Sharipova M R, Shakirov E V, Gabdrakhmanova L A, Balaban N P, Kalacheva N V, Rudenskaya G N, Leshchinskaya I B
Department of Microbiology, Kazan State University, Kremlievskaya str, 18, Kazan 420008, Russia.
Med Sci Monit. 2000 Jan-Feb;6(1):8-12.
Thiol-dependent serine proteinase and glutamylendopeptidase of Bacillus intermedius 3-19 being prevailing enzymes in the total pool of extracellular proteinases (95%) of this microorganism in catalytic active form were detected on the membrane of the cells. Production of these enzymes was maximum on the medium containing inorganic phosphate and gelatin and decreased 2-4-fold on the medium with glucose and lactate. The level of the activity of extracellular enzymes correlated with that of corresponding membrane-bound proteins. The addition of CoCl2 (2 mM) into the medium caused essential increase in extracellular glutamylendopeptidase activity and promoted the release of membrane-bound enzyme into cultural fluid. Proteolytic activity was detected in cytoplasm also. Proteinases localized in cytoplasm were shown to differ in properties from those secreted.
中间芽孢杆菌3-19的硫醇依赖性丝氨酸蛋白酶和谷氨酰胺内肽酶作为该微生物胞外蛋白酶总库中占主导地位的酶（95%），以催化活性形式在细胞膜上被检测到。这些酶在含有无机磷酸盐和明胶的培养基上产量最高，而在含有葡萄糖和乳酸的培养基上产量降低2至4倍。胞外酶的活性水平与相应膜结合蛋白的活性水平相关。向培养基中添加2 mM的CoCl2会导致胞外谷氨酰胺内肽酶活性显著增加，并促进膜结合酶释放到培养液中。在细胞质中也检测到了蛋白水解活性。结果表明，位于细胞质中的蛋白酶在性质上与分泌的蛋白酶不同。
