干酪乳杆菌的细胞结合蛋白酶系统——纯化与特性分析

The cell-bound proteinase system of Lactobacillus casei--purification and characterization.

作者信息

Ezzat N, el Soda M, el Shafei H

机构信息

Faculty of Agriculture, Alexandria University, Egypt.

出版信息

Int J Food Microbiol. 1988 Jun;6(4):327-32. doi: 10.1016/0168-1605(88)90026-8.

DOI:10.1016/0168-1605(88)90026-8

PMID:3152801

Abstract

The cell-wall crude extract from Lactobacillus casei NCDO 151 was partially purified by DEAE-Sephacel chromatography. Three active fractions were eluted. Two major peaks (eluted with 0.05 M and 0.27 M phosphate buffer) were further investigated. Peak I represented enzymatic activity with an optimum temperature of 40 degrees C, an optimum pH of 7.0 and was strongly inhibited by the serine proteinase inhibitor phenylmethylsulfonylfluoride. Peak II represented an enzymatic activity with an optimum temperature of 45 degrees C, an optimum pH of 7.5 and was totally inhibited by p-hydroxymercuribenzoate. None of the enzymes was affected by the metal chelator ethylenediaminetetraacetic acid at a concentration up to 1 x 10(-2).

摘要

干酪乳杆菌NCDO 151的细胞壁粗提物经DEAE-葡聚糖凝胶层析进行部分纯化。洗脱得到三个活性组分。对两个主要峰（分别用0.05 M和0.27 M磷酸盐缓冲液洗脱）进行了进一步研究。峰I代表一种酶活性，其最适温度为40℃，最适pH为7.0，且被丝氨酸蛋白酶抑制剂苯甲基磺酰氟强烈抑制。峰II代表一种酶活性，其最适温度为45℃，最适pH为7.5，且被对羟基汞苯甲酸完全抑制。在浓度高达1×10⁻²时，金属螯合剂乙二胺四乙酸对这些酶均无影响。