Isolation and Purification of Lactoperoxidase and Its Enzymatic Properties

FOOD SCIENCE ›› 2006, Vol. 27 ›› Issue (2): 100-104.

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Isolation and Purification of Lactoperoxidase and Its Enzymatic Properties

LU Rong-Rong, XU Shi-Ying, WANG Zhang

1.School of Food Science and Technology, Southern Yangtze University; 2.Key Laboratory of Food Science and Safety, Ministry of Education, Southern Yangtze University.

Online:2006-02-15 Published:2011-09-05

Abstract

Abstract: A stepwise procedure for isolation and purification of lactoperoxidase by ultrafiltration and ion exchange chromatography was investigated. It was shown as a single band in SDS-PAGE. The molecular weight of lactoperoxidase was 75035D. The recovery of lactoperoxidase activity was 76.17%. The optimum pH for lactoperoxidase was 5.0～5.5, and the optimum temperature for lactoperoxidase was 55℃. At 70℃ and 75℃, two independent first-order inactivation reactions were found just as the peroxidases from plants.

Key words: , lactoperoxidase； isolation； purification； enzyme activity；

LU Rong-Rong, XU Shi-Ying, WANG Zhang. Isolation and Purification of Lactoperoxidase and Its Enzymatic Properties[J]. FOOD SCIENCE, 2006, 27(2): 100-104.

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Isolation and Purification of Lactoperoxidase and Its Enzymatic Properties

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