Abstract：
:An intracellular esterase (BCE) from Bacillus cereus WZZ006 was purified to homogeneity with an 89.5-fold purification, specific activity of 1.79 U/mg, and 26.7% recovery. The estimated molecular weight of BCE was 96 kDa which was analyzed by SDS-PAGE and MALDI-TOF-MS. Activity staining denotes that BCE has an unexplored new carboxyl esterase characteristic. BCE enzyme activity was maximum at pH 8.5 and also at 50 °C with pNP-caproate as a substrate. This indicates that the studied BCE as a thermoalkaliphilic esterase. The kinetic properties like Km, Vmax, kcat and kcat/Km value for BCE was found to be 0.98 mM, 0.03 mM/min, 69.47 min-1 and 70.89 mM-1 min-1, respectively. Synthesis of (S)-5-chloro-1-oxo-2,3-dihydro-2-hydroxy-1H-indole-2-carboxylic acid methyl ester ((S)-CODHCM) by BCE can be shortened to 3 h compared to 36 h with whole-cell catalysis. The e.e.s achieved was 93.83%, and conversion around 52.78% with E being 39.95. These features render BCE as a promising biocatalyst for the synthesis of a key chiral intermediate for indoxacarb.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Zhang H,Xia Y,Zhou M,Zheng J,Wang Z,Zhang Ydoi
10.1016/j.ijbiomac.2019.08.140subject
Has Abstractpub_date
2019-11-01 00:00:00pages
358-367eissn
0141-8130issn
1879-0003pii
S0141-8130(19)33938-8journal_volume
140pub_type
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