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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
1993-7-21
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pubmed:abstractText |
Trichoderma reesei RUT C-30 formed an extracellular alpha-galactosidase when it was grown in a batch culture containing lactose or locust bean gum as a carbon source. Short-chain alpha-galactosides (melibiose, raffinose, stachyose), as well as the monosaccharides galactose, dulcitol, arabinose, and arabitol, also induced alpha-galactosidase activity both when they were used as carbon sources (at a concentration of 1%) in batch cultures and in resting mycelia (at concentrations in the millimolar range). The addition of 50 mM glucose did not affect the induction of alpha-galactosidase formation by galactose. alpha-Galactosidase from T. reesei RUT C-30 was purified to homogeneity from culture fluids of galactose-induced mycelia. The active enzyme was a 50 +/- 3-kDa, nonglycosylated monomer which had an isoelectric point of 5.2. It was active against several alpha-galactosides (p-nitrophenyl-alpha-D-galactoside, melibiose, raffinose, and stachyose) and galactomannan (locust bean gum) and was inhibited by the product galactose. It released galactose from locust bean gum and exhibited synergism with T. reesei beta-mannanase. Its activity was optimal at pH 4, and it displayed broad pH stability (pH 4 to 8). Its temperature stability was moderate (60 min at 50 degrees C resulted in recovery of 70% of activity), and its highest level of activity occurred at 60 degrees C. Its action on galactomannan was increased by the presence of beta-mannanase.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8390816-14323029,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8390816-2136347,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8390816-2287609,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8390816-39061,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8390816-4561015,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8390816-5418105,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8390816-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8390816-5772469,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8390816-6331399,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8390816-782186,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8390816-942051
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0099-2240
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
59
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1347-53
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:8390816-Enzyme Induction,
pubmed-meshheading:8390816-Enzyme Stability,
pubmed-meshheading:8390816-Hydrogen-Ion Concentration,
pubmed-meshheading:8390816-Isoelectric Point,
pubmed-meshheading:8390816-Molecular Weight,
pubmed-meshheading:8390816-Trichoderma,
pubmed-meshheading:8390816-alpha-Galactosidase
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pubmed:year |
1993
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pubmed:articleTitle |
Conditions of formation, purification, and characterization of an alpha-galactosidase of Trichoderma reesei RUT C-30.
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pubmed:affiliation |
Abteilung für Mikrobielle Biochemie, Technische Universität Wien, Austria.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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