摘要
研究了本组纯化的戊糖乳杆菌31~1菌株所产细菌素的理化和生物学特性及其对敏感菌株的抑菌作用,发现该细菌素在80℃热处理15min后活性基本不变,121℃处理15min仍保持一定活性;在pH2~8范围内37℃处理4h保持稳定。当pHi9时活性逐渐降低。胃蛋白酶、胰蛋白酶、蛋白酶K、木瓜蛋白酶、中性蛋白酶均可使该细菌素完全失活;α-淀粉酶可使其部分失活;酸性蛋白酶、溶菌酶不能使其失活。该细菌素抑菌效果明显,在3~5h内可减少敏感菌细胞数10^2~10^3个。测定了其抑菌谱,该细菌素可抑制乳杆菌属、链球菌属、片球菌属中的大部分菌株,还可抑制金黄色葡萄球菌、大肠杆菌、芽抱杆菌中的部分菌株。该细菌素是一种具有良好热、酸稳定性的蛋白活性物质,用于食品防腐将具有较高的安全性。
This study reports the characterization, spectrum of bacteriocin produced by Lactobacillus pentosus 31-1. This bacteriocin remained active when heated at 80℃ for 15 rain, and partly active at 121 "C for 15 rain. It was also active after incubation in pH 2 - 8 environment for 4 h at 37℃, but only partially inactive media above pH 9. Treatment with pepsin, proteinase K, trypsin, papain, neutral proteinase fully inactivated the bacteriocin, but was part-inactivated by a-amylase. The mechanism of activity of bacteriocin is bactericidal, as shown by an obvious decrease of about 2- 3 orders of magnitude in the viable cell numbers of L. plantarum over a period of 3 - 5 h. The bacteriocin had a broad spectrum, including most strains from Lactobacillus, Streptococcus, Pediococcus, especially including Staphylococcus aureus, E. coil, Bacillus cereus, B. subtilis and B. megaterium. Bacteriocin produced by Lactobacillus pentosus 31-1 was an active protein with stability to heat and acid, which will have good potential application in food preservation.
出处
《中国农业大学学报》
CAS
CSCD
北大核心
2006年第1期39-43,共5页
Journal of China Agricultural University
基金
北京市自然科学基金资助项目(6052015)
科技部"十五"科技攻关项目(2001BA501A11)
关键词
戊糖乳杆菌
细菌素
理化特性
Lactobacillus pentosus
bacteriocin
characterization