Gilot P, Andre P
Département de Microbiologie, Institut d'Hygiène et d'Epidémiologie, Brussels, Belgium.
Appl Environ Microbiol. 1995 Apr;61(4):1661-5. doi: 10.1128/aem.61.4.1661-1665.1995.
Esterases from Listeria monocytogenes strains isolated from cheeses were analyzed by starch gel electrophoresis. Five esterases, numbered from EST 1 to EST 5 in order of decreasing anodal migration, were identified. The EST 1, EST 3, EST 4, and EST 5 set was most active toward alpha-naphthyl propionate, while EST 2 was most active toward alpha-naphthyl acetate. Results from inhibitor studies suggest that all of these esterases were EC class 3.1.1.1 carboxylesterases, except that EST 1 and EST 3 also showed some sensitivity to parahydroxymercuribenzoate. Polymorphism of these five esterases was observed in the population. Twelve esterase patterns were defined and used to subdivide serotypes.
通过淀粉凝胶电泳分析从奶酪中分离出的单核细胞增生李斯特菌菌株的酯酶。鉴定出了五种酯酶,按照阳极迁移率递减的顺序编号为EST 1至EST 5。EST 1、EST 3、EST 4和EST 5组对α-萘基丙酸的活性最高,而EST 2对α-萘基乙酸的活性最高。抑制剂研究结果表明,所有这些酯酶均为EC 3.1.1.1类羧酸酯酶,但EST 1和EST 3对对羟基汞苯甲酸也表现出一定的敏感性。在群体中观察到这五种酯酶的多态性。定义了十二种酯酶模式并用于细分血清型。