地衣芽孢杆菌NCIM 2042产碱性蛋白酶理化条件优化的统计方法

Q2 Biochemistry, Genetics and Molecular Biology
Enzyme Research Pub Date : 2012-01-01 Epub Date: 2012-01-05 DOI:10.1155/2012/905804
Biswanath Bhunia, Apurba Dey
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引用次数: 46

摘要

采用Plackett-Burman设计和响应面法(RSM)对地衣芽孢杆菌NCIM 2042生产碱性蛋白酶的理化参数进行优化。实验验证了该模型,在最佳培养条件下,蛋白酶产量最高可达315.28 U。采用硫酸铵(60%)沉淀法纯化蛋白酶。透析样品的HPLC分析表明,保留时间为1.84 min,纯度为73.5%。在25% v/v DMSO、甲醇、乙醇、ACN、2-丙醇、苯、甲苯和己烷的存在下,37℃预孵生30分钟后,该酶保持了92%以上的初始活性。此外,在阴离子洗涤剂(Tween-80和Triton X-100)、表面活性剂(SDS)、漂白剂(过硼酸钠和过氧化氢)和抗再沉积剂(Na(2)CMC、Na(2)CO(3))的存在下,部分纯化酶在室温下表现出60 min的显著稳定性。含有10% w/v peg4000的纯化酶表现出较好的热稳定性、表面活性剂稳定性和局部洗涤剂稳定性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Statistical Approach for Optimization of Physiochemical Requirements on Alkaline Protease Production from Bacillus licheniformis NCIM 2042.

The optimization of physiochemical parameters for alkaline protease production using Bacillus licheniformis NCIM 2042 were carried out by Plackett-Burman design and response surface methodology (RSM). The model was validated experimentally and the maximum protease production was found 315.28 U using optimum culture conditions. The protease was purified using ammonium sulphate (60%) precipitation technique. The HPLC analysis of dialyzed sample showed that the retention time is 1.84 min with 73.5% purity. This enzyme retained more than 92% of its initial activity after preincubation for 30 min at 37°C in the presence of 25% v/v DMSO, methanol, ethanol, ACN, 2-propanol, benzene, toluene, and hexane. In addition, partially purified enzyme showed remarkable stability for 60 min at room temperature, in the presence of anionic detergent (Tween-80 and Triton X-100), surfactant (SDS), bleaching agent (sodium perborate and hydrogen peroxide), and anti-redeposition agents (Na(2)CMC, Na(2)CO(3)). Purified enzyme containing 10% w/v PEG 4000 showed better thermal, surfactant, and local detergent stability.

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来源期刊
Enzyme Research
Enzyme Research Biochemistry, Genetics and Molecular Biology-Biochemistry
CiteScore
4.60
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