Purification and Properties of Pyrophosphatase from Beef Semitendinosus

doi:10.7506/spkx1002-6300-201005036

FOOD SCIENCE ›› 2010, Vol. 31 ›› Issue (5): 160-164.doi: 10.7506/spkx1002-6300-201005036

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Purification and Properties of Pyrophosphatase from Beef Semitendinosus

SUN Zhen-zhen，PENG Zeng-qi*，JIN Hong-guo，SHI Jie

Key Laboratory of Animal Products Processing and Quality Control, Ministry of Education,Nanjing Agricultural University, Nanjing 210095, China

Received:2009-07-01 Revised:2009-10-30 Online:2010-03-01 Published:2010-12-29
Contact: PENG Zeng-qi*， E-mail:zqpeng@njau.edu.cn

Abstract

Abstract:

Pyrophosphatase (PPase) was isolated and purified from beef semitendinosus through homogenization with 0.25 mol/L sucrose, extraction with 0.6 mol/L NaCl solution, precipitation with 50%－70% ammonium sulfate, and ion-exchange chromatography on DEAE-52 cellulose column. SDS-PAGE showed a single band with the relative molecular mass of 72 kD. This enzyme exhibited high substrate specificity to sodium pyrophosphate. Mg2+ as an activator could promote the activity of pyrophosphatase; whereas, Ca2+, EDTA-Na2 and EDTA-Na4 all exhibited an inhibitory effect on its activity. The optimal pH and temperature for reaction were 6.8 and 47 ℃, respectively.

Key words: beef semitendinosus, pyrophosphatase, purification, property

CLC Number:

TS251.1

SUN Zhen-zhen，PENG Zeng-qi*，JIN Hong-guo，SHI Jie. Purification and Properties of Pyrophosphatase from Beef Semitendinosus[J]. FOOD SCIENCE, 2010, 31(5): 160-164.

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Purification and Properties of Pyrophosphatase from Beef Semitendinosus

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