doi:10.1016/j.procbio.2011.04.006

Paper Title

Properties of a major β-glucosidase-BGL1 from Aspergillus niger NII-08121 expressed differentially in response to carbon sources

Authors

Ashok Pandey

Reeta Rani Singhania

Rajeev Kumar Sukumaran

Keywords

β-Glucosidase
Aspergillus niger
BGL1
Enzyme Expression
Carbon Source Regulation
Submerged Fermentation
Isoforms of β-Glucosidase
Methyl Umbelliferyl β-D-Glucopyranoside (MUG) Assay
Lactose Induction
Cellulose Degradation
Wheat Bran
Rice Straw
Enzyme Purification
Native PAGE
Glucose Tolerance
Thermal Stability
Optimal pH 4.8
Optimal Temperature 70°C
Protein Characterization
Lignocellulosic Biomass Hydrolysis
Bioprocess Optimization
Renewable Biofuels
Biotechnological Applications
Enzyme Stability
Industrial Enzymes
Bioconversion
Fungal Enzymes

Article Type

Research Article

Journal

Process Biochemistry

Research Impact Tools

DOI

10.1016/j.procbio.2011.04.006

Issue

Volume : 46 | Issue : 7 | Page No : 1521-1524

Published On

July, 2011

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Abstract

Aspergillus niger NII-08121/MTCC 7956 exhibited differences in expression of β-glucosidase (BGL) in response to carbon sources provided in the medium. Activity staining with methyl umbelliferyl β-d-glucopyranoside (MUG) indicated that four different isoforms of BGL were expressed when A. niger was grown under submerged fermentation with either lactose or cellulose, whereas only two were expressed when wheat bran or rice straw was used as the carbon source. Among the four isoforms of BGL expressed during lactose supplementation, two were found to retain 92% and 82% activity respectively in presence of 250 mM glucose in the MUG assay. The major β-glucosidase (BGL1) was purified to homogeneity by electro elution from a Native PAGE gel. The purified 120 kDa protein was active at 50 °C and was stable for 48 h without any loss of activity. The optimum pH and temperature were 4.8 and 70 °C respectively.