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Citation: Ren Dajun, Fu Linjun, Wu Jian, Li Sheng, Zhang Shuqin, Zhang Xaioqing. Inactivation Kinetics of Laccase under Different Reaction Systems[J]. Chemistry, ;2019, 82(5): 452-456. shu

Inactivation Kinetics of Laccase under Different Reaction Systems

School of Resources and Environmental Engineering, Wuhan University of Science and Technology, Wuhan 430081

Received Date: 19 November 2018
Accepted Date: 7 January 2019

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In this paper, the kinetic thermal activity of laccases in three systems was studied, and the kinetic parameters were analyzed accordingly. The results showed that the inactivation of laccase in pure aqueous solution accords with the first-order kinetic inactivation model, and the inactivation equation was lnA=-0.1353t-2.2522. The inactivation of laccase in the toxic organic system (2, 4-dichlorophenol and indole solution) is still in accordance with the first-order inactivation mechanical model. The inactivation rate constant is reduced, but the half-life is increased. In polar solution (ethanol solution), the reaction rate constant of laccase is the smallest, probably because the change of internal force in laccase molecule causes the laccase reaction to be slow. In the non-polar system (isooctane solution), water-hydrophobic system reduces the damage to the enzyme, which is beneficial to the stability of the enzyme and prolongs the half-life of laccase. The laccase inactivation in the polar or non-polar system is consistent with the first-order kinetic inactivation model.
- Laccase,
- Toxic organic system,
- Polar system,
- Non-polar system,
- Inactivation,
- Kinetics
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