Study on Isolation and Purification of Pyrophosphatase from Chicken Breast and Its Properties

Abstract

Abstract: The pyrophosphatase was isolated and partially purified from chicken breast, by means of homogenation, 0.6 mol/L NaCl extractions, ammonium sulfate precipitation, and ion-exchange chromatography on DEAE cellulose column. This enzyme catalyzes the hydrolysis of sodium pyrophosphate but not that of other phosphate esters. Mg2+ not only is its activator, but also stabilizer, Ca2+ and EDTA-Na2 have inhibiting effects. With PPi as the substrate of pyrophosphatase. Its optimum pH and temperature are 7.4 and 40 ℃ respectively.

Key words: chicken breast, pyrophosphatase, isolation and purification, properties

YAO Rui, PENG Zeng-Qi, ZHOU Guang-Hong, HE Yan, JIN Hong-Guo. Study on Isolation and Purification of Pyrophosphatase from Chicken Breast and Its Properties[J]. FOOD SCIENCE, 2007, 28(7): 299-304.

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Study on Isolation and Purification of Pyrophosphatase from Chicken Breast and Its Properties

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