Expression and purification of recombinant Lactobacillus casei bacteriocin and analysis of its antibacterial activity. Issue 1 (1st January 2020)

• Record Type: Journal Article
• Authors: Yu, Wei; Ma, Jiage; Chen, Xiaoqian; Tan, Ying; Chen, Pin; Zhu, Xumeng; Liu, Libo
• Is Part Of: CyTA: journal of food. Volume 18:Issue 1(2020)
• Page Start: 301
• Page End: 308
• Publication Date: 2020-01-01
• Subjects: Bacteriocin -- lactobacillus casei -- heterologous expression -- antimicrobial activity -- protein purification; Bacteriocina -- Lactobacillus casei -- expresión heteróloga -- actividad antimicrobiana -- purificación de proteínas; Food -- Periodicals; Nutrition -- Periodicals; Food -- Research -- Periodicals; 641.05
• DOI: 10.1080/19476337.2020.1749134
• Languages: English
• ISSNs: 1947-6337

Abstract

ABSTRACT: Diseases caused by foodborne pathogens have largely promoted the search for natural biopreservatives. We constructed recombinant plasmids pGEX-4 T-1-lacA, pGEX-4 T-1-lacB, and pGEX-4 T-1-lacAB, harboring genes for bacteriocins lactocin (Lac) A, B, and AB, respectively, with protein expression achieved in Escherichia coli BL21 cells. LacAB was purified using a glutathione S-transferase (GST) protein purification kit, and the GST tag was removed using thrombin for a maximum concentration yield of 1.85 mg/mL. LacAB and the combination of LacA and LacB showed better antimicrobial activity than LacA or LacB alone. The antibacterial activity assay indicated that purified LacAB has broad-spectrum and significant antimicrobial activity against Staphylococcus aureus ATCC25923, with a minimum inhibitory concentration of 125 μg/mL. This study is the first, to our knowledge, to demonstrate the antimicrobial activity of LacAB; moreover, it provides an efficient strategy for the production of bacteriocin LacAB, which could be a food preservative candidate.