Properties of β-glucosidase purified from Aspergillus niger

Please use this identifier to cite or link to this item: https://doi.org/10.1007/BF00940168

Title:	Properties of β-glucosidase purified from Aspergillus niger
Authors:	Yeoh, H.H. Tan, T.K. Chua, S.L. Lim, G.
Issue Date:	Dec-1988
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. https://doi.org/10.1007/BF00940168
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.
Source Title:	MIRCEN Journal of Applied Microbiology and Biotechnology
URI:	http://scholarbank.nus.edu.sg/handle/10635/99725
ISSN:	02650762
DOI:	10.1007/BF00940168
Appears in Collections:	Staff Publications

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