Department of Food Science, Rutgers, The State University of New Jersey, New Brunswick, 08901, USA.
J Appl Microbiol. 2009 Apr;106(4):1370-7. doi: 10.1111/j.1365-2672.2008.04105.x. Epub 2009 Feb 2.
To characterize the antimicrobial protein produced by Bacillus coagulans used in the probiotic dietary supplement (Lactospore) Probiotic, Sabinsa Corp., Piscataway, NJ, USA).
Bacillus coagulans ATCC 7050 was grown at 37 degrees C for 18 h. The cell free supernatant was concentrated 10-fold (lactosporin preparation, LP). The antimicrobial activity of LP was confirmed against Micrococcus luteus ATCC 10420 in a well diffusion assay. The proteinaceous nature of LP was determined following exposure to different enzymes. The activity of LP was pH-dependent but stable to heat. The isoelectric point of LP was determined to be 3.5-4.0. PCR analyses showed no similarity between lactosporin and known antimicrobial proteins produced by the Bacillus spp.
Lactosporin is a novel antimicrobial protein. Initial characterization indicates that it may fall outside of the conventional classification of class I and II bacteriocins. Loss of activity after exposure to a number of proteolytic enzymes and lipase suggest that lactosporin may posses a lipid moiety which contributes to its inhibitory activity.
The unique characteristics of lactosporin, including its antimicrobial activity against pathogenic micro-organisms, indicate that it may have potential for application in foods and personal care products.
对用于益生菌膳食补充剂(Lactospore)的凝结芽孢杆菌产生的抗菌蛋白进行特征描述,该益生菌由美国新泽西州皮斯卡塔韦的 Sabinsa 公司生产。
将凝结芽孢杆菌 ATCC 7050 在 37°C 下培养 18 小时。将无细胞上清液浓缩 10 倍(Lactosporin 制剂 LP)。采用孔扩散法证实 LP 对微球菌 ATCC 10420 具有抗菌活性。用不同的酶处理后,确定 LP 的蛋白性质。LP 的活性依赖于 pH,但对热稳定。LP 的等电点测定为 3.5-4.0。PCR 分析表明,Lactosporin 与芽孢杆菌属产生的已知抗菌蛋白之间没有相似性。
Lactosporin 是一种新型抗菌蛋白。初步特征表明,它可能不属于传统的 I 类和 II 类细菌素分类。暴露于多种蛋白水解酶和脂肪酶后活性丧失表明,Lactosporin 可能具有脂质部分,这有助于其抑制活性。
Lactosporin 的独特特性,包括其对致病微生物的抗菌活性,表明它可能具有在食品和个人护理产品中的应用潜力。