CLONING, EXPRESSION, BIOCHEMICAL PARTIAL CHARATERIZATION AND MODELING OF ESTERASE FROM ACINETOBACTER CALCOACETICUS SP DSM587
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Published:
Jun 19, 2020
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Abstract
The aim of this paper has been to clone, express, purify and characterization the EstB from
Acinetobacter calcoaceticus encoded by the gen X8895. The esterase was cloned in Pet28a and
partially purified. The molecular mass of the purified enzyme was 36 kDa (by SDS) and 68.9
KDa (by gel filtration chromatography). The EstB showed a maximum activity at 35ºC and pH 8
and towards shorter acyl chain lengths (PNPA, PNPB, PNPC) and showed activity about Smethyltiobutanoate,
too. The catalytic triad has been predicted by aminoacid sequence
alignment and the structure modeling was performed used esterase 1QoR as template.
Acinetobacter calcoaceticus encoded by the gen X8895. The esterase was cloned in Pet28a and
partially purified. The molecular mass of the purified enzyme was 36 kDa (by SDS) and 68.9
KDa (by gel filtration chromatography). The EstB showed a maximum activity at 35ºC and pH 8
and towards shorter acyl chain lengths (PNPA, PNPB, PNPC) and showed activity about Smethyltiobutanoate,
too. The catalytic triad has been predicted by aminoacid sequence
alignment and the structure modeling was performed used esterase 1QoR as template.
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How to Cite
Navarro-González, I. (2020). CLONING, EXPRESSION, BIOCHEMICAL PARTIAL CHARATERIZATION AND MODELING OF ESTERASE FROM ACINETOBACTER CALCOACETICUS SP DSM587. BIOCYT Biología Ciencia Y Tecnología, 6. https://doi.org/10.22201/fesi.20072082.2013.6.76113