04-01 11:48:19
- date last changed
- 2022-01-26 18:30:11
@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}},
keywords = {{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/10.1016/S0141-0229(03)00215-1}},
doi = {{10.1016/S0141-0229(03)00215-1}},
volume = {{33}},
year = {{2003}},
}