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Isolation and purification of Mn-peroxidase from Azospirillum brasilense SP245

Isolation and purification of Mn-peroxidase from Azospirillum brasilense SP245 Homogenous Mn-peroxidase of a 26-fold purity grade was isolated from a culture of Azospirillum brasilense Sp245 cultivated on a medium containing 0.1 mM pyrocatechol. The molecular weight of the enzyme is 43 kD as revealed by electrophoresis in SDS-PAAG. It was shown that the use of pyrocatechol and 2,2′-azino-bis(3-ethylbenzotiazoline-6-sulfonate) at concentrations of 0.1 and 1 mM as inductors increased the Mn-peroxidase activity by a factor of 3. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Applied Biochemistry and Microbiology Springer Journals

Isolation and purification of Mn-peroxidase from Azospirillum brasilense SP245

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Publisher
Springer Journals
Copyright
Copyright © 2012 by Pleiades Publishing, Ltd.
Subject
Life Sciences; Microbiology; Medical Microbiology; Biochemistry, general
ISSN
0003-6838
eISSN
1608-3024
DOI
10.1134/S0003683812010097
Publisher site
See Article on Publisher Site

Abstract

Homogenous Mn-peroxidase of a 26-fold purity grade was isolated from a culture of Azospirillum brasilense Sp245 cultivated on a medium containing 0.1 mM pyrocatechol. The molecular weight of the enzyme is 43 kD as revealed by electrophoresis in SDS-PAAG. It was shown that the use of pyrocatechol and 2,2′-azino-bis(3-ethylbenzotiazoline-6-sulfonate) at concentrations of 0.1 and 1 mM as inductors increased the Mn-peroxidase activity by a factor of 3.

Journal

Applied Biochemistry and Microbiology – Springer Journals

Published: Dec 29, 2011

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