Abstract
The genome sequence of Streptomyces coelicolor A3(2) contains 51 putative lipase and esterase genes mostly of unknown function. The gene estB (locus SCO 6966) was expressed as a His-tagged protein in E. coli. Esterase B was active at low temperatures exerting its maximum activity at 30°C and retaining more than 25% of its activity at 4°C. The optimum pH was 8–8.5. The enzyme was active against short synthetic p-nitrophenylesters (C2–C10) with maximum activity towards the acetate ester (C2). The esterase was tested on 13 series of racemic esters of potential interest for the synthesis of chiral pharmaceutical compounds. 4 of the series were substrates and a modest degree of enantioselectivity was observed (enantiomeric ratios of 1.1–1.9).
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Soror, S.H., Verma, V., Rao, R. et al. A cold-active esterase of Streptomyces coelicolor A3(2): from genome sequence to enzyme activity. J Ind Microbiol Biotechnol 34, 525–531 (2007). https://doi.org/10.1007/s10295-007-0224-6
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DOI: https://doi.org/10.1007/s10295-007-0224-6