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Characterization of bacteriocin ABC transporter ATP-binding protein produced by a newly isolated Enterococcus casseliflavus MI001 strain
Beni-Suef University Journal of Basic and Applied Sciences ( IF 2.5 ) Pub Date : 2019-09-12 , DOI: 10.1186/s43088-019-0006-z
Indira Mikkili , Venkateswarulu TC , Abraham Peele Karlapudi , Vidya Prabhakar Kodali , Krupanidhi Srirama

ATP-binding cassette (ABC) transporters constitute one of the largest transporter protein families and play a role in diverse biological processes. In the present study, bacteriocin isolated from the Enterococcus casseliflavus MI001 strain was identified as an ABC transporter ATP-binding protein. The optimal conditions for the production of bacteriocin were found to be at 35 °C, a pH 5.5, and an incubation time of 24 h. Purification was performed using ammonium sulphate precipitation, gel filtration, and DEAE ion exchange chromatography. The bacteriocin was purified with an eightfold purification scheme resulting with a specific activity of 15,000 AU/mg. The NMR spectrum of purified bacteriocin revealed the presence of amino acids, namely lysine, methionine, cysteine, proline, threonine, tryptophan, and histidine. Further, the bacteriocin ABC transporter showed antimicrobial activity against food spoilage microorganisms. The ABC transporter ATP-binding protein could be used as a potential alternative for food preservation, and it may be considered as a bio-preservative agent in food processing industries.

中文翻译:

新分离的球状肠球菌 MI001 菌株产生的细菌素 ABC 转运蛋白 ATP 结合蛋白的表征

ATP 结合盒 (ABC) 转运蛋白构成最大的转运蛋白家族之一,并在多种生物过程中发挥作用。在本研究中,从卡氏肠球菌 MI001 菌株中分离出的细菌素被鉴定为一种 ABC 转运蛋白 ATP 结合蛋白。发现产生细菌素的最佳条件是 35°C、pH 5.5 和 24 小时的孵育时间。使用硫酸铵沉淀、凝胶过滤和DEAE离子交换层析进行纯化。细菌素采用八倍纯化方案纯化,比活性为 15,000 AU/mg。纯化细菌素的 NMR 谱显示存在氨基酸,即赖氨酸、蛋氨酸、半胱氨酸、脯氨酸、苏氨酸、色氨酸和组氨酸。更多,细菌素 ABC 转运蛋白对食品腐败微生物显示出抗菌活性。ABC 转运蛋白 ATP 结合蛋白可用作食品保鲜的潜在替代品,并可被视为食品加工行业的生物防腐剂。
更新日期:2019-09-12
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