Paper Report for: Takehara_2012_Biosci.Biotechnol.Biochem_76_1721
Reference
Title: A novel alkaline esterase from Sporosarcina sp. nov. strain eSP04 catalyzing the hydrolysis of a wide variety of aryl-carboxylic acid esters Takehara M, Kinoshita K, Miyamoto M, Hirohara H Ref: Biosci Biotechnol Biochem, 76:1721, 2012 : PubMed
A novel esterase showing activity specific for esters of aryl-carboxylic acids was discovered in Sporosarcina sp. nov., which was identified by the 16S rDNA sequencing method in addition to morphological and physiological analyses. The aryl-carboxylesterase (named EstAC) was purified 780-fold from crude cell extracts by a 5-step procedure. EstAC was characterized as a monomeric protein with a molecular weight of 43,000, an optimum pH of around 9.0, and an optimum temperature of 40 degrees C. The pH optimum and the effects of inhibitors together with an internal amino acid sequence suggested that EstAC is a member of family VIII esterases. EstAC was found to be highly active on a wide variety of substrates such as alkyl benzoates, alkyl phenylacetates, ethyl alpha- or beta-substituted phenylpropionates, dialkyl terephthalates, dimethyl isophthalate, and ethylene glycol dibenzoate. However, monomethyl terephthalate was not hydrolyzed. It was suggested that EstAC had 4-hydroxybenzoyl and cinnamoyl esterase activities as well.
Comment
beta-lactamase C not alpha/beta hydrolase family VIII
Takehara M, Kinoshita K, Miyamoto M, Hirohara H (2012) A novel alkaline esterase from Sporosarcina sp. nov. strain eSP04 catalyzing the hydrolysis of a wide variety of aryl-carboxylic acid esters Biosci Biotechnol Biochem76: 1721-7
Takehara M, Kinoshita K, Miyamoto M, Hirohara H (2012) Biosci Biotechnol Biochem76: 1721-7
