食品科学 ›› 2008, Vol. 29 ›› Issue (7): 286-290.

• 生物工程 • 上一篇    下一篇

Lactobacillus helveticus 9的酪蛋白水解作用研究

王立平,廖铃,高莉莉, 吴荣荣,张柏林   

  1. 北京林业大学生物科学与技术学院食品科学系; 衡水学院生命科学系; 北京林业大学生物科学与技术学院食品科学系 北京100083; 北京100083; 河北衡水053000
  • 出版日期:2008-07-15 发布日期:2011-07-28

Proteolytic Activity of Lactobacillus helveticus 9 Enzyme to Casein

 WANG  Li-Ping, LIAO  Ling, GAO  Li-Li, WU  Rong-Rong, ZHANG  Bai-Lin   

  1. 1.Department of Food Science, College of Biological Science and Technology, Beijing Forestry University, Beijing 100083, China; 2. Department of Biological Science, Hengshui University, Hengshui 053000, China
  • Online:2008-07-15 Published:2011-07-28

摘要: 基于酪蛋白水解度和多肽含量数据,研究了两株瑞士乳杆菌(L.helveticus 9和L.helveticus 6)与酪蛋白共培养后的蛋白水解效果,菌株L.helveticus 9蛋白水解活性显著高于菌株L.helveticus 6。在不同发酵时间下,菌株L.helveticus9对酪蛋白的水解作用随时间延长而逐渐递增,培养48h时酪蛋白的水解度可达17.3%,多肽含量达到0.62mg/ml;SDS-PAGE分析和Sephadex G-25层析鉴定表明,酪蛋白水解产物多肽含量随培养时间延长而增加。显然,具有较高蛋白水解活力的菌株L.helveticus 9可以用于从酪蛋白中来制备潜在的生物活性肽。

关键词: 酪蛋白, L.helveticus9, 水解活性, 水解度

Abstract: Casein degradation in the presence of two Lactobacillus helveticus strains (strain 6 and strain 9) was investigated based on the formation of transparent zone from hydrolyzed protein, the degree of hydrolysis and the concentration of peptides produced. Strain 9 enzyme has a significant higher activity to degrade casein than that of strain 6. The degree of casein hydrolysis by strain 9 grows gradually as fermentation time delaying from 0 h to 48 h, reaches to 17.3%. The concentration of peptides from casein derived by strain 9 cells is 0.62 mg/ml following 48 h incubation at 37 ℃ SDS-PAGE analysis and profiles of Sephadex G-25 gel filtration also proved that L. helveticus stain 9 is able to release more peptides from casein as co-culture time delaying. The present study indicated that utilization of L. helveticus strain 9 with high proteolytic activity can provide a promising technology to produce potential bio-activity peptides from casein.

Key words: casein, Lactobacillus helveticus 9, proteolytic activity, degree of hydrolysis