乳酸菌SD501抗李斯特菌素的分离与鉴定。

Q2 Agricultural and Biological Sciences
In-Chan Hwang, Ju Kyoung Oh, Sang Hoon Kim, Sejong Oh, Dae-Kyung Kang
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引用次数: 1

摘要

尽管已从多种乳酸菌中分离出具有抗李斯特菌活性的细菌素,但对乳酸菌中具有抗李斯特菌活性的细菌素知之甚少,乳酸菌是一种在乳制品中产生双乙酰和胞外多糖的异发酵细菌。本研究从白杆菌中分离出一种抗李斯特菌素。乳酸SD501和表征。它对单核增生李斯特菌特别有效,对粪肠球菌也有抑制作用。抗李斯特菌活性在稳定期早期达到最大值,随后逐渐降低。该抗李斯特菌物质对蛋白酶K和凝乳胰蛋白酶敏感,证实了其蛋白性质。其活性在pH值1 ~ 10范围内保持稳定。此外,它具有较强的耐高温性,即使在121℃下孵育15 min,其活性仍保持不变。部分纯化的抗李斯特菌素的表观分子质量约为7 kDa。SD501细菌素的特点,包括其小分子大小(
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Isolation and Characterization of an Anti-listerial Bacteriocin from <i>Leuconostoc lactis</i> SD501.

Isolation and Characterization of an Anti-listerial Bacteriocin from <i>Leuconostoc lactis</i> SD501.

Isolation and Characterization of an Anti-listerial Bacteriocin from Leuconostoc lactis SD501.

Although bacteriocins with anti-listerial activity have been isolated from a wide variety of lactic acid bacteria, little is known about those from Leuconostoc lactis, a heterofermentative bacterium that produces diacetyl and exopolysaccharides in dairy foods. In this study, an anti-listerial bacteriocin was isolated from Leuc. lactis SD501 and characterized. It was particularly potent against Listeria monocytogenes and also inhibited Enterococcus faecalis. Anti-listerial activity reached a maximum during the early stationary phase and then decreased gradually. The anti-listerial substance was sensitive to proteinase K and ɑ-chymotrypsin, confirming its proteinaceous nature. Its activity remained stable at pH values ranging from 1 to 10. In addition, it was strongly resistant to high temperatures, retaining its activity even after incubation for 15 min at 121℃. The apparent molecular mass of the partially purified anti-listerial bacteriocin was approximately 7 kDa. The characteristics of the SD501 bacteriocin, including its small molecular size (<10 kDa), strong anti-listerial activity, wide pH stability and good thermostability, indicate its classification as a Class IIa bacteriocin.

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CiteScore
1.22
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