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|Title:||Properties of β-glucosidase purified from Aspergillus niger mutants USDB 0827 and USDB 0828||Authors:||Hoh, Y.K.
|Issue Date:||Aug-1992||Citation:||Hoh, Y.K.,Yeoh, H.-H.,Tan, T.K. (1992-08). Properties of β-glucosidase purified from Aspergillus niger mutants USDB 0827 and USDB 0828. Applied Microbiology and Biotechnology 37 (5) : 590-593. ScholarBank@NUS Repository. https://doi.org/10.1007/BF00240731||Abstract:||Two extracellular β-glucosidases (EC 188.8.131.52) were isolated from Aspergillus niger USDB 0827 and A. niger USDB 0828, and their physical and kinetic properties studied. Both enzymes were very similar in terms of molecular size (230000 Da), pH optimum (pH 4.6), temperature optimum (65° C), stability at high temperatures and substrate preferences. They were capable of hydrolysing β-linked disaccharides, phenyl β-d-glucoside, p-nitrophenyl β-d-glucoside (PNPG), o-nitrophenyl β-d-glucoside, salicin and methyl β-d-glucoside but lacked activity towards α-linked disaccharides, a range of p-nitrophenyl monoglycosides and p-nitrophenyl diglycosides. Both β-glucosidases were better at hydrolysing cellobiose than cellotriose, cellotetraose or cellopentaose. For both enzymes, glucose showed competitive inhibition with PNPG as substrate but had no effect with cellobiose. However, the two β-glucosidases differed in inhibition by glucono-1,5-lactone and affinity for cellobiose. β-Glucosidase from A. niger USDB 0827 also gave lower specific activity, and was more susceptible to metal ions (Ag+, Fe2+ and Fe3+) inhibition than that of A. niger USDB 0828. © 1992 Springer-Verlag.||Source Title:||Applied Microbiology and Biotechnology||URI:||http://scholarbank.nus.edu.sg/handle/10635/99726||ISSN:||01757598||DOI:||10.1007/BF00240731|
|Appears in Collections:||Staff Publications|
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