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Purification and characterization of milk-clotting enzymes from oyster mushroom (Pleurotus ostreatus (Fr.) Kumm)

Purification and characterization of milk-clotting enzymes from oyster mushroom (Pleurotus... Three enzymes with milk-clotting activity have been isolated from the fruiting bodies of Pleurotus ostreatus (Fr.) Kumm) by (NH4)2SO4 precipitation, gel chromatography on Sephadex G75, and ion exchange chromatography on carboxymethylcellulose (CMC). Isoelectric points of the enzymes, as determined by isoelectrofocusing, equaled 4.2, 6.7, and 8.8. Inhibition analysis showed that the enzymes with isoelectric points of 4.2 and 6.7 belong to the class of metal-dependent proteinases, while the enzyme with the isoelectric point of 8.8 belongs to the serine protease class. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Applied Biochemistry and Microbiology Springer Journals

Purification and characterization of milk-clotting enzymes from oyster mushroom (Pleurotus ostreatus (Fr.) Kumm)

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References (6)

Publisher
Springer Journals
Copyright
Copyright © 2009 by Pleiades Publishing, Ltd.
Subject
Life Sciences; Medical Microbiology ; Microbiology ; Biochemistry, general
ISSN
0003-6838
eISSN
1608-3024
DOI
10.1134/S0003683809060088
Publisher site
See Article on Publisher Site

Abstract

Three enzymes with milk-clotting activity have been isolated from the fruiting bodies of Pleurotus ostreatus (Fr.) Kumm) by (NH4)2SO4 precipitation, gel chromatography on Sephadex G75, and ion exchange chromatography on carboxymethylcellulose (CMC). Isoelectric points of the enzymes, as determined by isoelectrofocusing, equaled 4.2, 6.7, and 8.8. Inhibition analysis showed that the enzymes with isoelectric points of 4.2 and 6.7 belong to the class of metal-dependent proteinases, while the enzyme with the isoelectric point of 8.8 belongs to the serine protease class.

Journal

Applied Biochemistry and Microbiology – Springer Journals

Published: Nov 6, 2009

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