首页> 外文期刊>African Journal of Biotechnology >Hydrolysis of proteinaceous tannery solid waste for the production of extracellular acidic protease by Selenomonas ruminantium
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Hydrolysis of proteinaceous tannery solid waste for the production of extracellular acidic protease by Selenomonas ruminantium

机译:反刍动物硒酸酶水解蛋白制革固体废料生产胞外酸性蛋白酶

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The objective of this?study was?to produce protease from?Selenomonas ruminantiumusing animal fleshing (ANFL), an untanned tannery solid waste as the sole protein source. Optimization of the minimal medium composition for the production of protease was carried out by a statistical approach using response surface methodology (RSM) which includes the variables such as NH4Cl, K2HPO4, KH2PO4and NaCl. The isolate was found to produce maximum protease at pH 6 and at a temperature of about 40°C. Protease was purified 56 fold with a total yield of 28.14%. The enzyme was found to be monomeric having a molecular weight around 53 kDa. The purified enzyme was stable at a pH of about 4 revealing its acid protease nature and was also found to be stable up to 40°C. The enzyme was activated by divalent cations like Ca2+?and Mg2+?and inhibited by dithiothreitol?(DTT), where the latter suggested its cysteine protease nature. The enzyme had good stability in the presence of non-ionic surfactants like tween 20, tween 40, tween 80 and triton X100 and also in the presence of solvents like methanol, ethanol and isopropanol. These characteristics reveal the potential of the enzyme for different industrial applications.
机译:这项研究的目的是利用动物肉(ANFL)(一种未经鞣制的制革厂固体废物作为唯一的蛋白质来源)从反刍动物(Selenomonas ruminantium)生产蛋白酶。用于生产蛋白酶的最小培养基组成的优化是通过使用响应面方法(RSM)的统计方法进行的,该方法包括变量如NH4Cl,K2HPO4,KH2PO4和NaCl。发现该分离物在pH 6和约40℃的温度下产生最大的蛋白酶。蛋白酶被纯化56倍,总产率为28.14%。发现该酶是分子量约为53kDa的单体。纯化的酶在约4的pH下是稳定的,显示出其酸性蛋白酶性质,并且还发现在高达40℃下是稳定的。该酶被二价阳离子如Ca2 +,Mg2 +激活,并被二硫苏糖醇(DTT)抑制,后者表明其半胱氨酸蛋白酶的性质。在非离子表面活性剂(例如吐温20,吐温40,吐温80和Triton X100)的存在下,以及在溶剂(例如甲醇,乙醇和异丙醇)的存在下,该酶具有良好的稳定性。这些特征揭示了该酶在不同工业应用中的潜力。

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