Journal
CHINESE JOURNAL OF CATALYSIS
Volume 39, Issue 5, Pages 937-945Publisher
SCIENCE PRESS
DOI: 10.1016/S1872-2067(18)63033-5
Keywords
Lipase; Paenibacillus pasadenensis CS0611; Expression; Characterization; Organic solvent tolerant
Funding
- National Natural Science Foundation of China [21336002, 21376096, 21676104]
- Program of State Key Laboratory of Pulp and Paper Engineering [2017ZD05]
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We found a novel lipase gene in the Paenibacillus pasadenensis CS0611 strain. The lipase gene sequence was cloned into the pET-28a expression vector to construct a recombinant lipase protein containing 6 x His tags at the C- and N-termini, respectively. High-level expression of the lipase in E.coli BL21 (DE3) was obtained upon induction with IPTG at 20 degrees C. The recombinant lipase activity was approximately 1631-fold higher than the wild type. His-tagged recombinant lipase was purified rapidly and efficiently by using Ni-charged affinity chromatography with 63.5% recovery and a purification factor of 10.78. The purified lipase was stable in a broad range of temperatures and pH values, with the optimal temperature and pH being 50 degrees C and 7.0, respectively. Its activity was stimulated to different degrees in the presence of metal ions such as Ca2+, Mg2+, and some non-ionic surfactants. In addition, the purified lipase was activated by a series of water-miscible organic solvents such as some short carbon chain alcohols and was highly tolerant to some water-immiscible organic solvents. (C) 2018, Dalian Institute of Chemical Physics, Chinese Academy of Sciences. Published by Elsevier B.V. All rights reserved.
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