Journal
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Volume 111, Issue -, Pages 1183-1193Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.ijbiomac.2018.01.152
Keywords
Esterase; Salt-tolerant; Bacillus licheniformis
Funding
- National Twelfth Five-year Science and Technology support program [2014BAD02B02]
- Sichuan Science and Technology Bureau [2014GXZ0005, 2017TJPT0001]
- National Infrastructure of Natural Resources for Science and Technology Program of China [NIMR-2016-8-1]
- Antibiotic Research and Re-evaluation Key Laboratory of Sichuan Province [ARRLKF14-04]
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Bacterial esterases and lipases, especially extremozymes attract increasing attention due to various advantages both in good properties and wide applications. In the present study, a cold-adapted, alkali-stable and highly salt-tolerant esterase (Est700) was cloned from Bacillus licheniformis, expressed and purified with a molecular mass of 25 kDa. The optimal temperature of Est700 was 30 degrees C, with 35% maximal activity retaining at 0 degrees C. Its optimal pH was 8.0 and showed high stability at pH 5.0-11.0. Noticeably, Est700 was highly activated by 3.5 M NaCl and the extent of this activation is much stronger than that of currently reported halophilic ones. It was also stable in 5 M NaCl with no activity loss. High salt concentrations changed the secondary structure and folding properties of Est700 with formation of more alpha-helix and less beta-sheet domains. With salt incubation, its melting temperature was estimated to be 57.2 degrees C, which is 12.8 degrees C higher than that of native one. Interestingly, Est700 lacks the acidic surface that is considered essential for enzyme stability at high salinity. However, it has a mainly positive surface electrostatic potential, which is probably different from most reported halotolerant esterases. These multiple properties make Est700 a valuable candidate in both basic research and industrial applications. (C) 2018 Published by Elsevier B.V.
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