Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10235783 | Process Biochemistry | 2013 | 8 Pages |
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 mLâ1 at 44 h, and the productivity reached 48.58 U (mL h)â1 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.
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Bioengineering
Authors
Mouyong Zou, Xuezhi Li, Wenjing Shi, Fenfen Guo, Jian Zhao, Yinbo Qu,