Purification and characterization of extracellular proteinase produced by Brevibacterium linens ATCC 9172

被引：1
|
作者：
Tomaschová, J [1 ]
Buchinger, W
Hampel, W
Zemanovic, J
机构：
[1] Slovak Univ Technol Bratislava, Fac Chem Technol, Dept Milk Fat & Food Hyg, Bratislava 81237, Slovakia
[2] Univ Technol, Dept Biochem Technol & Microbiol, A-1060 Vienna, Austria
来源：
FOOD CHEMISTRY | 1998年 / 63卷 / 04期
关键词：
D O I：
10.1016/S0308-8146(98)00045-4
中图分类号：
O69 [应用化学];
学科分类号：
081704 ;
摘要：
The micro-organism Brevibacterium linens ATCC 9172 produced five extracellular proteinases, as shown by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) with copolymerized gelatine. One of these was purified to homogeneity by ion-exchange chromatography and native preparative PAGE. The optimum pH and temperature for the proteinase were 8.0 and 50 degrees C, respectively. The enzyme remained stable over a pH range from 6 to 10. The molecular weight estimated by SDS-PAGE was 56 kDa. Serine proteinase inhibitors 3,4-dichloroisocoumarin (3,4-DCI) and phenylmethylsulphonylfluoride (PMSF) inhibited, while Mg2+ and Ca2+ ions activated the proteinase. (C) 1998 Elsevier Science Ltd. All rights reserved.
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页码：499 / 503
页数：5
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