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  • Title: Characterization of intracellular esterase A from Bacillus subtilis.
    Author: Riefler JF, Higerd TB.
    Journal: Biochim Biophys Acta; 1976 Mar 11; 429(1):191-7. PubMed ID: 4118.
    Abstract:
    Esterase A (EC 3.1.1.1) obtained by sonic disruption of Bacillus subtilis SR22 (spoA12, trpC2) was purified approximately 400-fold by differential chemical and heating precipitation, DEAE-cellulose chromatography, and Bio-Rad P-150 gel filtration chromatography, with an overall yield of 59%. The purified enzyme hydrolyzed both aliphatic and aromatic acetate esters at substrate concentrations of 0.25 M but did not hydrolyze amino acid esters. Aliphatic alcohols did not inhibit the hydrolysis of p-nitrophenyl acetate; the most potent inhibitors of esterase activity were mercuric chloride, diisopropylfluorophosphate, eserine, and sodium fluoride.
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