Montville T J, Chen Y
Department of Food Science, Cook College, Rutgers, The State University of New Jersey, New Brunswick 08901, USA.
Appl Microbiol Biotechnol. 1998 Nov;50(5):511-9. doi: 10.1007/s002530051328.
Nisin and pediocin PA-1 are examples of bacteriocins from lactic acid bacteria (LAB) that have found practical applications as food preservatives. Like other natural antimicrobial peptides, LAB bacteriocins act primarily at the cytoplasmic membranes of susceptible microorganisms. Studies with in vivo as well as in vitro membrane systems are directed toward understanding how bacteriocins interact with membranes so as to provide a mechanistic basis for their rational applications. The dissipation of proton motive force was identified early on as the common mechanism for the lethal activity of LAB bacteriocin. Models for nisin/membrane interactions propose that the peptide forms poration complexes in the membrane through a multistep process of binding, insertion, and pore formation. This review focuses on the current knowledge of: (1) the mechanistic action of nisin and pediocin-like bacteriocins, (2) the requirement for a cell factor such as a membrane protein, (3) the influence of membrane potential, pH, and lipid composition on the specificity and efficacy of bacteriocins, and (4) the roles of specific amino acids and structural domains of the bacteriocins in their action.
乳链菌肽和片球菌素PA-1是来自乳酸菌（LAB）的细菌素实例，它们已作为食品防腐剂得到实际应用。与其他天然抗菌肽一样，LAB细菌素主要作用于敏感微生物的细胞质膜。体内和体外膜系统的研究旨在了解细菌素如何与膜相互作用，从而为其合理应用提供机制基础。质子动力的耗散很早就被确定为LAB细菌素致死活性的共同机制。乳链菌肽/膜相互作用模型提出，该肽通过结合、插入和孔形成的多步过程在膜中形成孔道复合物。本综述重点关注以下方面的现有知识：（1）乳链菌肽和片球菌素样细菌素的作用机制，（2）对细胞因子如膜蛋白的需求，（3）膜电位、pH值和脂质组成对细菌素特异性和功效的影响，以及（4）细菌素的特定氨基酸和结构域在其作用中的作用。
