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Catalytic characteristics of plant-esterase from wheat flour

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Abstract

A plant-esterase extracted from wheat flour and purified with a PEG1000/NaH2PO4 aqueous two-phase system was characterized for its catalytic characteristics. The optimal condition for plant-esterase to catalyze 1-naphthyl acetate was at 30°C, pH 6.5. It kept stability at 20°C during 120 min and at pH 5.5 during 60 h. The effects of metal ions, chemical modification reagents and pesticides on plant-esterase activity were investigated. It was found that Ba2+ and Pb2+ at concentrations of 20 mM significantly inhibited the activity of plant-esterase while Mg2+, Ca2+ and Fe2+ at the same concentration enhanced the enzyme activity. Chemical modification reagents significantly influenced the activity of plant-esterase. Particularly, PMSF (4.5 mM) and N-bromosuccinimide (11 mM) inhibited by 5.40–19.87% of the enzyme activity. It is implied that serine and tryptophan are related to the enzyme activity. Plant-esterase were displayed concentration-dependent inhibition by dichlorvos, carbofuran and carbendazim (IC50 = 0.31–63.12 ppm). All these results indicated that catalytic efficiency of plant-esterase strongly depends on reaction conditions, activity effectors and amino acid residues at the active site. It makes meaningful guidance on further design of sensing material in monitoring pesticides.

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Acknowledgments

This work was supported by the National Natural Science Foundation of China (No. 30770568), Fundamental Research Funds for the Central Universities (No. CDJXS11231178), Commissioner Program of the Ministry of Science and Technology (No. 2009GJF10041), Key Laboratory Program of Sichuan Province, China (No. NJ 2009-04), Research Program of General Administration of Quality Supervision, Inspection and Quarantine of the People’s Republic of China (No. 2011IK254), and Project supported by the National Science Foundation for Post-doctoral Scientists of China (Grant No. 20080440702).

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  1. Key Laboratory of Biorheology Science and Technology of Ministry of Education, College of Bioengineering, Chongqing University, Shazheng Ave. 174, Chongqing, 400030, People’s Republic of China

    Chang-jun Hou, Kun He, Li-min Yang, Dan-qun Huo, Mei Yang, Shun Huang & Liang Zhang

  2. Luzhou Laojiao Group Co. Ltd., Sichuan, 646000, People’s Republic of China

    Liang Zhang & Cai-hong Shen

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  1. Chang-jun Hou
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  2. Kun He
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  3. Li-min Yang
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  4. Dan-qun Huo
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Correspondence to Chang-jun Hou.

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Hou, Cj., He, K., Yang, Lm. et al. Catalytic characteristics of plant-esterase from wheat flour. World J Microbiol Biotechnol 28, 541–548 (2012). https://doi.org/10.1007/s11274-011-0845-9

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  • DOI: https://doi.org/10.1007/s11274-011-0845-9

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