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Position: Home > Articles > Study on Isolation and Purification of Pyrophosphatase from Chicken Breast and Its Properties FOOD SCIENCE 2007,28 (7) 299-304

鸡胸大肌中焦磷酸酶的分离纯化及特性研究

作  者:
姚蕊;彭增起;周光宏;何燕;靳红果
单  位:
南京农业大学教育部肉品加工与质量控制重点实验室
关键词:
鸡胸肉;焦磷酸酶;分离纯化;性质
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℃。
译  名:
Study on Isolation and Purification of Pyrophosphatase from Chicken Breast and Its Properties
作  者:
YAO Rui,PENG Zeng-qi,ZHOU Guang-hong,HE Yan,JIN Hong-guo (Key Laboratory of Aniaml Products Processing and Quality Control, Ministry of Education, Nanjing Agricultural University, Nanjing 210095, China)
关键词:
chicken breast;pyrophosphatase;isolation and purification;properties
摘  要:
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.

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