Purification，Spectroscopic and Thermodynamic Characterization of Metallo-β-Lactamase L1 from Stenotrophomonas maltophilia

Hui-Zhou GAO; Xiao-Yan YAN; Qi YANG; Xia YANG; Ji-Li FENG; Sheng-Li GAO; Ke-Wu YANG

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Purification，Spectroscopic and Thermodynamic Characterization of Metallo-β-Lactamase L1 from Stenotrophomonas maltophilia

Hui-Zhou GAO #,Xiao-Yan YAN,Qi YANG,Xia YANG,Ji-Li FENG,Sheng-Li GAO,Ke-Wu YANG *

Key Laboratory of Synthetic and Natural Functional Molecule Chemistry of Ministry of Education College of Chemistry and Materials Science, Northwest University

*Correspondence author

#Submitted by

Subject:

Funding: China Provincial Bureau of Foreign Experts Affairs （No.No. SLZ2008013）, Natural Science Foundation of China （No.No. 20972127）

Opened online:26 September 2010

Accepted by: none

Citation: Hui-Zhou GAO,Xiao-Yan YAN,Qi YANG.Purification，Spectroscopic and Thermodynamic Characterization of Metallo-β-Lactamase L1 from Stenotrophomonas maltophilia[OL]. [26 September 2010] http://en.paper.edu.cn/en_releasepaper/content/4386049

In an effort to probe the antibiotic resistance in bacteria, metallo-β-lactamase L1 from stenotrophomonas maltophilia was overexpressed in Escherichia coli, purified by ion-exchange chromatography and characterized by mass spectroscopy, fluorescence and sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The matrix-assisted laser desorption ionization and time-of-flight (MALDI-TOF) mass spectroscopy result shows that a monomeric molecular mass of L1 is 28.8 kDa. This paper first report the determination of the thermodynamic enthalpy change of L1-catalyzed hydrolysis reaction of penicillin G and the enthalpy change value in average at 298.15K is 76.8 kJ/mol.

Keywords:Antibiotic resistance in bacteria, metallo-β-Lactamase L1, overexpression and purification, characterization, thermodynamics

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