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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1999-7-13
pubmed:abstractText
A novel raw starch degrading cyclomaltodextrin glucanotransferase (CGTase; E.C. 2.4.1.19), produced by Bacillus firmus, was purified to homogeneity by ultrafiltration, affinity and gel filtration chromatography. The molecular weight of the pure protein was estimated to be 78,000 and 82,000 Da, by SDS-PAGE and gel filtration, respectively. The pure enzyme had a pH optimum in the range 5.5-8.5. It was stable over the pH range 7-11 at 10 degrees C, and at pH 7.0 at 60 degrees C. The optimum temperature for enzyme activity was 65 degrees C. In the absence of substrate, the enzyme rapidly lost its activity above 30 degrees C. K(m) and kcat for the pure enzyme were 1.21 mg/ml and 145.17 microM/mg per minute respectively, with soluble starch as the substrate. For cyclodextrin production, tapioca starch was the best substrate used when gelatinized, while wheat starch was the best substrate used when raw. This CGTase could degrade raw wheat starch very efficiently; up to 50% conversion to cyclodextrins was obtained from 150 g/l starch without using any additives. The enzyme produced alpha-, beta- and gamma-cyclodextrins in the ratio of 0.2:9.2:0.6 and 0.2:8.6:1.2 from gelatinized tapioca starch and raw wheat starch with 150 g/l concentration respectively, after 18 h incubation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0175-7598
pubmed:author
pubmed:issnType
Print
pubmed:volume
51
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
504-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Purification and properties of a novel raw starch degrading cyclomaltodextrin glucanotransferase from Bacillus firmus.
pubmed:affiliation
Chemical Engineering Division, National Chemical Laboratory, Pune, India.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't