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Purification and characterization of a thermostable endo-β-1,4-glucanase from a novel strain of Penicillium purpurogenum

Paper ID Volume ID Publish Year Pages File Format Full-Text
17630 42686 2010 6 PDF Available
Title
Purification and characterization of a thermostable endo-β-1,4-glucanase from a novel strain of Penicillium purpurogenum
Abstract

A novel endo-β-1,4-glucanase (EG)-producing strain was isolated and identified as Penicillium purpurogenum KJS506 based on its morphology and internal transcribed spacer (ITS) rDNA gene sequence. P. purpurogenum produced one of the highest levels of EG (5.6 U mg-protein−1) with rice straw and corn steep powder as carbon and nitrogen sources, respectively. The extracellular EG was purified to homogeneity by sequential chromatography of P. purpurogenum culture supernatants on a DEAE sepharose column, a gel filtration column, and then on a Mono Q column with fast protein liquid chromatography. The purified EG was a monomeric protein with a molecular weight of 37 kDa and showed broad substrate specificity with maximum activity towards lichenan. P. purpurogenum EG showed t1/2 value of 2 h at 70 °C and catalytic efficiency of 118 ml mg−1 s−1, one of the highest levels seen for EG-producing microorganisms. Although EGs have been reported elsewhere, the high catalytic efficiency and thermostability distinguish P. purpurogenum EG.

Keywords
Catalytic efficiency; Endo-β-1,4-glucanase; Penicillium purpurogenum; Thermostability
First Page Preview
Purification and characterization of a thermostable endo-β-1,4-glucanase from a novel strain of Penicillium purpurogenum
Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 46, Issues 3–4, 5 March 2010, Pages 206–211
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering