德氏乳杆菌保加利亚亚种ACA-DC 178的细胞壁结合蛋白酶：特性及对β-酪蛋白的特异性
Cell-wall-bound proteinase of Lactobacillus delbrueckii subsp. lactis ACA-DC 178: characterization and specificity for beta-casein.
作者信息
Tsakalidou E, Anastasiou R, Vandenberghe I, van Beeumen J, Kalantzopoulos G
机构信息
Laboratory of Dairy Research, Department of Food Science and Technology, Agricultural University of Athens, 118 55 Athens, Greece.
出版信息
Appl Environ Microbiol. 1999 May;65(5):2035-40. doi: 10.1128/AEM.65.5.2035-2040.1999.
Abstract
Lactobacillus delbrueckii subsp. lactis ACA-DC 178, which was isolated from Greek Kasseri cheese, produces a cell-wall-bound proteinase. The proteinase was removed from the cell envelope by washing the cells with a Ca2+-free buffer. The crude proteinase extract shows its highest activity at pH 6.0 and 40 degrees C. It is inhibited by phenylmethylsulfonyl fluoride, showing that the enzyme is a serine-type proteinase. Considering the substrate specificity, the enzyme is similar to the lactococcal PI-type proteinases, since it hydrolyzes beta-casein mainly and alpha- and kappa-caseins to a much lesser extent. The cell-wall-bound proteinase from L. delbrueckii subsp. lactis ACA-DC 178 liberates four main peptides from beta-casein, which have been identified.
摘要
德氏乳杆菌乳酸亚种ACA-DC 178分离自希腊卡塞里奶酪，可产生一种细胞壁结合蛋白酶。通过用无Ca2+缓冲液洗涤细胞，可将该蛋白酶从细胞膜中去除。粗蛋白酶提取物在pH 6.0和40℃时表现出最高活性。它被苯甲基磺酰氟抑制，表明该酶是一种丝氨酸型蛋白酶。考虑到底物特异性，该酶与乳球菌PI型蛋白酶相似，因为它主要水解β-酪蛋白，而对α-酪蛋白和κ-酪蛋白的水解程度要小得多。德氏乳杆菌乳酸亚种ACA-DC 178的细胞壁结合蛋白酶从β-酪蛋白中释放出四种主要肽段，这些肽段已被鉴定。
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