Medium-based optimization of an organic solvent-tolerant extracellular lipase from the isolated halophilic Alkalibacillus salilacus

A haloalkaliphilic solvent-tolerant lipase was produced from Alkalibacillus salilacus within 48 h of growth in liquid medium. An overall 4.9-fold enhanced production was achieved over unoptimized media after medium optimization by statistical approaches. Plackett–Burman screening suggested lipase pr...

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Bibliographic Details
Published in:Extremophiles : life under extreme conditions 2015-09, Vol.19 (5), p.933-947
Main Authors: Samaei-Nouroozi, Amene, Rezaei, Shahla, Khoshnevis, Nika, Doosti, Mahmoud, Hajihoseini, Reza, Khoshayand, Mohammad Reza, Faramarzi, Mohammad Ali
Format: Article
Language:English
Subjects:
Alcohols - chemistry
Alkalies
Aluminum - chemistry
Bacillaceae - enzymology
Bacterial Proteins - chemistry
Bacterial Proteins - metabolism
Biochemistry
Biomedical and Life Sciences
Biotechnology
Cations
Chemical agents
Cobalt - chemistry
Enzyme Stability
Enzymes
Fatty Acids - chemistry
Life Sciences
Lipase - chemistry
Lipase - metabolism
Microbial Ecology
Microbiology
Nitrophenols - chemistry
Olea
Olive oil
Organic solvents
Original Paper
Salt-Tolerance
Sodium chloride
Solvents
Space life sciences
Substrate Specificity
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Summary:A haloalkaliphilic solvent-tolerant lipase was produced from Alkalibacillus salilacus within 48 h of growth in liquid medium. An overall 4.9-fold enhanced production was achieved over unoptimized media after medium optimization by statistical approaches. Plackett–Burman screening suggested lipase production maximally influenced by olive oil, KH 2 PO 4 , NaCl, and glucose; and response surface methodology predicted the appropriate levels of each parameter. Produced lipase was highly active and stable over broad ranges of temperature (15–65 °C), pH (4.0–11.0), and NaCl concentration (0–30 %) showing excellent thermostable, pH-stable, and halophilic properties. The enzyme was optimally active at pH 8.0 and 40 °C. Majority of cations, except some like Co 2+ and Al 3+ were positive signals for lipase activity. In addition, the presence of chemical agents and organic solvents with different log P ow was well tolerated by the enzyme. Finally, efficacy of lipase-mediated esterification of various alcohols with oleic acid in organic solvents was studied.
ISSN:1431-0651
1433-4909
DOI:10.1007/s00792-015-0769-7