期刊
FEMS MICROBIOLOGY LETTERS
卷 362, 期 10, 页码 -出版社
OXFORD UNIV PRESS
DOI: 10.1093/femsle/fnv054
关键词
alginate lyase; carbohydrate-binding module; catalytic activity; thermostability; product distribution
类别
资金
- National High-tech R&D Program of China [2014AA093504]
- National Natural Science Foundation of China [31000361, 41376144]
- Special Fund for Marine Scientific Research in the Public Interest [201105027-3, 201005024]
The carbohydrate-binding module (CBM) in polysaccharide hydrolases plays a key role in the hydrolysis of cellulose, xylan and chitin. However, the function of CBM in alginate lyases has not been elucidated. A new alginate lyase gene, alyL2, was cloned from the marine bacterium Agarivorans sp. L11 by using degenerate and site-finding PCR. The alginate lyase, AlyL2, contained an N-terminal CBM13 and a C-terminal catalytic family 7 polysaccharide lyase (PL7) module. To better understand the function of CBM13 in alginate lyase AlyL2, the full-length enzyme (AlyL2-FL) and its catalytic module (AlyL2-CM) were expressed in Escherichia coli and characterized. The specific activity and catalytic efficiency of AlyL2-FL were approximately twice those of AlyL2-CM. The half-lives of AlyL2-FL were 4.7-6.6 times those of AlyL2-CM at 30-50 degrees C. In addition, the presence of CBM13 in AlyL2 changed its substrate preference and increased the percentage of disaccharides from 50.5% to 64.6% in the total products. This first report of the function of CBM13 in alginate lyase provides new insights into the degradation of alginate by marine microorganisms.
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