A cold-active esterase of Streptomyces coelicolor A3(2): from genome sequence to enzyme activity |
| |
Authors: | Sameh H. Soror V. Verma Ren Rao Shafaq Rasool S. Koul G. N. Qazi John Cullum |
| |
Affiliation: | (1) LB Genetik University of Kaiserslautern, Postfach 3049, 67653 Kaiserslautern, Germany;(2) Biotechnology Regional Research Laboratory (CSIR), Canal Road, JammuTawi, 180001, India |
| |
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). |
| |
Keywords: | Streptomyces coelicolor Esterases Cold-active enzyme Enantioselectivity |
本文献已被 PubMed SpringerLink 等数据库收录! |