Abstract:
:A carboxylesterase gene from thermophilic bacterium, Alicyclobacillus tengchongensis, was cloned and expressed in Escherichia coli BL21 (DE3). The gene coded for a 513 amino acid protein with a calculated molecular mass of 57.82 kDa. The deduced amino acid sequence had structural features highly conserved among serine hydrolases, including Ser204, Glu325, and His415 as a catalytic triad, as well as type-B carboxylesterase serine active site (FGGDPENITIGGQSAG) and type-B carboxylesterase signature 2 (EDCLYLNIWTP). The purified enzyme exhibited optimum activity with β-naphthyl acetate at 60 °C and pH 7 as well as stability at 25 °C and pH 7. One unit of the enzyme hydrolyzed 5 mg malathion l(-1) by 50 % within 25 min and 89 % within 100 min. The enzyme strongly degraded malathion and has a potential use for the detoxification of malathion residues.
journal_name
Biotechnol Lettjournal_title
Biotechnology lettersauthors
Xie Z,Xu B,Ding J,Liu L,Zhang X,Li J,Huang Zdoi
10.1007/s10529-013-1195-5subject
Has Abstractpub_date
2013-08-01 00:00:00pages
1283-9issue
8eissn
0141-5492issn
1573-6776journal_volume
35pub_type
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