A cold-active esterase of Streptomyces coelicolor A3(2): from genome sequence to enzyme activity

作者：Soror Sameh H; Verma V; Rao Ren; Rasool Shafaq; Koul S; Qazi G N; Cullum John^*

来源：Journal of Industrial Microbiology and Biotechnology, 2007, 34(8): 525-531.

DOI：10.1007/s10295-007-0224-6

• Streptomyces coelicolor
• esterases
• cold-active enzyme
• enantioselectivity

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 degrees C and retaining more than 25% of its activity at 4 degrees C. The optimum pH was 8-8.5. The enzyme was active against short synthetic p- nitrophenylesters (C-2-C-10) with maximum activity towards the acetate ester (C-2). 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).

• 出版日期2007-8