High level expression and characterization of a thermostable lysophospholipase from Thermococcus kodakarensis KOD1
作者： Zhicheng Cui , Yuhan Wang , Bang Phuong Pham , Fangfang Ping , Hongyu Pan
DOI: 10.1007/S00792-012-0461-0
关键词: Enzyme 、 Phosphodiester bond 、 Catalytic triad 、 Lysophospholipase 、 Biology 、 Hydrolysis 、 Molecular mass 、 Biochemistry 、 Thermococcus kodakarensis 、 Peptide sequence
摘要: Phospholipases can catalyze the hydrolysis of one or more ester and phosphodiester bonds have a considerable interest in food, oil leather pharmaceutical industries. In this report, lysophospholipase gene from hyperthermophilic archaeon Thermococcus kodakarensis KOD1 (LysoPL-tk) was cloned. The 783 bp encodes 260-amino acid protein with molecular mass 29 kDa. LysoPL-tk has consensus motif (GxSxG) catalytic triad (S, D, H) esterases deduced amino sequence. expressed Escherichia coli purified to homogeneity. enzyme degrade substrates both short long acyl chain lengths. apparent K m value for p-nitrophenyl butyrate 607.1 μM V max values 95.5 U/mg. active at broad range pH (5–8) temperatures (70–95 °C) optimum temperature being 8.0 85 °C, respectively. high yield, substrate along its thermo-stability indicates that is potential industrial application.
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