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Biochemical charact...
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Mamma, Diomi
(författare)
Biochemical characterization of the multi-enzyme system produced by Penicillium decumbens grown on rutin
- Artikel/kapitelEngelska2004
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Nummerbeteckningar
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LIBRIS-ID:oai:DiVA.org:ltu-3141
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https://urn.kb.se/resolve?urn=urn:nbn:se:ltu:diva-3141URI
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https://doi.org/10.1081/FBT-120030382DOI
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Språk:engelska
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Sammanfattning på:engelska
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Ämneskategori:ref swepub-contenttype
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Ämneskategori:art swepub-publicationtype
Anmärkningar
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Upprättat; 2004; 20130213 (ysko)
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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 30 °C with an initial pH of 7.0, using 8.0 g/L rutin and 9.0 g/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.
Biuppslag (personer, institutioner, konferenser, titlar ...)
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Kalogeris, Emmanuel
(författare)
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Hatzinikolaou, Dimitris G
(författare)
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Lekanidou, Afroditi
(författare)
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Kekos, Dimitris
(författare)
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Macris, Basil J
(författare)
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Christakopoulos, Paul
(författare)
Sammanhörande titlar
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Ingår i:Food biotechnology18:1, s. 1-180890-54361532-4249
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