Stefanitsi D, Garel J R
LEBS-CNRS, Gif-sur-Yvette, France.
Lett Appl Microbiol. 1997 Mar;24(3):180-4. doi: 10.1046/j.1472-765x.1997.00376.x.
A zinc-dependent proteinase was extracted from the cell wall of Lactobacillus delbrueckii subsp. bulgaricus and partially purified despite a marked unstability. The caseinolytic activity was associated with a polypeptide chain of 65 kDa that belonged to the M1 family of zinc-dependent proteases. This zinc-dependent proteinase could degrade intact caseins, with a significant preference for beta-casein. The pH-profile of its activity indicated that its relative contribution to the caseinolytic activity increased at acidic pH, suggesting that this zinc proteinase could be involved in the late stages of milk fermentation.
从德氏乳杆菌保加利亚亚种的细胞壁中提取出一种锌依赖性蛋白酶,尽管其稳定性明显不足,但仍进行了部分纯化。酪蛋白水解活性与一条65 kDa的多肽链相关,该多肽链属于锌依赖性蛋白酶的M1家族。这种锌依赖性蛋白酶能够降解完整的酪蛋白,对β-酪蛋白有显著偏好。其活性的pH曲线表明,在酸性pH条件下,它对酪蛋白水解活性的相对贡献增加,这表明这种锌蛋白酶可能参与了牛奶发酵的后期阶段。