Improved production of alkaline polygalacturonate lyase by homologous overexpression pelA in Bacillus subtilis |
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Authors: | Mouyong Zou Xuezhi Li Wenjing Shi Fenfen Guo Jian Zhao Yinbo Qu |
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Institution: | State Key Laboratory of Microbial Technology, Shandong University, Ji-nan City 250100, PR China |
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Abstract: | A polygalacturonate lyase (PGL), PelA, was purified from the culture broth of Bacillus subtilis 7-3-3, with a molecular weight, optimal temperature, and pH of approximately 45 kDa, 55 °C, and 9.4, respectively. The PGL gene (pelA) was homologously overexpressed in B. subtilis 7-3-3 to increase the gene copies and enhance the PGL production. The resulting PGL activity was 2138 U mL?1 at 44 h, and the productivity reached 48.58 U (mL h)?1 through the homologous overexpression of strain B-pN-pelA in a 7.5 L fermentor, the highest PGL production compared to those reported in literature to the best of our knowledge. Crude enzyme has high PGL and PGase activity, which can remove 50.58% of pectin in unpretreatment ramie fibers at 50 °C for 4 h. Meanwhile, the enzyme system with a low level hemicellulase and almost no cellulase will further help in enhancing the efficiency of degumming besides maintaining tenacity of plant fiber. The B. subtilis B-pN-pelA shows high genetic stability and has great potential in the textile industry. |
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Keywords: | Polygalacturonate lyase Degumming Homologous overexpression |
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