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Essential Role of Gly33 in a Novel Organic Solvent-Tolerant Lipase from Serratia marcescens ECU1010 as Determined by Site-Directed Mutagenesis

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Abstract

A novel lipase lipB from Serratia marcescens ECU1010 is highly stable in the presence of organic solvents. By sequence and structure comparison with homologous lipase lipA, three amino acid residues were found to be different between them. To identify the residues which increase the organic solvent stability of lipB, residues that potentially provide this stability were mutated to the ones of lipA at equivalent positions. The replacement of Gly at position 33 by Asp obviously decreased its stability in organic solvents. Molecular modeling and structural analysis also suggested that the Gly33 residue is important for the organic solvent stability of lipB.

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Acknowledgments

This work was financially supported by the National High-tech R&D (863) Program (No. 2007AA02Z225) and the National Special Fund for State Key Laboratory of Bioreactor Engineering (no. 2060204), People’s Republic of China.

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Authors and Affiliations

  1. State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 130 Meilong Road, Shanghai, 200237, People’s Republic of China

    Su-Xia Li, Qiang Ma, Kang Lin, Jiao-Jiao Wu & Jian-He Xu

  2. Department of Biochemistry, Hamamatsu University School of Medicine, Hamamatsu, Japan

    Yi-Xin Wu

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  1. Su-Xia Li
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  2. Qiang Ma
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  3. Kang Lin
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  4. Jiao-Jiao Wu
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Correspondence to Su-Xia Li or Jian-He Xu.

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Li, SX., Ma, Q., Lin, K. et al. Essential Role of Gly33 in a Novel Organic Solvent-Tolerant Lipase from Serratia marcescens ECU1010 as Determined by Site-Directed Mutagenesis. Appl Biochem Biotechnol 172, 2945–2954 (2014). https://doi.org/10.1007/s12010-013-0690-4

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  • DOI: https://doi.org/10.1007/s12010-013-0690-4

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