HEAL DSpace

Tannin-Resistant α-Amylase from Calvatia Gigantea

DSpace/Manakin Repository

Show simple item record

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


Files in this item

Files Size Format View

There are no files associated with this item.

This item appears in the following Collection(s)

Show simple item record