Purification and Characterization of a Bacteriocin Produced by Lactobacillus lactis Isolated from Marine Environment
Purification and Characterization of a Bacteriocin Produced by Lactobacillus lactis Isolated from Marine Environment
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发表时间：
2010-03
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通讯作者：
G. Rajaram;P. Manivasagan;B. Thilagavathi;A. Saravanakumar
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作者：
G. Rajaram;P. Manivasagan;B. Thilagavathi;A. Saravanakumar
从海洋环境中分离出的产生细菌素的乳酸乳杆菌菌株，对一些主要食源性病原体表现出广泛的抗菌活性。在30℃、pH 6.0和1.5%氯化钠溶液下观察到最大细菌素产量。除酶外，α-淀粉酶、DNase、RNase 和脂肪酶对细菌素的产生有轻微的积极作用。蛋白酶K和胃蛋白酶强烈抑制细菌素的产生。在洗涤剂中，十二烷基硫酸钠 (SDS)、Tween 80 和 Tritone X-100 会刺激细菌素的产生，但会被 EDTA 和尿素强烈抑制。细菌素已通过硫酸铵沉淀和离子交换（DEAE 纤维素）色谱法纯化。从生化角度看，它是纯蛋白质部分，分子量为 94 kDa。该研究揭示了使用细菌素作为食品防腐剂和乳酸乳球菌菌株作为益生菌的可能性。
Bacteriocin producing Lactobacillus lactis strain isolated from marine environment, showed broad range of antibacterial activity against some major food borne pathogens. Maximum bacteriocin production was observed at 30℃, pH 6.0 and 1.5% sodium chloride solution. In addition of enzymes, α-amylase, DNase, RNase and lipase were slightly positive effect bacteriocin production. Proteinase K and pepsin were strongly inhibited bacteriocin production. Among detergents, Sodium dodecyl sulphate (SDS), Tween 80 and Tritone X-100 stimulated bacteriocin production and strongly inhibited by EDTA and urea. The bacteriocin has purified by ammonium sulphate precipitate and ion exchange (DEAE cellulose) chromatography. Biochemically it was pure protein moiety and the molecular weight was 94 kDa. The study revealed the possibility of using bacteriocin as a food preservative and the L. lactis strain as probiotic.