期刊
BIOTECHNOLOGY LETTERS
卷 37, 期 3, 页码 665-671出版社
SPRINGER
DOI: 10.1007/s10529-014-1706-z
关键词
Biofuel; Cloning; Monomeric sugar acid; Oligoalginate lyase OalS17; Shewanella sp Kz7
资金
- Special Fund for Marine Scientific Research in the Public Interest [201105027-3]
- National High-tech R&D Program of China [2011AA09070304]
- National Natural Science Foundation of China [41376144]
- Key Technologies Research and Development Program of China [2013BAB01B02]
Is to report an oligoalginate lyase with high enzymatic activity and high-level expression. Using site-finding PCR and degenerate PCR, a gene (designated oalS17) encoding a new oligoalginate lyase was cloned from Shewanella sp. Kz7 and expressed in Escherichia coli. The gene consisted of 2,292 bp with deduced amino acid size of 763 including a putative signal peptide of 44 amino acid residues belonging to polysaccharide lyase (PL) family 17. The recombinant protein was most active at 50 A degrees C and pH 6.2 in 50 mM phosphate buffer. It degraded alginate more efficiently than polyM and polyG block into a monomeric sugar acid, with a specific activity of 32 U mg(-1) toward alginate, 24 U mg(-1) toward polyM and 5 U mg(-1) toward polyG. With the high-level expression and high enzymatic activity, the recombinant oligoalginate lyase OalS17 could be a potential enzyme for further research on alginate saccharification and biofuels production.
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