Park Sang-Hee, Itoh Kikuji, Kikuchi Eisaku, Niwa Hidekazu, Fujisawa Tomohiko
Laboratory of Veterinary Public Health, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.
Curr Microbiol. 2003 May;46(5):385-8. doi: 10.1007/s00284-002-3898-z.
We isolated bacteriocin-producing Lactococcus lactis subsp. lactis from Kimchi. The bacteriocin inhibited strains of Clostridium perfringens, C. difficile, Listeria monocytogenes, vancomycin-resistant Enterococcus, and one out of four methicillin-resistant Staphylococcus aureus strains, as well as some closely related lactic acid bacteria. In tricine-SDS-PAGE, the bacteriocin migrated with an apparent molecular weight of about 4 kDa to the same location as nisin A and crude nisin Z. The gene encoding this bacteriocin was found to be identical to that of nisin Z with direct PCR sequence methods. The inhibitory activity was stable against heat and pH, but it was lost at 100 degrees C for 1 h and at 121 degrees C for 15 min. The bacteriocin was inactivated by proteolytic enzymes, but was not affected by lysozyme, lipase, catalase, or beta-glucosidase. There were some differences in characteristics from those of nisins described previously.
我们从泡菜中分离出了产细菌素的乳酸乳球菌乳酸亚种。该细菌素可抑制产气荚膜梭菌、艰难梭菌、单核细胞增生李斯特菌、耐万古霉素肠球菌以及四株耐甲氧西林金黄色葡萄球菌中的一株，以及一些密切相关的乳酸菌。在tricine-SDS-PAGE中，该细菌素迁移时的表观分子量约为4 kDa，与乳酸链球菌素A和粗制乳酸链球菌素Z迁移到相同位置。通过直接PCR测序方法发现，编码该细菌素的基因与乳酸链球菌素Z的基因相同。其抑制活性对热和pH稳定，但在100℃下1小时和121℃下15分钟会丧失。该细菌素可被蛋白水解酶灭活，但不受溶菌酶、脂肪酶、过氧化氢酶或β-葡萄糖苷酶影响。其特性与先前描述的乳酸链球菌素存在一些差异。
