Medium optimization for the production of thermal stable β-glucanase by Bacillus subtilis ZJF-1A5 using response surface methodology
Medium optimization for the production of thermal stable β-glucanase by Bacillus subtilis ZJF-1A5 using response surface methodology
复制标题
使用响应面法对枯草芽孢杆菌 ZJF-1A5 生产热稳定 β-葡聚糖酶进行培养基优化。
DOI：
10.1016/j.biortech.2003.10.013
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发表时间：
2004-06-01
影响因子：
11.4
通讯作者：
Ali, MAM
中科院分区：
文献类型：
--
作者：
Tang, XJ;He, GQ;Ali, MAM
对于枯草芽孢杆菌ZJF-1A5的细胞生长和β -葡聚糖酶的生成，大麦粉、糊精和可溶性淀粉等多糖的碳源优于葡萄糖和麦芽糖等单糖和双糖。枯草芽孢杆菌ZJF-1A5产生的β -葡聚糖酶与细胞生长部分相关，在细胞进入静止期后显著增加；酵母浸膏为最佳氮源，豆粉次之。实验中选用的无机氮源均不利于细胞生长和产酶。采用分数因子设计（2(6-2)）来阐明显著影响β -葡聚糖酶产生的培养基成分。培养基中大麦粉、玉米粉和大豆粉的浓度是显著影响因素。采用最陡爬坡法确定最佳区域，采用中心复合设计估计二次响应面，确定β -葡聚糖酶最大产量的因子水平。响应面法优化的发酵培养基组成为（g/1）：大麦粉，63.5；玉米粉，44.8；KH2PO4, 1.0 MgSO4 （.）7 h(2)啊,0.1;氯化钙,0.1。优化培养基48h β -葡聚糖酶活性为251 U/ml，比原始培养基提高1.4倍。(C) 2003 Elsevier Ltd.版权所有。
Polysaccharides, such as barley flour, dextrin and soluble starch, were better carbon sources than monosaccharides and disaccharides, such as glucose and maltose, for cell growth of Bacillus subtilis ZJF-1A5 and beta-glucanase production. beta-Glucanase produced by B. subtilis ZJF-1A5 was associated partially with cell growth and increased significantly when cells entered stationary phase; yeast extract was the best nitrogen source, followed by soybean flour. All inorganic nitrogen sources chosen in the experiments were not favorable for cell growth and enzyme production. A fractional factorial design (2(6-2)) was applied to elucidate medium components that significantly affect beta-glucanase production. The concentration of barley flour, corn flour and soybean flour in medium were significant factors. The steepest ascent method was used to locate the optimal domain and a central composite design was used to estimate the quadratic response surface from which the factor levels for maximum production of beta-glucanase were determined. The composition of fermentation medium optimized with response surface methodology was (g/1): barley flour, 63.5; corn flour, 44.8; KH2PO4, 1.0 MgSO4 (.) 7H(2)O, 0.1; CaCl2, 0.1. beta-Glucanase activity was 251 U/ml at 48 h using optimized medium, 1.4 times higher than that in original medium. (C) 2003 Elsevier Ltd. All rights reserved.