Linked Life Data

19049410

Source:http://linkedlifedata.com/resource/pubmed/id/19049410

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
2008-12-18
pubmed:abstractText
It was found that commercial cellulase preparations from Trichoderma viride showed transglucosylation activity toward (+)-catechin and (-)-epigallocatechin gallate (EGCG) using dextrin as a glucosyl donor. To isolate the enzyme exhibiting transglucosylation activity toward (+)-catechin and EGCG, the present study isolated the cDNA encoding the T. viride JCM22452 alpha-amylase homologue (TRa2), which showed high amino acid sequence identity to functionally uncharacterized alpha-amylase homologues from other ascomycetes, which also produced some (+)-catechin and EGCG glucosides. TRa2 was able to glucosylate a wide range of natural flavonoids, particularly (+)-catechin and EGCG, and to hydrolyze maltooligosaccharides (k(cat)/K(m) for maltotriose, maltotetraose, maltopentaose, maltohexaose, and maltoheptaose were 1.98, 45.2, 58.3, 97.4, and 92.6 s(-1) mM(-1), respectively) except maltose but could not transfer the monoglucosyl residue to maltooligosaccharides. By (1)H NMR and (13)C NMR, the structures of several novel glucosides obtained by commercial cellulase preparations from T. viride and TRa2 were determined as (+)-catechin 5-O-alpha-D-glucopyranoside, (+)-catechin 5-O-alpha-D-maltoside, (+)-catechin 4'-O-alpha-D-maltoside, EGCG 5-O-alpha-D-glucopyranoside, and EGCG 7-O-alpha-D-maltoside. One of these glucosides, EGCG 5-O-alpha-D-glucopyranoside, showed higher heat stability and solubility and lower astringency and astringent stimulation than its aglycon, suggesting that EGCG glucosides are functionally superior to EGCG as food additives.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1520-5118
pubmed:author
pubmed:issnType
Electronic
pubmed:day
24
pubmed:volume
56
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
12016-24
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
A novel glucosylation enzyme: molecular cloning, expression, and characterization of Trichoderma viride JCM22452 alpha-amylase and enzymatic synthesis of some flavonoid monoglucosides and oligoglucosides.
pubmed:affiliation
Institute for Advanced Core Technology, Suntory Ltd., 1-1-1 Wakayamadai, Shimamoto-cho, Mishima-gun, Osaka 618-8503, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't