Skip to main content
Log in

Studies on the reaction between Laccase ando-methoxyphenol by microcalorimetry

  • Letter
  • Published:
Wuhan University Journal of Natural Sciences

Abstract

The reaction between Laccase ando-methoxyphenol have been studied by LKB-2107 batch microcalorimetry system. Thermodynamic parameters Δ r H m , ΔG o , ΔG T and kinetic parameters (K m ,k 2) have been determined. The process of the reaction has been analyzed from changes in energy by using the transition state theory. Two methods for enhancing catalytic power of Laccase are proposed. The results shown that formation of an enzyme-substrate complex is “anticatalytic”. The enter and sole source of catalytic power is the stabilization of transition state; reactant-state interactions are by nature inhibitory and only waste catalytic power.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

References

  1. Liu J S, Zeng X C, Deng Y,et al. Reduced extent method for thermokinetics.Acta Chinica Sinica, 1994,52:767–773

    Google Scholar 

  2. Bohmhammel K, Hüttl R, Pritzkat K,et al. Calorimetric investigation into enzyme catalyzed glucose oxidation.Thermochim Acta, 1993,217:1–7.

    Article  Google Scholar 

  3. Holwerda R A, Gray H B. Mechanistic studies of the reduction of rhus vernicifera laccase by hydroquinone.J Am Chem Soc, 1974,96:6008–6018

    Article  Google Scholar 

  4. Cole J L, Bollou D P, Solomon E I. Spectroscopic and chemical studies of the ascorbate oxidase trinuclear copper active site: comparison to laccase.J Am Chem Soc, 1991,113:8544–8546

    Article  Google Scholar 

  5. Andreasson L E, Reinhammar B. Kinetic studies of rhus vernicifera laccase role of the metal centers in electron transfer.Biochim Biophys Acta, 1976,445:579–593

    Google Scholar 

  6. Wu D Q, Mei F M, Qu S S,et al. Study on thermokinetic properties of the reaction between laccase and hydroquinone.Thermochim Acta, 1990,167:203–208

    Article  Google Scholar 

  7. Du Y M. Recent advance in study of Chinese Lacquer.Chinese Chem Bull, 1986,1(1):1–9

    Google Scholar 

  8. Fersht A.Enzyme structure and mechanism, Second Edition. New York: W H Freeman, 1985, 311

    Google Scholar 

  9. Richard W. Analog approaches to the structure of the transition state in enzyme reactions.Accounts Chem Research, 1972,5:10–17

    Article  Google Scholar 

  10. Menger F M. Analysis of ground-state and transition-state effects in enzyme catalysis.Biochemistry, 1992,31:5368–5373

    Article  Google Scholar 

  11. Khmelnitsk Yurii L, Stphabie H, Welch D S,et al., Salts dramatically enhance activity of enzymes suspended in organic solvents.J Am Chem Soc, 1994,116: 2647–2648

    Article  Google Scholar 

  12. Khmelnitsk Yurii L, Mozhaev V V, Belova A B,et al. Denaturation capacity: a new quantitative citerion for selection of organic solvents as reaction media in biocatalysis.Eur J Biochem, 1991,198:31–41.

    Article  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Additional information

Supported by the National Natural Science Foundation of China

Wang Tianzhi: born in 1968. Ph D

Rights and permissions

Reprints and permissions

About this article

Cite this article

Tianzhi, W., Weiping, L., Dingquan, W. et al. Studies on the reaction between Laccase ando-methoxyphenol by microcalorimetry. Wuhan Univ. J. Nat. Sci. 2, 511–513 (1997). https://doi.org/10.1007/BF02830271

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF02830271

Key words

Navigation