Effect of polyhydroxyl compounds on the thermal stability and structure of laccase

• Autorzy: Kang C. , Ren D. , Zhang S. , Zhang X. , He X. , Deng Z. , Huang C. , Guo H.
• Języki publikacji: EN

Abstrakty

EN

In this study, glucose, inositol, glycerol, and sorbitol have been chosen as chemical modifiers to enhance laccase stability. The regularity of laccase activity variations was studied at different temperatures. Low concentrations of four polyhydroxyl compounds can improve the thermal stability of laccase at the whole temperature gradient (20~60ºC). The effect of glycerol is best in the all additives, and the relative enzyme activity of laccase increased 1.35 times by glycerol, in the concentration of 0.6 mol/L. The conformation of modified laccase is characterized by UV, fluorescence and circular dichroism. The result shows that the polyhydroxy compounds can change the conformation of laccase by increasing the hydrogen bonds between the laccase molecules and prevent the adverse change due to the increase of temperature in the secondary structure of laccase. Therefore, low concentrations of polyhydroxy compounds could be served as an additive to improve the thermal stability of the laccase.

• Wydawca: -
• Czasopismo: Polish Journal of Environmental Studies
• Rocznik: 2019
• Tom: 28
• Numer: 5
• Opis fizyczny: p.3253-3259,fig.,ref.

Twórcy

autor

Kang C.

• College of Resource and Environmental Engineering, Wuhan University of Science and Technology, Wuhan, China
• Hubei Key Laboratory for Efficient Utilization and Agglomeration of Metallurgic Mineral Resources, Wuhan University of Science and Technology, Wuhan, Hubei, China

autor

Ren D.

• College of Resource and Environmental Engineering, Wuhan University of Science and Technology, Wuhan, China
• Hubei Key Laboratory for Efficient Utilization and Agglomeration of Metallurgic Mineral Resources, Wuhan University of Science and Technology, Wuhan, Hubei, China

autor

Zhang S.

• College of Resource and Environmental Engineering, Wuhan University of Science and Technology, Wuhan, China
• Hubei Key Laboratory for Efficient Utilization and Agglomeration of Metallurgic Mineral Resources, Wuhan University of Science and Technology, Wuhan, Hubei, China

autor

Zhang X.

• College of Resource and Environmental Engineering, Wuhan University of Science and Technology, Wuhan, China
• Hubei Key Laboratory for Efficient Utilization and Agglomeration of Metallurgic Mineral Resources, Wuhan University of Science and Technology, Wuhan, Hubei, China

autor

He X.

• College of Resource and Environmental Engineering, Wuhan University of Science and Technology, Wuhan, China
• Hubei Key Laboratory for Efficient Utilization and Agglomeration of Metallurgic Mineral Resources, Wuhan University of Science and Technology, Wuhan, Hubei, China

autor

Deng Z.

• College of Resource and Environmental Engineering, Wuhan University of Science and Technology, Wuhan, China
• Hubei Key Laboratory for Efficient Utilization and Agglomeration of Metallurgic Mineral Resources, Wuhan University of Science and Technology, Wuhan, Hubei, China

autor

Huang C.

• College of Resource and Environmental Engineering, Wuhan University of Science and Technology, Wuhan, China
• Hubei Key Laboratory for Efficient Utilization and Agglomeration of Metallurgic Mineral Resources, Wuhan University of Science and Technology, Wuhan, Hubei, China

autor

Guo H.

• College of Resource and Environmental Engineering, Wuhan University of Science and Technology, Wuhan, China
• Hubei Key Laboratory for Efficient Utilization and Agglomeration of Metallurgic Mineral Resources, Wuhan University of Science and Technology, Wuhan, Hubei, China

Bibliografia

• 1. GIARDINA P., FARACO V., PEZZELLA C., PISCITELLI A., VANHULLE S., SANNIA G. Laccases: a never-ending story [J]. Cellular & Molecular Life Sciences, 67 (3), 369, 2010.
• 2. MORE S.S., RENUKA P.S., PRUTHVI K., SWETHA M., MALINI S., VEENA S.M. Isolation, Purification, and Characterization of Fungal Laccase fromPleurotussp [J]. Enzyme Research, 2011, (2011-08-09), 2011 (1), 248735, 2011.
• 3. STRONG P.J., CLAUS H. Laccase: A Review of Its Past and Its Future in Bioremediation [J]. Critical Reviews in Environmental Science & Technology, 41 (4), 373, 2011.
• 4. LLORET L., EIBES G., L-CHAU T.A., MOREIRA M.T., FEIJOO G., LEMA J.M. Laccase-catalyzed degradation of anti-inflammatories and estrogens [J]. Biochemical Engineering Journal, 51 (3), 124, 2010.
• 5. LU C., CAO L., LIU R., LEI Y., DING G. Effect of common metal ions on the rate of degradation of 4-nitrophenol by a laccase-Cu²⁺ synergistic system [J]. Journal of Environmental Management, 113 (1), 1, 2012.
• 6. ZEEB B., GIBIS M., FISCHER L., WEISS J. Crosslinking of interfacial layers in multilayered oil-in-water emulsions using laccase: Characterization and pH-stability [J]. Food Hydrocolloids, 27 (1), 126, 2012.
• 7. BOUTUREIRA O., BERNARDES G.J. Advances in chemical protein modification [J]. Chemical Reviews, 115 (5), 2174, 2015.
• 8. RODRIGUES R.C., BERENGUER-MURCIA A., FERNANDEZ-LAFUENTE R. ChemInform Abstract: Coupling Chemical Modification and Immobilization to Improve the Catalytic Performance of Enzymes [J]. Advanced Synthesis & Catalysis, 353 (13), 2216, 2011.
• 9. RODRIGUES R.C., BERENGUER-MURCIA Á., FERNANDEZ-LAFUENTE R. Coupling chemical modification and immobilization to improve the catalytic performance of enzymes [J]. Advanced Synthesis & Catalysis, 353 (13), 2216, 2011.
• 10. SIMON L.M., KOTORM N.M., GARAB G., LACZK I. Effects of polyhydroxy compounds on the structure and activity of alpha-chymotrypsin [J]. Biochemical & Biophysical Research Communications, 293 (1), 416, 2002.
• 11. ORTBAUER M., POPP M. Functional role of polyhydroxy compounds on protein structure and thermal stability studied by circular dichroism spectroscopy [J]. Plant Physiology & Biochemistry, 46 (4), 428, 2008.
• 12. DEMCHENKO A.P. Ultraviolet spectroscopy of proteins [M]. Springer Science & Business Media, 2013.
• 13. GHOSH S., BADRUDDOZA A., UDDIN M., HIDAJAT K. Adsorption of chiral aromatic amino acids onto carboxymethyl-β-cyclodextrin bonded Fe3O4/SiO2 core–shell nanoparticles [J]. Journal of colloid and interface science, 354 (2), 483, 2011.
• 14. RANI A., VENKATESU P. Insights into the interactions between enzyme and co-solvents: stability and activity of stem bromelain [J]. International Journal of Biological Macromolecules, 73 189, 2015.
• 15. LI X., XU L., WANG G., ZHANG H., YAN Y. Conformation studies on Burkholderia cenocepacia lipase via resolution of racemic 1-phenylethanol in non-aqueous medium and its process optimization [J]. Process Biochemistry, 48 (12), 1905, 2013.
• 16. LIU W., BRATKO D., PRAUSNITZ J.M., BLANCH H.W. Effect of alcohols on aqueous lysozyme-lysozyme interactions from static light-scattering measurements [J]. Biophysical Chemistry, 107 (3), 289, 2004.
• 17. LI J.J., LIU Y.D., WANG F.W., MA G.H., SU Z.G. Hydrophobic interaction chromatography correctly refolding proteins assisted by glycerol and urea gradients [J]. Journal of Chromatography A, 1061 (2), 193, 2004.

Identyfikatory

DOI

10.15244/pjoes/94839