干酪乳杆菌干酪亚种IFPL 731中脯氨酰二肽酶的纯化与特性分析
Purification and characterization of a prolidase from Lactobacillus casei subsp. casei IFPL 731.
作者信息
Fernández-Esplá M D, Martín-Hernández M C, Fox P F
机构信息
Instituto del Frío (CSIC), Ciudad Universitaria, Madrid, Spain.
出版信息
Appl Environ Microbiol. 1997 Jan;63(1):314-6. doi: 10.1128/aem.63.1.314-316.1997.
Abstract
A peptidase showing a high level of specificity towards dipeptides of the X-Pro type was purified to homogeneity from the cell extract of Lactobacillus casei subsp. casei IFPL 731. The enzyme was a monomer having a molecular mass of 41 kDa. The pH and temperature optima were 6.5 to 7.5 and 55 degrees C, respectively. Metal chelating agents completely inhibited enzyme activity, indicating that the prolidase was a metalloenzyme. The Michaelis constant (K(m)) and Vmax for several proline-containing dipeptides were determined.
摘要
从干酪乳杆菌干酪亚种IFPL 731的细胞提取物中纯化出一种对X-Pro型二肽具有高度特异性的肽酶，直至达到同质状态。该酶为单体，分子量为41 kDa。最适pH值和温度分别为6.5至7.5和55℃。金属螯合剂完全抑制酶活性，表明脯氨酰二肽酶是一种金属酶。测定了几种含脯氨酸二肽的米氏常数（K(m)）和最大反应速度（Vmax）。
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