食品保藏是一种用于维持和改善食品质量的示意性和科学的程序,保质期,和营养价值。虽然,一方面,古老的常规方法,如冷冻,巴氏灭菌,罐装,和化学方法有可能延长可食用物质的保质期,但另一方面,它们也会降低其营养价值。本研究的重点是通过消减蛋白质组学管道鉴定有前途的细菌素,以作为食品保存的替代方法。细菌素是由某些微生物产生的小肽,通过破坏居住在其附近的其他密切相关的细菌来自然地保护自己。P.fragi是引起食物腐败的最著名的微生物之一。由于多药耐药菌的出现和流行,有必要解开新的药物靶点,在食物腐烂过程中至关重要。基于减法审查,UDP-N-乙酰葡糖胺O-酰基转移酶(LpxA)被选为有前途的治疗性蛋白质靶标,可在食物腐败的发展中起重要作用。SubtilosinA,Thuricin-CD,根据分子对接测定结果,发现变酸B-NY266是LpxA的最有效抑制剂。通过MM/PBSA方法对LpxA和三个顶级对接复合物进行分子动力学模拟和结合能计算,即,LpxA-subtilosinA,LpxA-Thuricin-CD,和LpxA-mutacinB-NY266在整个模拟过程中显示出稳定性,并确保入围的细菌素对LpxA具有很强的亲和力。
Food preservation is a schematic and scientific procedure employed for the maintenance and improvement of food\'s quality, shelf life, and nutritional value. Although, on one hand, ancient conventional methods such as freezing, pasteurization, canning, and chemical methods have the potential to lengthen the shelf life of edible substances, but on the other hand, they can deteriorate its nutritional value as well. Present research focuses on the identification of promising
bacteriocins against Pseudomonas fragi via subtractive proteomics pipeline as an alternative approach for food preservation.
Bacteriocins are small peptides produced by certain microbes to naturally defend themselves by destroying other closely related bacteria residing in their neighborhood. P. fragi lies among the most notable microbes responsible for the elicitation of food spoilage. Due to increasing emergence and prevalence of multidrug resistance bacteria, there is a need to unravel novel drug targets, crucially involved in food decay process. Based on subtractive scrutinization, UDP-N-acetylglucosamine O-acyltransferase (LpxA) was chosen as promising therapeutic protein target that could play a significant role in progression of food spoilage. Subtilosin A, thuricin-CD, and mutacin B-NY266 were found as the most robust inhibitors of LpxA according to the molecular docking assay results. Molecular dynamic simulations and binding energy calculations via MM/PBSA method of LpxA and three top hit docked complexes, i.e., LpxA-subtilosin A, LpxA-thuricin-CD, and LpxA-mutacin B-NY266, revealed stability throughout simulations and ensured that shortlisted
bacteriocins had strong affinity for LpxA.