Tannin-Resistant α-Amylase from Calvatia Gigantea

Komninos, J; Kekos, D; Macris, BJ; Galiotou-Panayotou, M

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	https://dspace.lib.ntua.gr/xmlui/handle/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