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Purification and characterization of ββ‐glucosidase fromAspergillus nigerstrain 322

Archana Peshin, J. M. S. Mathur

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Abstract

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 Km was 0·1 mmol l−1 for cellobiose. Enzyme activity was inhibited by several divalent metal ions.

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What this paper is about

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 Km was 0·1 mmol l−1 for cellobiose. Enzyme activity was inhibited by several divalent metal ions.

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Available abstract

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 Km was 0·1 mmol l−1 for cellobiose. Enzyme activity was inhibited by several divalent metal ions.

Key concepts: Cellobiose, Aspergillus niger, Enzyme, Strain (injury), Molecular mass, Enzyme assay, Chemistry, Divalent

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