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首页> 外文期刊>World journal of agricultural sciences >Characterization of a Feather Degrading by Bacillus amyloliquefaciens Protease: A New Strain
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Characterization of a Feather Degrading by Bacillus amyloliquefaciens Protease: A New Strain

机译:由解淀粉芽孢杆菌蛋白酶降解的羽毛的表征:一种新菌株。

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摘要

Feathers are rich in aminoacids and can be employed as a dietary protein supplement for animal feed. Microbial degradation of feathers (keratinase) represents an alternative technology for improving their nutritional value. The strain Bacillus amyloliquefaciens isolated of poultry processing plant, showed efficient for application in biotechnological processes. Optimum pH and temperature for the enzyme were 8.0 and 50 degree C, respectively. Enzyme activity was significantly inhibited by EDTA (50mM). Strong activation occurred when the enzyme was incubated with mercaptoethanol (0.1 and 0.5% w/v), resulting in a proteolytic and keratinolytic relative activity of 838 and 197 percent, respectively. The addition of triton at concentrations of 0.1 and 0.5 percent (w/v) also favored enzyme proteolytic activity, resulting in a 97 percent increase when incubated in 0.1% triton (w/v). The enzyme produced by Bacillus amyoliquefaciens exhibited activity in base pH and 50 degree C and was active in presence of different metals.
机译:羽毛富含氨基酸,可用作动物饲料的膳食蛋白质补充剂。羽毛的微生物降解(角蛋白酶)是提高其营养价值的另一种技术。从家禽加工厂分离出的解淀粉芽孢杆菌菌株显示出在生物技术过程中的有效应用。该酶的最佳pH和温度分别为8.0和50摄氏度。 EDTA(50mM)明显抑制了酶的活性。当将酶与巯基乙醇(0.1和0.5%w / v)一起孵育时,发生了强烈的激活,从而导致蛋白水解和角蛋白水解的相对活性分别为838%和197%。以0.1%和0.5%(w / v)的浓度添加triton也有利于酶的蛋白水解活性,当在0.1%triton(w / v)中孵育时导致97%的增加。由淀粉芽孢杆菌产生的酶在碱性pH和50℃下表现出活性,并且在不同金属的存在下具有活性。

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