PRODUCTION AND CHARACTERIZATION OF PARTIALLY PURIFIED EXTRACELLULAR THERMOSTABLE α-AMYLASE BY Bacillus subtilis IN SUBMERGED FERMENTATION (SmF)
PRODUCTION AND CHARACTERIZATION OF PARTIALLY PURIFIED EXTRACELLULAR THERMOSTABLE α-AMYLASE BY Bacillus subtilis IN SUBMERGED FERMENTATION (SmF)
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DOI：
10.1080/10826068.2011.552142
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发表时间：
2011-10
影响因子：
2.9
通讯作者：
S. Özdemir;Fatma Matpan;K. Güven;Zübeyde Baysal
中科院分区：
文献类型：
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作者：
S. Özdemir;Fatma Matpan;K. Güven;Zübeyde Baysal
从Dicle大学校园土壤样品中分离到一株芽孢杆菌。根据16 S核糖体RNA序列分析，该微生物与枯草芽孢杆菌（Bacillus subtilis）亲缘关系最近。研究了不同培养基、培养时间、碳源和氮源、不同淀粉、面粉和化学品对α-淀粉酶产生的影响。在含0.05%吐温40的基础培养基A中，24 h酶产量最高，达7516 U/mL。部分纯化的酶在60°C下显示最大活性，最适pH为6.0。研究了0.2%洗涤剂（十二烷基硫酸钠[SDS]、CHAPS [3-[（3-胆酰胺丙基）二甲铵]-1-丙磺酸盐]和商业洗涤剂Omo Matic）在一段时间（15-150 min）内对部分纯化的酶活性的影响，发现抑制效果从大到小的顺序为SDS > Omo Matic > CHAPS。不同金属离子在低浓度（1.5 mM）下抑制α-淀粉酶活性。Co ~（2+）对酶活性有轻度抑制作用，Hg ~（2+）和Cd ~（2+）对酶活性有较强的抑制作用，Ca ~（2+）和Mg ~（2+）对酶活性有促进作用。在20 mM时，Ca 2+增强酶活性，并研究了不同Ca 2+浓度（10-300 mM）。
A Bacillus strain was isolated from soil samples from the campus area of Dicle University. Based on 16S ribosomal RNA sequencing, the microorganism was closely related to Bacillus subtilis. Effects of different culture medium, incubation time, carbon and nitrogen sources, and various starches, flours, and chemicals on α-amylase production were examined. Maximum enzyme production (7516 U/mL) was obtained in a basal medium A containing 0.05% Tween 40 in 24 h. Partially purified enzyme showed maximum activity at 60°C with an optimum pH of 6.0. The effects of 0.2% detergents (sodium dodecyl sulfate [SDS], CHAPS [3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate], and commercial detergent Omo Matic) on partially purified enzyme activity over a period of time (15–150 min) were examined and the order of inhibition effect from the most to the least was found as SDS > Omo Matic > CHAPS. Different metal ions inhibited α-amylase activity at low concentrations (1.5 mM). Co2+ was a mild inhibitor and Hg2+ and Cd2+ were potent inhibitors, whereas Ca2+ and Mg2+ increased the enzyme activity. At 20 mM, Ca2+ enhanced enzyme activity, and different Ca2+ concentrations (10–300 mM) were studied.