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A new thermostable peroxidase from garlic Allium sativum

A new thermostable peroxidase from garlic Allium sativum Analysis of peroxidase activity by native polyacrylamide gel electrophoresis (PAGE) from a garlic bulb (Allium sativum L) extract showed two major activities (designated POX1 and POX2). The POX2 isoenzyme was purified to homogeneity by ammonium sulfate precipitation, gel filtration, and cation-exchange chromatography. The purified enzyme was found to be monomeric with a molecular mass of 36.5 kDa, as determined by sodium dodecyl sulfate-PAGE. The optimum temperature ranged from 25 to 40°C and optimum pH was about 5.0. The apparent K m values for guaiacol and H2O2 were 9.5 and 2 mM, respectively. POX2 appeared highly stable since 50% of its activity was conserved at 50°C for 5h. Moreover POX2 was stable over a pH range of 3.5–11.0. Immobilization of POX2 was achieved by covalent binding of the enzyme to an epoxy-Sepharose matrix. The immobilized enzyme showed great stability toward heat and storage when compared with soluble enzyme. These properties permit the use of this enzyme as a biosensor to detect H2O2 in some food components such as milk or its derivatives. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Applied Biochemistry and Biotechnology Springer Journals

A new thermostable peroxidase from garlic Allium sativum

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References (32)

Publisher
Springer Journals
Copyright
Copyright © 2005 by Humana Press Inc
Subject
Chemistry; Biotechnology; Biochemistry, general
ISSN
0273-2289
eISSN
1559-0291
DOI
10.1385/ABAB:127:3:201
Publisher site
See Article on Publisher Site

Abstract

Analysis of peroxidase activity by native polyacrylamide gel electrophoresis (PAGE) from a garlic bulb (Allium sativum L) extract showed two major activities (designated POX1 and POX2). The POX2 isoenzyme was purified to homogeneity by ammonium sulfate precipitation, gel filtration, and cation-exchange chromatography. The purified enzyme was found to be monomeric with a molecular mass of 36.5 kDa, as determined by sodium dodecyl sulfate-PAGE. The optimum temperature ranged from 25 to 40°C and optimum pH was about 5.0. The apparent K m values for guaiacol and H2O2 were 9.5 and 2 mM, respectively. POX2 appeared highly stable since 50% of its activity was conserved at 50°C for 5h. Moreover POX2 was stable over a pH range of 3.5–11.0. Immobilization of POX2 was achieved by covalent binding of the enzyme to an epoxy-Sepharose matrix. The immobilized enzyme showed great stability toward heat and storage when compared with soluble enzyme. These properties permit the use of this enzyme as a biosensor to detect H2O2 in some food components such as milk or its derivatives.

Journal

Applied Biochemistry and Biotechnology – Springer Journals

Published: Apr 17, 2007

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