Biochemical and catalytic properties of two intracellular β-glucosidases from the fungus Penicillium decumbens active on flavonoid glucosides

Mamma, D; Hatzinikolaou, DG; Christakopoulos, P

dc.contributor.author	Mamma, D	en
dc.contributor.author	Hatzinikolaou, DG	en
dc.contributor.author	Christakopoulos, P	en
dc.date.accessioned	2014-03-01T01:19:57Z
dc.date.available	2014-03-01T01:19:57Z
dc.date.issued	2004	en
dc.identifier.issn	1381-1177	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/15783
dc.subject	β-Glucosidases	en
dc.subject	Deglycosylation	en
dc.subject	Flavonoids glycosides	en
dc.subject	Kinetics	en
dc.subject	Penicillium decumbens	en
dc.subject	Purification	en
dc.subject.classification	Biochemistry & Molecular Biology	en
dc.subject.classification	Chemistry, Physical	en
dc.subject.other	Biochemistry	en
dc.subject.other	Catalysis	en
dc.subject.other	Hydrolysis	en
dc.subject.other	pH	en
dc.subject.other	Proteins	en
dc.subject.other	Substrates	en
dc.subject.other	Flavanols	en
dc.subject.other	Rutin	en
dc.subject.other	Glucose	en
dc.subject.other	beta glucosidase	en
dc.subject.other	flavonoid	en
dc.subject.other	glucose	en
dc.subject.other	glucoside	en
dc.subject.other	kaempferol	en
dc.subject.other	protein subunit	en
dc.subject.other	quercetin	en
dc.subject.other	rutoside	en
dc.subject.other	article	en
dc.subject.other	carbon source	en
dc.subject.other	catalysis	en
dc.subject.other	competitive inhibition	en
dc.subject.other	deglycosylation	en
dc.subject.other	enzyme activity	en
dc.subject.other	enzyme glycosylation	en
dc.subject.other	enzyme substrate	en
dc.subject.other	Penicillium	en
dc.subject.other	pH measurement	en
dc.subject.other	protein purification	en
dc.subject.other	temperature	en
dc.subject.other	Fungi	en
dc.subject.other	Penicillium	en
dc.subject.other	Penicillium decumbens	en
dc.title	Biochemical and catalytic properties of two intracellular β-glucosidases from the fungus Penicillium decumbens active on flavonoid glucosides	en
heal.type	journalArticle	en
heal.identifier.primary	10.1016/j.molcatb.2003.11.011	en
heal.identifier.secondary	http://dx.doi.org/10.1016/j.molcatb.2003.11.011	en
heal.language	English	en
heal.publicationDate	2004	en
heal.abstract	In the presence of rutin as sole carbon source, Penicillium decumbens produces two intracellular beta-glucosidases named G(I) and G(II), with molecular masses of 56,000 and 460,000 Da, respectively. The two proteins have been purified to homogeneity. G(I) and G(II) composed of two and four equal sub-units, respectively and displayed optimal activity at pH 7.0 and temperature 65-75 degreesC. Both beta-glucosidases were competitively inhibited by glucose and glucono-delta-lactone. G(I) and G(II) exhibited broad substrate specificity, since they hydrolyzed a range of (1,3)-, (1,4)- and (1,6)-beta-glucosides as well as aryl beta-glucosides. Determination of k(cat)/K-m revealed that G(II) hydrolyzed 3-8 times more efficiently the above-mentioned substrates. The ability of G(I) and G(II) to deglycosylate various flavonoid glycosides was also investigated. Both enzymes were active against flavonoids glycosylated at the 7 position but G(II) hydrolyzed them 5 times more efficiently than G(I). Of the flavanols tested, both enzymes were incapable of hydrolyzing quercetrin and kaempferol-3-glucoside. The main difference between G(I) and G(II) as far as the hydrolysis of flavanols is concerned, was the ability of G(II) to hydrolyze the quercetin-3-glucoside. (C) 2003 Elsevier B.V. All rights reserved.	en
heal.publisher	ELSEVIER SCIENCE BV	en
heal.journalName	Journal of Molecular Catalysis B: Enzymatic	en
dc.identifier.doi	10.1016/j.molcatb.2003.11.011	en
dc.identifier.isi	ISI:000220344900006	en
dc.identifier.volume	27	en
dc.identifier.issue	4-6	en
dc.identifier.spage	183	en
dc.identifier.epage	190	en