新分离的气单胞菌部分纯化表面活性剂-清洁剂和碱耐热蛋白酶的制备、表征和固定化

Sumitra Datta, G. Menon, Bincy Varughese
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引用次数: 8

摘要

从印度Thanjavur的牛棚中分离出生长在大范围pH值(7.0-11.0)和中盐度(0-5% NaCl)条件下的蛋白水解气单胞菌caviae p -1。它产生脂肪酶、明胶酶和聚羟基丁酸酯。考察了不同培养条件、培养时间、碳氮源、维生素、氨基酸、表面活性剂和金属离子对P-1-1最佳生长和蛋白酶产量的影响。在37℃条件下,在pH 8.0条件下,1%果糖、1%酵母提取物、0.1%硫酸铵、3% NaCl、0.1% CaCl2·2H2O、1%甘氨酸、0.1%维生素E和0.1%吐温-40培养42小时,蛋白酶产量达到最大(0.128 U/mL)。在pH(7.0-12.0)、温度(15-100°C)和盐度(0-9% NaCl)的较宽范围内均有活性,其中pH 10.0、55°C和3% NaCl的活性最强。在pH 12.0和100℃时,其活性分别为65%和48%。部分纯化的蛋白酶在pH 7.0-12.0和NaCl 0-5%的盐度范围内保持高度稳定(100%)48小时。Cu2+、Mn2+、Co2+和Ca2+对其活性没有抑制作用。它在极端ph值、温度以及存在表面活性剂和商业洗涤剂时的稳定性表明它可能应用于洗衣洗涤剂。部分纯化的蛋白酶被固定化和重复使用。这是首次报道从鱼子酱中分离到耐碱、耐热、表面活性剂、洗涤剂稳定的部分纯化的细胞外蛋白酶。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Production, characterization, and immobilization of partially purified surfactant–detergent and alkali-thermostable protease from newly isolated Aeromonas caviae
ABSTRACT Proteolytic Aeromonas caviae P-1-1 growing at wide-ranging pH (7.0–11.0) and moderate salinity (0–5% NaCl) was isolated from cattle shed of Thanjavur, India. It produced lipase, gelatinase, and polyhydroxybutyrate. Different culture conditions, incubation time, carbon and nitrogen sources, vitamins, amino acids, surfactants, and metal ions for optimal growth and protease production of P-1-1 were examined. Maximum protease (0.128 U/mL) production was achieved with 1% fructose, 1% yeast extract, 0.1% ammonium sulfate, 3% NaCl, 0.1% CaCl2 · 2H2O, 1% glycine, 0.1% vitamin E, and 0.1% Tween-40 at pH 8.0 after 42 hr of incubation at 37°C. It was active over broad range of pH (7.0–12.0), temperature (15–100°C), and salinity (0–9% NaCl) with optima at pH 10.0, 55°C, and 3% NaCl. It retained 65 and 48% activities at pH 12.0 and 100°C, respectively. Partially purified protease was highly stable (100%) within pH range 7.0–12.0 and salinities of 0–5% NaCl for 48 hr. Cu2+, Mn2+, Co2+, and Ca2+ did not inhibit its activity. Its stability at extreme pHs, temperatures, and in the presence of surfactants and commercial detergents suggests its possible application in laundry detergents. Partially purified protease was immobilized and reused. This is the first report of alkali-thermotolerant, surfactant–detergent-stable partially purified extracellular protease from A. caviae.
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