Soror Sameh H, Verma V, Rao Ren, Rasool Shafaq, Koul S, Qazi G N, Cullum John
LB Genetik University of Kaiserslautern, Postfach 3049, 67653 Kaiserslautern, Germany.
J Ind Microbiol Biotechnol. 2007 Aug;34(8):525-31. doi: 10.1007/s10295-007-0224-6.
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 (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).
天蓝色链霉菌A3(2)的基因组序列包含51个推定的脂肪酶和酯酶基因,其功能大多未知。estB基因(基因座SCO 6966)在大肠杆菌中表达为带His标签的蛋白。酯酶B在低温下具有活性,在30℃时发挥最大活性,在4℃时保留超过25%的活性。最适pH为8 - 8.5。该酶对短链合成对硝基苯酯(C2 - C10)有活性,对乙酸酯(C2)的活性最高。对13个系列可能对手性药物化合物合成有潜在意义的外消旋酯进行了该酯酶的测试。其中4个系列是底物,观察到了一定程度的对映体选择性(对映体比率为1.1 - 1.9)。