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dc.contributor.authorLi, YKen_US
dc.contributor.authorChang, LFen_US
dc.contributor.authorShu, HHen_US
dc.contributor.authorChir, Jen_US
dc.date.accessioned2014-12-08T15:02:03Z-
dc.date.available2014-12-08T15:02:03Z-
dc.date.issued1997-02-01en_US
dc.identifier.issn0009-4536en_US
dc.identifier.urihttp://hdl.handle.net/11536/761-
dc.description.abstractA sweet almond beta-glucosidase (EC 3.2.1.21) isozyme was purified from commercial crude product. The process of purification consisted of a Protein-Pak Q anion exchange chromatography following by a Superdex 75 HR gel filtration separation. The purified enzyme is a monomeric glycoprotein with molecular weight of 58 kDa and pI = 4.55 which is distinguished from reported isozymes. The enzyme has a pH optimum in the range of 5.2-5.6 when p-nitrophenyl-beta-D-glycopyranosides are used as substrate and is stable up to 50 degrees C at that pH range. The purified protein also exhibits profound beta-galactosidase and alpha-L-arabinosidase activity. The study of substrate specificity revealed that lacking of hydroxymethyl group at C-5 of glycosides resulted in higher affinity for substrate binding to enzyme, whereas the chemical step of hydrolysis (k(cat)) was prevented significantly. The pH activity profile displayed a bell-shaped curve for all measured p-nitrophenyl-beta-D-glycopyranosides with apparent pK(1) and pK(2) values of 4.4-4.7 and 6.2-6.4, respectively. This isozyme was strongly inhibited by delta-gluconolactone (K-i = 160 mu M) and 4-phenylimidazole (K-i = 17.8 mu M) reversibly at pH 6.2. Among the tested glycoses, the binding affinity of N-acetyl-beta-D-glucosamine to the enzyme (K-i = 52 mM) was 6 times stronger than that of glucose and its epimers.en_US
dc.language.isoen_USen_US
dc.subjectsweet almond beta-glucosidaseen_US
dc.subjectbeta-galactosidaseen_US
dc.subjectbeta-D-glycopyranosidesen_US
dc.subjectisozymeen_US
dc.subjectsubstrate specificityen_US
dc.titleCharacterization of an isozyme of beta-glucosidase from sweet almonden_US
dc.typeArticleen_US
dc.identifier.journalJOURNAL OF THE CHINESE CHEMICAL SOCIETYen_US
dc.citation.volume44en_US
dc.citation.issue1en_US
dc.citation.spage81en_US
dc.citation.epage87en_US
dc.contributor.department交大名義發表zh_TW
dc.contributor.department應用化學系zh_TW
dc.contributor.departmentNational Chiao Tung Universityen_US
dc.contributor.departmentDepartment of Applied Chemistryen_US
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