Abstract

A psychrotolerant bacterium identified as Serratia DLCP2 was isolated from sediment of Dal Lake (Jammu and Kashmir, India). The bacterium was able to secrete cold–adapted and alkali–tolerant protease with the highest protease production of 72.1 U/mL in the medium at 20°C and pH 9.0. The protease was 97–fold purified using various chromatographic techniques. The purified enzyme had an apparent molecular weight of about 60 kDa and showed maximal activity at 15°C and pH 10.0. The enzyme showed more than 40% of activity at 0°C. The protease activity was completely inhibited by EDTA, EGTA and phenylmethylsulphonyl fluoride demonstrating that it’s a serine-type metalloprotease. In addition, the Serratia DLCP2 protease had ability to remove the protein stains from the white cloth pieces in a short span of time. The above results indicate that the enzyme is unique for both industrial applications and basic research.

中文翻译：

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沙雷氏菌DLCP2的冷适应丝氨酸金属蛋白酶：纯化，表征和工业潜力。

摘要

从达尔湖（印度贾木和克什米尔）的沉积物中分离出一种鉴定为沙雷氏菌DLCP2的抗精神病细菌。该细菌能够在20°C和pH 9.0的培养基中分泌冷适应和耐碱的蛋白酶，其中蛋白酶的最高产量为72.1 U / mL。使用各种色谱技术将蛋白酶纯化97倍。纯化的酶具有约60kDa的表观分子量，并且在15℃和pH 10.0下显示最大活性。该酶在0°C下显示超过40％的活性。EDTA，EGTA和苯甲基磺酰氟完全抑制了蛋白酶的活性，表明它是一种丝氨酸型金属蛋白酶。此外，沙雷氏菌DLCP2蛋白酶具有在短时间内从白布块上去除蛋白质污渍的能力。以上结果表明该酶对于工业应用和基础研究都是独特的。