Please use this identifier to cite or link to this item: https://doi.org/10.1007/BF00386292
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dc.titleIsolation and characterization of β-glucosidases from Aspergillus nidulans mutant USDB 1183
dc.contributor.authorHoh, Y.K.
dc.contributor.authorYeoh, H.-H.
dc.contributor.authorTan, T.K.
dc.date.accessioned2014-10-27T07:03:16Z
dc.date.available2014-10-27T07:03:16Z
dc.date.issued1993-09
dc.identifier.citationHoh, Y.K., Yeoh, H.-H., Tan, T.K. (1993-09). Isolation and characterization of β-glucosidases from Aspergillus nidulans mutant USDB 1183. World Journal of Microbiology & Biotechnology 9 (5) : 555-558. ScholarBank@NUS Repository. https://doi.org/10.1007/BF00386292
dc.identifier.issn09593993
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/99697
dc.description.abstractTwo extracellular β-glucosidases (cellobiase, EC 3.2.1.21), I and II, from Aspergillus nidulans USDB 1183 were purified to homogeneity with molecular weights of 240,000 and 78,000, respectively. Both hydrolysed laminaribiose, β-gentiobiose, cellobiose, p-nitrophenyl-β-L-glucoside, phenyl-β-L-glucoside, o-nitrophenyl-β-L-glucoside, salicin and methyl-β-L-glucoside but not α-linked disaccharides. Both were competitively inhibited by glucose and non-competitively (mixed) inhibited by glucono-1,5-lactone. β-Glucosidase I was more susceptible to inhibition by Ag+ and less inhibited by Fe2+ and Fe3+ than β-glucosidase II. © 1993 Rapid Communications of Oxford Ltd.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1007/BF00386292
dc.sourceScopus
dc.subjectβ-glucosidase
dc.subjectAspergillus nidulans
dc.subjectcellobiase
dc.typeArticle
dc.contributor.departmentBOTANY
dc.description.doi10.1007/BF00386292
dc.description.sourcetitleWorld Journal of Microbiology & Biotechnology
dc.description.volume9
dc.description.issue5
dc.description.page555-558
dc.description.codenWJMBE
dc.identifier.isiutA1993LV77500012
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