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Purification and characterization of ββ‐glucosidase from Aspergillus niger strain 322
Author(s) -
Peshin A.,
Mathur J. M. S.
Publication year - 1999
Publication title -
letters in applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.698
H-Index - 110
eISSN - 1472-765X
pISSN - 0266-8254
DOI - 10.1046/j.1365-2672.1999.00533.x
Subject(s) - cellobiose , aspergillus niger , enzyme , strain (injury) , molecular mass , enzyme assay , chemistry , divalent , gel electrophoresis , extracellular , biochemistry , chromatography , biology , cellulase , organic chemistry , anatomy
An extracellular β‐glucosidase enzyme was purified from the fungus Aspergillus niger strain 322 . The molecular mass of the enzyme was estimated to be 64 kDa by SDS gel electrophoresis. Optimal pH and temperature for β‐glucosidase were 5·5 and 50 °C, respectively. Purified enzyme was stable up to 50 °C and pH between 2·0 and 5·5. The K m was 0·1 mmol l −1 for cellobiose. Enzyme activity was inhibited by several divalent metal ions.