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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
8
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pubmed:dateCreated |
1991-12-30
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pubmed:abstractText |
The production of pectinase was studied in Neurospora crassa, using the hyperproducer mutant exo-1, which synthesized and secreted five to six times more enzyme than the wild-type. Polygalacturonase, pectin lyase and pectate lyase were induced by pectin, and this induction was glucose-repressible. Polygalacturonase was induced by galactose four times more efficiently than by pectin; in contrast the activity of lyases was not affected by galactose. The inducing effect of galactose on polygalacturonase was not glucose-repressible. Extracellular pectinases were separated by ion exchange chromatography. Pectate and pectin lyases eluted into three main fractions containing both activities; polygalacturonase eluted as a single, symmetrical peak, apparently free of other protein contaminants, and was purified 56-fold. The purified polygalacturonase was a monomeric glycoprotein (38% carbohydrate content) of apparent molecular mass 36.6-37.0 kDa (Sephadex G-100 and urea-SDS-PAGE, respectively). The enzyme hydrolysed predominantly polypectate. Pectin was also hydrolysed, but at 7% of the rate for polypectate. Km and Vmax for polypectate hydrolysis were 5.0 mg ml-1 and 357 mumol min-1 (mg protein)-1, respectively. Temperature and pH optima were 45 degrees C and 6.0, respectively. The purified polygalacturonase reduced the viscosity of a sodium polypectate solution by 50% with an increase of 7% in reducing sugar groups. The products of hydrolysis at initial reaction times consisted of oligogalacturonates without detectable monomer. Thus, the purified Neurospora crassa enzyme was classified as an endopolygalacturonase [poly(1,4-alpha-D-galacturonide) glycanohydrolase; EC 3.2.1.15].
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Galactose,
http://linkedlifedata.com/resource/pubmed/chemical/Glucose,
http://linkedlifedata.com/resource/pubmed/chemical/Pectins,
http://linkedlifedata.com/resource/pubmed/chemical/Polygalacturonase,
http://linkedlifedata.com/resource/pubmed/chemical/Polysaccharide-Lyases,
http://linkedlifedata.com/resource/pubmed/chemical/pectate lyase,
http://linkedlifedata.com/resource/pubmed/chemical/pectin,
http://linkedlifedata.com/resource/pubmed/chemical/pectin lyase
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0022-1287
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
137
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1815-23
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1835496-Chromatography,
pubmed-meshheading:1835496-Enzyme Induction,
pubmed-meshheading:1835496-Galactose,
pubmed-meshheading:1835496-Gene Expression Regulation, Fungal,
pubmed-meshheading:1835496-Glucose,
pubmed-meshheading:1835496-Hydrogen-Ion Concentration,
pubmed-meshheading:1835496-Kinetics,
pubmed-meshheading:1835496-Neurospora crassa,
pubmed-meshheading:1835496-Pectins,
pubmed-meshheading:1835496-Polygalacturonase,
pubmed-meshheading:1835496-Polysaccharide-Lyases,
pubmed-meshheading:1835496-Temperature
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pubmed:year |
1991
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pubmed:articleTitle |
Pectinase production by Neurospora crassa: purification and biochemical characterization of extracellular polygalacturonase activity.
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pubmed:affiliation |
Departamento de Biologia, Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo, Brazil.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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