Cloning,Expression, Purification,and Characterization of a Novel Esterase from <Emphasis Type="Italic">Lactobacillus plantarum</Emphasis> |
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Authors: | Fábio Cristiano Angonesi Brod Javier Vernal Jean Borges Bertoldo Hernán Terenzi Ana Carolina Maisonnave Arisi |
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Institution: | 1.Department of Food Science and Technology,Universidade Federal de Santa Catarina,Florianópolis,Brazil;2.Departmento de Bioquímica,Universidade Federal de Santa Catarina,Florianópolis,Brazil |
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Abstract: | Lactobacillus plantarum is an important lactic acid bacterium, usually found as natural inhabitant of food, such as fermented vegetables and meat
products. However, little information about lactic acid bacteria, especially concerning L. plantarum, as a source of useful enzymes has been reported. The aim of this study was to clone, express in Escherichia coli, purify, and characterize an esterase from L. plantarum ATCC 8014. The esterase gene (1014 bp) was amplified and cloned in pET14b expression vector to express a His6-tagged protein in E. coli. Recombinant L. plantarum esterase was purified by Ni-NTA resin, presenting an apparent molecular mass of about 38 kDa. It presented highest activity
at pH 6.0 and 40°C. Also, it presented preference for p-nitrophenyl butyrate, but hydrolyzed more efficiently p-nitrophenyl acetate. Besides, this study shows, for the first time, CD data about secondary structure of an esterase from
L. plantarum. |
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