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Cell-associated acid β-xylosidase production by Penicillium sclerotiorum

Paper ID Volume ID Publish Year Pages File Format Full-Text
33905 44997 2009 8 PDF Available
Title
Cell-associated acid β-xylosidase production by Penicillium sclerotiorum
Abstract

In recent decades, β-xylosidases have been used in many processing industries. In this work, the study of xylosidase production by Penicillium sclerotiorum and its characterization are reported. Optimal production was obtained in medium supplemented with oat spelts xylan, pH 5.0, at 30 °C, under stationary condition for six days. The optimum activity temperature was 60 °C and unusual optimum pH 2.5. The enzyme was stable at 50 and 55 °C, with half-life of 240 and 232 min, respectively. High pH stability was verified from pH 2.0 to 4.0 and 7.5. The β-xylosidase was strongly inhibited by divalent cations, sensitive to denaturing agents SDS, EDTA and activated by thiol-containing reducing agents. The apparent Vmax and Km values was 0.48 μmol PNXP min−1 mg−1 protein and 0.75 mM, respectively. The enzyme was xylose tolerant with a Ki of 28.7. This enzyme presented interesting characteristics for biotechnological process such as animal feed, juice and wine industries.

Keywords
Biochemical properties; Enzyme characterization; Enzyme production; Penicillium sclerotiorum; β-Xylosidase
First Page Preview
Cell-associated acid β-xylosidase production by Penicillium sclerotiorum
Publisher
Database: Elsevier - ScienceDirect
Journal: New Biotechnology - Volume 26, Issues 1–2, 1 October 2009, Pages 60–67
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering