New function of laccase from Trametes sp.SQ01:transforming 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
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Supported by the National Natural Science Foundation of China (3080030) and by the High-tech Industrialization Projects of Universities of Shanxi Province (2012002)

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    Abstract:

    Abstract:[Objective] To study the transformation of 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoates (HOPDAs) by laccase from Trametes sp.SQ01 so to further understand the new catalytic properties of laccase and solve the problem of accumulations of HOPDAs in polychlorinated biphenyls (PCBs) degradation. [Methods] With UV-vis spectrophotometer,we studied the transformations of 8 substituted HOPDAs by laccase,and measured the steady-state kinetics parameters of laccase against parts of HOPDAs.[Results] Laccase catalyzed HOPDAs to colorless substances without any mediators; among them,especially 3,8,11-3Cl HOPDA that was barely transformed by 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase (BphD) and Rhodococcus sp.R04,also could be transformed by this laccase.The analysis of the steady-state kinetics indicated that 10-Cl HOPDA was the optimal substrate of laccase among 5 HOPDAs,and the Km was lower than that of HOPDA and 8-Cl HOPDA.Although 3,10-2F HOPDA was not the optimal substrate (Km=17.02 μmol/L),its transformation efficiency (kcat/Km) was the highest.[Conclusion]Laccase from Trametes sp. SQ01could transform various HOPDAs effectively,and has its potential in eliminating PCB pollution.

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Xiuqing Yang, Xiaowei Wen. New function of laccase from Trametes sp.SQ01:transforming 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate. [J]. Acta Microbiologica Sinica, 2014, 54(8): 913-918

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History
  • Received:February 28,2014
  • Revised:May 05,2014
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  • Online: July 24,2014
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