NDLI: Production and Purification of a Solvent-Resistant Esterase from Bacillus licheniformis S-86

Content Provider	Springer Nature Link
Author	Torres, Sebastián Baigorí, Mario D. Pandey, Ashok Castro, Guillermo R.
Copyright Year	2008
Abstract	New thermophilic and organic-solvent-tolerant Bacillus licheniformis S-86 strain is able to produce two active and solvent-stable esterases. Production of type I and II esterases was substantially enhanced when oils and surfactants were supplied as carbon sources. Grape oil (0.1% v/v) and Tween 20 to 60 (0.1% v/v) had enhanced enzyme production between 1.6- and 2.2-folds. Type II esterase was purified to homogeneity in a five-step procedure. This esterase was purified 76.7-fold with a specific activity of 135 U mg$^{−1}$. Molecular mass of the enzyme was estimated to be 38.4 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Type II esterase was active mostly on esters with short acyl chains, which allowed to classify the enzyme as a carboxylesterase with a K $_{m}$ of 80.2 mmol l$^{−1}$ and a V $_{max}$ of 256.4 μmol min$^{−1}$ mg$^{−1}$ for p-nitrophenyl acetate. Also, B. licheniformis S-86 type II esterase displayed activity in presence of water-miscible organic solvents at 50% concentration and stability after 1-h incubation.
Starting Page	221
Ending Page	232
Page Count	12
File Format	PDF
ISSN	02732289
Journal	Applied Biochemistry and Biotechnology
Volume Number	151
Issue Number	2-3
e-ISSN	15590291
Language	English
Publisher	Humana Press Inc
Publisher Date	2008-06-10
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Esterases B. licheniformis Production Purification Enzyme characterization Detergents Oils Biochemistry Biotechnology
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Environmental Engineering Biochemistry Bioengineering Applied Microbiology and Biotechnology Biotechnology

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