一株新分离枯草芽孢杆菌葡聚糖酶的鉴定和过表达

Houda Hmani, L. Daoud, M. Ali, Adel Haj Brahim, Mouna Jlidi, S. Bejar, Mamdouh Ben Ali
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引用次数: 0

摘要

葡聚糖酶是水解谷物细胞壁主要成分葡聚糖的酶。新分离的细菌被命名为枯草芽孢杆菌HB2,产生一种分子量为75 kDa的单体葡聚糖酶(GLU HB2)。GLU HB2在pH 5和55℃条件下具有最佳活性。它在广泛的pH范围和高达65°C的温度下非常稳定,存在5mm的CaCl2。为了克服野生型菌株存在的酶抑制问题,将GluHB2基因整合到枯草芽孢杆菌HB2基因组中,重组菌株命名为HB2G。葡萄糖酶产量与细菌生长的相关性表明,HB2G的表达水平仍然很低,与野生型菌株相对相当。但就生产力而言,HB2G菌株在整个细菌培养过程中都具有更高的生产力。重组菌株的低产量和生长可归因于在组成启动子下葡聚糖酶基因的过度表达的毒性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Characterization and overexpression of a glucanase from a newly isolated B. subtilis strain
Glucanases are enzymes that hydrolysis glucans which are the major cell wall components in cereals. Newly isolated bacteria assigned as Bacillus subtilis HB2, produces a monomeric glucanase (GLU HB2) of a molecular mass of 75 kDa. GLU HB2 has an optimal activity at pH 5 and 55 °C. It is extremely stable at a broad range of pH and temperature up to 65 °C, in presence of 5 mM of CaCl2. In order to overcome the enzymatic inhibition problem observed in wild-type strains, GluHB2 gene was integrated into the genome of B. subtilis HB2 and the recombinant strain was named HB2G. The correlation of glucanase production with bacterial growth shows that the level of expression of HB2G remains low and relatively comparable to the wild-type strain. But in terms of productivity, the HB2G strain is more productive throughout bacterial culture. This low production and growth of the recombinant strain can be attributed to the toxicity of the overexpression of the glucanase gene under a constitutive promoter.
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