Biochemical characterization of the multi-enzyme system produced by Penicillium decumbens grown on rutin

Mamma, D; Kalogeris, E; Hatzinikolaou, DG; Lekanidou, A; Kekos, D; Macris, BJ; Christakopoulos, P

dc.contributor.author	Mamma, D	en
dc.contributor.author	Kalogeris, E	en
dc.contributor.author	Hatzinikolaou, DG	en
dc.contributor.author	Lekanidou, A	en
dc.contributor.author	Kekos, D	en
dc.contributor.author	Macris, BJ	en
dc.contributor.author	Christakopoulos, P	en
dc.date.accessioned	2014-03-01T01:19:58Z
dc.date.available	2014-03-01T01:19:58Z
dc.date.issued	2004	en
dc.identifier.issn	0890-5436	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/15784
dc.subject	β-Glucosidase	en
dc.subject	Flavonoids	en
dc.subject	Penicillium decumbens	en
dc.subject	Quercetin	en
dc.subject	Quercetinase	en
dc.subject	Rhamnosidase	en
dc.subject	Rutin degradation	en
dc.subject.classification	Biotechnology & Applied Microbiology	en
dc.subject.classification	Food Science & Technology	en
dc.subject.other	Ammonium compounds	en
dc.subject.other	Carbon	en
dc.subject.other	Electrophoretic coatings	en
dc.subject.other	Enzymes	en
dc.subject.other	Fungi	en
dc.subject.other	Glucose	en
dc.subject.other	Glycols	en
dc.subject.other	Negative ions	en
dc.subject.other	Nitrogen	en
dc.subject.other	pH	en
dc.subject.other	Aglycone	en
dc.subject.other	Ammonium hydrogen phosphate	en
dc.subject.other	Glucosidase	en
dc.subject.other	Glycosidases	en
dc.subject.other	Monooxygenase	en
dc.subject.other	Penicillium	en
dc.subject.other	Biotechnology	en
dc.subject.other	Fungi	en
dc.subject.other	Penicillium	en
dc.subject.other	Penicillium decumbens	en
dc.title	Biochemical characterization of the multi-enzyme system produced by Penicillium decumbens grown on rutin	en
heal.type	journalArticle	en
heal.identifier.primary	10.1081/FBT-120030382	en
heal.identifier.secondary	http://dx.doi.org/10.1081/FBT-120030382	en
heal.language	English	en
heal.publicationDate	2004	en
heal.abstract	Penicillium decumbens produced a set of enzymes, including a monoxygenase and two glycosidases, which degrade rutin, a nontoxic flavonoid glycoside, to water-soluble products. The monoxygenase (quercetinase) cleaves the heterocyclic ring in quercetin, the aglycone part of rutin. The glycosidases (alpha-L-rhamnosidase and beta-glucosidase) hydrolyze the bonds between quercetin and rutinose, and between glucose and rhamnose, the constituent monosaccharides of rutinose. Simultaneous production of the three enzymes was optimized following the examination of a number of culture conditions. Maximum enzyme activities were observed when the fungus was grown at 30degreesC with an initial pH of 7.0, using 8.0 g/L rutin and 9.0g/L di-ammonium hydrogen phosphate as carbon and nitrogen sources, respectively. The enzymes were purified to electrophoretic homogeneity by a series of consecutive chromatographic steps including anion and cation exchange as well as gel filtration. The purified quercetinase revealed an apparent tetrameric structure, with a reduced molecular mass of 45 kDa. alpha-L-Rhamnosidase showed an apparent molecular mass of 58 kDa and the purified beta-glucosidase was a tetramer exhibiting a reduced molecular mass of 120 kDa.	en
heal.publisher	MARCEL DEKKER INC	en
heal.journalName	Food Biotechnology	en
dc.identifier.doi	10.1081/FBT-120030382	en
dc.identifier.isi	ISI:000220795200001	en
dc.identifier.volume	18	en
dc.identifier.issue	1	en
dc.identifier.spage	1	en
dc.identifier.epage	18	en