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https://doi.org/10.1007/BF00940168
DC Field | Value | |
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dc.title | Properties of β-glucosidase purified from Aspergillus niger | |
dc.contributor.author | Yeoh, H.H. | |
dc.contributor.author | Tan, T.K. | |
dc.contributor.author | Chua, S.L. | |
dc.contributor.author | Lim, G. | |
dc.date.accessioned | 2014-10-27T07:03:33Z | |
dc.date.available | 2014-10-27T07:03:33Z | |
dc.date.issued | 1988-12 | |
dc.identifier.citation | Yeoh, H.H.,Tan, T.K.,Chua, S.L.,Lim, G. (1988-12). Properties of β-glucosidase purified from Aspergillus niger. MIRCEN Journal of Applied Microbiology and Biotechnology 4 (4) : 425-430. ScholarBank@NUS Repository. <a href="https://doi.org/10.1007/BF00940168" target="_blank">https://doi.org/10.1007/BF00940168</a> | |
dc.identifier.issn | 02650762 | |
dc.identifier.uri | http://scholarbank.nus.edu.sg/handle/10635/99725 | |
dc.description.abstract | Extracellular β-glucosidase from Aspergillus niger USDB 0355 was purified 120-fold. It gave a single band on PAGE and had an Mr of 325 000. It was optimally active at 60°C and pH 4.6. It had Km values for p-nitrophenyl-β-glucoside and cellobiose of 0.82±0.10 mm and 1.33±0.20 mm, respectively. It was competitively inhibited by glucose and non-competitively (mixed) inhibited by glucono-δ-lactone. © 1988 Oxford University Press. | |
dc.description.uri | http://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1007/BF00940168 | |
dc.source | Scopus | |
dc.type | Article | |
dc.contributor.department | BOTANY | |
dc.description.doi | 10.1007/BF00940168 | |
dc.description.sourcetitle | MIRCEN Journal of Applied Microbiology and Biotechnology | |
dc.description.volume | 4 | |
dc.description.issue | 4 | |
dc.description.page | 425-430 | |
dc.identifier.isiut | NOT_IN_WOS | |
Appears in Collections: | Staff Publications |
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