Tannin-Resistant α-Amylase from Calvatia Gigantea

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dc.contributor.author Komninos, J en
dc.contributor.author Kekos, D en
dc.contributor.author Macris, BJ en
dc.contributor.author Galiotou-Panayotou, M en
dc.date.accessioned 2014-03-01T01:07:17Z
dc.date.available 2014-03-01T01:07:17Z
dc.date.issued 1988 en
dc.identifier.issn 0006-3592 en
dc.identifier.uri http://hdl.handle.net/123456789/9902
dc.subject.classification Biotechnology & Applied Microbiology en
dc.subject.other Amylase en
dc.subject.other Enzyme Activity en
dc.subject.other Tannins en
dc.subject.other Enzymes en
dc.subject.other Calvatia gigantea en
dc.subject.other Ceratonia siliqua en
dc.title Tannin-Resistant α-Amylase from Calvatia Gigantea en
heal.type journalArticle en
heal.identifier.primary 10.1002/bit.260320717 en
heal.identifier.secondary http://dx.doi.org/10.1002/bit.260320717 en
heal.language English en
heal.publicationDate 1988 en
heal.abstract Highly inhibitory concentrations of acorn and carob tannins and catechin and tannic acid exhibited a small inhibition on α-amylase excreted from C. gigantea. The kinetics of inhibition of amylolytic activity of the enzyme by the tested phenolic inhibitors indicated a noncompetitive type of inhibition. α-amylase excreted from C. gigantea exhibited a high resistance to the inhibitory action of certain toxic phenolic compounds. en
heal.publisher JOHN WILEY & SONS INC en
heal.journalName Biotechnology and Bioengineering en
dc.identifier.doi 10.1002/bit.260320717 en
dc.identifier.isi ISI:A1988P977800016 en
dc.identifier.volume 32 en
dc.identifier.issue 7 en
dc.identifier.spage 939 en
dc.identifier.epage 941 en

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