食品科学 ›› 2007, Vol. 28 ›› Issue (7): 299-304.

• 生物工程 • 上一篇    下一篇

鸡胸大肌中焦磷酸酶的分离纯化及特性研究

 姚蕊, 彭增起, 周光宏, 何燕, 靳红果   

  1. 南京农业大学教育部肉品加工与质量控制重点实验室; 南京农业大学教育部肉品加工与质量控制重点实验室 江苏南京210095; 江苏南京210095;
  • 出版日期:2007-07-15 发布日期:2011-10-24

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

 YAO  Rui, PENG  Zeng-Qi, ZHOU  Guang-Hong, HE  Yan, JIN  Hong-Guo   

  1. Key Laboratory of Aniaml Products Processing and Quality Control, Ministry of Education, Nanjing Agricultural University, Nanjing 210095, China
  • Online:2007-07-15 Published:2011-10-24

摘要: 经匀浆、0.6mol/L NaCl提取、硫酸铵分级分离、DEAE-纤维素离子交换柱层析,从鸡胸肉中纯化了焦磷酸酶。该酶有较强的底物专一性,只对添加到肉中的焦磷酸四钠发生作用。Mg2+不仅是其激活剂,还对酶的稳定性发挥作用,Ca2+、EDTA-Na2抑制酶活性。以焦磷酸四钠为底物,测得该酶的最适pH为7.4,最适温度为40℃。

关键词: 鸡胸肉, 焦磷酸酶, 分离纯化, 性质

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