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Factors affecting the specificity of beta-glucosidase from Fusarium oxysporum in enzymatic synthesis of alkyl-beta-D-glucosides

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dc.contributor.author Makropoulou, M en
dc.contributor.author Christakopoulos, P en
dc.contributor.author Tsitsimpikou, C en
dc.contributor.author Kekos, D en
dc.contributor.author Kolisis, FN en
dc.contributor.author Macris, BJ en
dc.date.accessioned 2014-03-01T01:47:35Z
dc.date.available 2014-03-01T01:47:35Z
dc.date.issued 1998 en
dc.identifier.issn 0141-8130 en
dc.identifier.uri https://dspace.lib.ntua.gr/xmlui/handle/123456789/25266
dc.subject beta-glucosidase en
dc.subject transglucosylation en
dc.subject Fusarium oxysporum en
dc.subject.classification Biochemistry & Molecular Biology en
dc.subject.other HYDROLYSIS REACTION en
dc.subject.other REVERSE HYDROLYSIS en
dc.subject.other PURIFICATION en
dc.subject.other ENDO-1,4-BETA-D-GLUCANASE en
dc.title Factors affecting the specificity of beta-glucosidase from Fusarium oxysporum in enzymatic synthesis of alkyl-beta-D-glucosides en
heal.type journalArticle en
heal.language English en
heal.publicationDate 1998 en
heal.abstract Fusarium oxysporum beta-glucosidase has been used to catalyze the production of alkyl-beta-D-glucosides from various disaccharides, based on the transglucosylation reaction, in the presence of primary, secondary and tertiary alcohols as glucosyl accepters. Primary alcohols were found to be the best accepters. The influence of the glucosyl donor concentration, as well as the enzyme specificity towards the cleaved glucosidic bond and the aglucone part of the donor, have also been investigated. The enzyme does not exhibit regiospecificity and seems to be unspecific towards the aglucone part. The specificity of the beta linkage has been confirmed by proton nuclear magnetic resonance (H-1 NMR) analysis. (C) 1998 Elsevier Science B.V. All rights reserved. en
heal.publisher ELSEVIER SCIENCE BV en
heal.journalName INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES en
dc.identifier.isi ISI:000073332900004 en
dc.identifier.volume 22 en
dc.identifier.issue 2 en
dc.identifier.spage 97 en
dc.identifier.epage 101 en


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