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Production and characterization of β-1,4-glucosidase from a strain of Penicillium pinophilum

Paper ID Volume ID Publish Year Pages File Format Full-Text
35602 45098 2010 8 PDF Available
Title
Production and characterization of β-1,4-glucosidase from a strain of Penicillium pinophilum
Abstract

A high β-glucosidase (BGL)-producing strain was isolated and identified as Penicillium pinophilum KMJ601 based on its morphology and internal transcribed spacer rDNA gene sequence. Under the optimal culture conditions, a maximum BGL specific activity of 3.2 U ml−1 (83 U mg-protein−1), one of the highest levels among BGL-producing microorganisms was obtained. An extracellular BGL was purified to homogeneity by sequential chromatography of P. pinophilum culture supernatants on a DEAE-Sepharose column, a gel filtration column, and then on a Mono Q column. The relative molecular weight of P. pinophilum BGL was determined to be 120 kDa by SDS-PAGE and size exclusion chromatography, indicating that the enzyme is a monomer. The hydrolytic activity of the BGL had a pH optimum of 3.5 and a temperature optimum of 32 °C. P. pinophilum BGL showed a higher activity (Vmax = 1120 U mg-protein−1) than most BGLs purified from other sources. The internal amino acid sequences of P. pinophilum BGL showed a significant homology with hydrolases from glycoside hydrolase family 3. Although BGLs have been purified and characterized from several other sources, P. pinophilum BGL is distinguished from other BGLs by its high activity.

Keywords
Enzyme production; β-Glucosidase; Glycoside hydrolase family 3; Penicillium pinophilum
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Production and characterization of β-1,4-glucosidase from a strain of Penicillium pinophilum
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 45, Issue 6, June 2010, Pages 851–858
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
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Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
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Full-text PDF Download
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