Infl uence of counteranions on catalytic ability of immobilized laccase in Cu-alginate matrices:Inhibition of chloride and activation of acetate

Ting Pan Yao-Jin Sun Xiao-Lei Wang Ting Shi Yi-Lei Zhao

Citation:  Ting Pan, Yao-Jin Sun, Xiao-Lei Wang, Ting Shi, Yi-Lei Zhao. Infl uence of counteranions on catalytic ability of immobilized laccase in Cu-alginate matrices:Inhibition of chloride and activation of acetate[J]. Chinese Chemical Letters, 2014, 25(7): 983-988. doi: 10.1016/j.cclet.2014.05.045 shu

Infl uence of counteranions on catalytic ability of immobilized laccase in Cu-alginate matrices:Inhibition of chloride and activation of acetate

    通讯作者: Yi-Lei Zhao,
  • 基金项目:

    The first author gave special thanks to Mr. Yanbing Qi, Mr. Lanxuan Liu for discussions. This work is supported in part by the National High-Tech R&D Program of China "863" (No. 2012AA020403)  (No. 2012AA020403)

    the National Basic Research Program of China "973" (Nos. 2012CB721005, 2013CB966802) (Nos. 2012CB721005, 2013CB966802)

    National Natural Science Foundation of China (Nos. 21377085, 21303101, 31121064, J1210047) (Nos. 21377085, 21303101, 31121064, J1210047)

    MOE New Century Excellent Talents in University (No. NCET-12-0354). (No. NCET-12-0354)

摘要: Laccase is a promising oxidase with environmental applications, such as lignin degradation and chlorophenol detoxification. Laccase immobilization can significantly improve physiochemical stability and reusability compared to the free enzymes. In this work, anion effect was investigated in entrapment of Cu-alginate matrix with five types of anions, including perchlorate (ClO4-), nitrate (NO3-), sulfate (SO42- ), chloride (Cl-), and acetate (CH3CO2-). Accordingly, chloride inhibition and acetate activation were detected in the o-tolidine kinetic experiments, while effects of the other three anions were much smaller. Such counteranion effects were also observed in the laccase-catalyzed biodegradation of 2,4-dichlorophenol. The results indicated that counteranions in the enzyme immobilization process are crucial for catalytic capacity, probably due to the competition with the carboxylate groups in alginate. Our results also imply that these anions might coordinate the copper cations in laccase.

English

    1. [1] N. Duran, E. Esposito, Potential applications of oxidative enzymes and phenoloxidase-like compounds in wastewater and soil treatment, Appl. Catal. B: Environ. 28 (2000) 83-99.[1] N. Duran, E. Esposito, Potential applications of oxidative enzymes and phenoloxidase-like compounds in wastewater and soil treatment, Appl. Catal. B: Environ. 28 (2000) 83-99.

    2. [2] H. Claus, Laccase: structure, reactions, distribution, Micron 35 (2004) 93-96.[2] H. Claus, Laccase: structure, reactions, distribution, Micron 35 (2004) 93-96.

    3. [3] S. Riva, Laccases: blue enzymes for green chemistry, Trends Biotechnol. 24 (2006) 219-226.[3] S. Riva, Laccases: blue enzymes for green chemistry, Trends Biotechnol. 24 (2006) 219-226.

    4. [4] Y.B. Qi, J.R. Zhu,Y.J. Sun, et al., Theoretical studies of the binding-affinity andreactivity between laccase and phenolic substrates, Chem. J. Chin. Univ. 35 (2014) 776-783.[4] Y.B. Qi, J.R. Zhu,Y.J. Sun, et al., Theoretical studies of the binding-affinity andreactivity between laccase and phenolic substrates, Chem. J. Chin. Univ. 35 (2014) 776-783.

    5. [5] L. Quintanar, J.J. Yoon, C.P. Aznar, et al., Spectroscopic and electronic structure studies of the trinuclear Cu cluster active site of the multicopper oxidase laccase: nature of its coordination unsaturation, J. Am. Chem. Soc. 127 (2005) 13832-13845.[5] L. Quintanar, J.J. Yoon, C.P. Aznar, et al., Spectroscopic and electronic structure studies of the trinuclear Cu cluster active site of the multicopper oxidase laccase: nature of its coordination unsaturation, J. Am. Chem. Soc. 127 (2005) 13832-13845.

    6. [6] K. Piontek, M. Antorini, T. Choinowski, Crystal structure of a laccase from the fungus Trametes versicolor at 1.90Åresolution containing a full complement of coppers, J. Biol. Chem. 277 (2002) 37663-37669.[6] K. Piontek, M. Antorini, T. Choinowski, Crystal structure of a laccase from the fungus Trametes versicolor at 1.90Åresolution containing a full complement of coppers, J. Biol. Chem. 277 (2002) 37663-37669.

    7. [7] L. Quintana, C. Stoj, A.B. Taylor, et al., Shall we dance? How a multicopper oxidase chooses its electron transfer partner, Acc. Chem. Soc. 40 (2007) 445-452.[7] L. Quintana, C. Stoj, A.B. Taylor, et al., Shall we dance? How a multicopper oxidase chooses its electron transfer partner, Acc. Chem. Soc. 40 (2007) 445-452.

    8. [8] O.V. Morozova, G.P. Shumakovich, S.V. Shleev, Y.I. Yaropolov, Laccase-mediator systems and their applications, Appl. Biochem. Microbiol. 43 (2007) 523-535.[8] O.V. Morozova, G.P. Shumakovich, S.V. Shleev, Y.I. Yaropolov, Laccase-mediator systems and their applications, Appl. Biochem. Microbiol. 43 (2007) 523-535.

    9. [9] Y. Wang, D. Zhang, F.R. He, X.C. Chen, Immobilization of laccase by Cu2+ chelate affinity interaction on surface modified magnetic silica particles and its use for the removal of pentachlorophenol, Environ. Sci. Pollut. Res. 23 (2012) 197-200.[9] Y. Wang, D. Zhang, F.R. He, X.C. Chen, Immobilization of laccase by Cu2+ chelate affinity interaction on surface modified magnetic silica particles and its use for the removal of pentachlorophenol, Environ. Sci. Pollut. Res. 23 (2012) 197-200.

    10. [10] C. Garcia-Galan, A. Berenguer-Murcia, R. Fernandez-Lafuente, R.C. Rodrigues, Potential of different enzyme immobilization strategies to improve enzyme performance, Adv. Synth. Catal. 353 (2011) 2885-2904.[10] C. Garcia-Galan, A. Berenguer-Murcia, R. Fernandez-Lafuente, R.C. Rodrigues, Potential of different enzyme immobilization strategies to improve enzyme performance, Adv. Synth. Catal. 353 (2011) 2885-2904.

    11. [11] H.C. Flemming, J. Wingender, The biofilm matrix, Nat. Rev. Microbiol. 8 (2010) 623-633.[11] H.C. Flemming, J. Wingender, The biofilm matrix, Nat. Rev. Microbiol. 8 (2010) 623-633.

    12. [12] Y. Dong, H.Z. Liu, L. Xu, et al., A novel CHS/ALG bi-layer composite membrane with sustained anti-microbial efficacy used as wound dressing, Chin. Chem. Lett. 21 (2010) 1011-1014.[12] Y. Dong, H.Z. Liu, L. Xu, et al., A novel CHS/ALG bi-layer composite membrane with sustained anti-microbial efficacy used as wound dressing, Chin. Chem. Lett. 21 (2010) 1011-1014.

    13. [13] K.Y. Lee, D.J. Mooney, Alginate: properties and biomedical applications, Prog. Polym. Sci. 37 (2012) 106-126.[13] K.Y. Lee, D.J. Mooney, Alginate: properties and biomedical applications, Prog. Polym. Sci. 37 (2012) 106-126.

    14. [14] K.N. Niladevi, P. Prema, Immobilization of laccase from Streptomyces psammoticus and its application in phenol removal using packed bed reactor, World J. Microbiol. Biotechnol. 24 (2008) 1215-1222.[14] K.N. Niladevi, P. Prema, Immobilization of laccase from Streptomyces psammoticus and its application in phenol removal using packed bed reactor, World J. Microbiol. Biotechnol. 24 (2008) 1215-1222.

    15. [15] Y. Liu, Y. Tong, S. Wang, Q. Deng, A. Chen, Influence of different divalent metal ions on the properties of alginate microcapsules and microencapsulated cells, J. Sol. Gen. Sci. Technol. 67 (2013) 66-67.[15] Y. Liu, Y. Tong, S. Wang, Q. Deng, A. Chen, Influence of different divalent metal ions on the properties of alginate microcapsules and microencapsulated cells, J. Sol. Gen. Sci. Technol. 67 (2013) 66-67.

    16. [16] K.I. Draget, K. Steinsvag, E. Onsoyen, O. Smidsrod, Na-and K-alginate; effect on Cu2+-gelation, Carbohydr. Polym. 35 (1998) 1-6.[16] K.I. Draget, K. Steinsvag, E. Onsoyen, O. Smidsrod, Na-and K-alginate; effect on Cu2+-gelation, Carbohydr. Polym. 35 (1998) 1-6.

    17. [17] I. Donati, J.C. Benegas, A. Cesaro, S. Paoletti, Specific interactions versus counterion condensation, Biomacromolecules 7 (2006) 1587-1597.[17] I. Donati, J.C. Benegas, A. Cesaro, S. Paoletti, Specific interactions versus counterion condensation, Biomacromolecules 7 (2006) 1587-1597.

    18. [18] F. Topuz, A. Henke, W. Richtering, J. Groll, Magnesium ions and alginate do form hydrogels: a rheological study, Soft Matter 8 (2012) 4877-4881.[18] F. Topuz, A. Henke, W. Richtering, J. Groll, Magnesium ions and alginate do form hydrogels: a rheological study, Soft Matter 8 (2012) 4877-4881.

    19. [19] K. Mazur, R. Buchner,M. Bonn, J. Hunger, Hydration of sodium alginate in aqueous solution, Macromolecules 47 (2014) 771-776.[19] K. Mazur, R. Buchner,M. Bonn, J. Hunger, Hydration of sodium alginate in aqueous solution, Macromolecules 47 (2014) 771-776.

    20. [20] H.B. Gray, B.G. Malmstrom, R.J.P. Williams, Copper coordination in blue proteins, J. Biol. Inorg. Chem. 5 (2000) 551-559.[20] H.B. Gray, B.G. Malmstrom, R.J.P. Williams, Copper coordination in blue proteins, J. Biol. Inorg. Chem. 5 (2000) 551-559.

    21. [21] B.B. Lee, P. Ravindra, E.E. Chan, Size and shape of calcium alginate beads produced by extrusion dripping, Chem. Eng. Technol. 36 (2013) 1627-1642.[21] B.B. Lee, P. Ravindra, E.E. Chan, Size and shape of calcium alginate beads produced by extrusion dripping, Chem. Eng. Technol. 36 (2013) 1627-1642.

    22. [22] A. Martinsen, G. Skjak-Braek, O. Smidsrod, Alginate as immobilization material: I. Correlation between chemical and physical properties of alginate gel beads, Biotechnol. Bioeng. 33 (1989) 79-89.[22] A. Martinsen, G. Skjak-Braek, O. Smidsrod, Alginate as immobilization material: I. Correlation between chemical and physical properties of alginate gel beads, Biotechnol. Bioeng. 33 (1989) 79-89.

    23. [23] R. Miller, J. Kuglin, S. Gallagher, W.H. Flurkey, A spectrophotometric assay for laccase using o-tolidine, J. Food Biochem. 21 (1997) 445-459.[23] R. Miller, J. Kuglin, S. Gallagher, W.H. Flurkey, A spectrophotometric assay for laccase using o-tolidine, J. Food Biochem. 21 (1997) 445-459.

    24. [24] R. Murugan, Solution to Michaelis-Menten enzyme kinetic equation via undetermined gauge functions: resolving the nonlinearity of Lineweaver-Burk plot, J. Chem. Phys. 117 (2002) 4178-4183.[24] R. Murugan, Solution to Michaelis-Menten enzyme kinetic equation via undetermined gauge functions: resolving the nonlinearity of Lineweaver-Burk plot, J. Chem. Phys. 117 (2002) 4178-4183.

    25. [25] Y. Wang, X. Chen, J. Liu, F. He, R. Wang, Immobilization of laccase by Cu2+ chelate affinity interaction on surface-modified magnetic silica particles and its use for the removal of 2,4-dichlorophenol, Environ. Sci. Pollut. Res. 20 (2013) 6222-6231.[25] Y. Wang, X. Chen, J. Liu, F. He, R. Wang, Immobilization of laccase by Cu2+ chelate affinity interaction on surface-modified magnetic silica particles and its use for the removal of 2,4-dichlorophenol, Environ. Sci. Pollut. Res. 20 (2013) 6222-6231.

    26. [26] J. Jia, S. Zhang, P. Wang, H. Wang, Degradation of high concentration 2,4-dichlorophenol by simultaneous photocatalytic-enzymatic process using TiO2/UV and laccase, J. Hazard. Mater. 205 (2012) 150-155.[26] J. Jia, S. Zhang, P. Wang, H. Wang, Degradation of high concentration 2,4-dichlorophenol by simultaneous photocatalytic-enzymatic process using TiO2/UV and laccase, J. Hazard. Mater. 205 (2012) 150-155.

    27. [27] AWWA, Standard Methods for the Examination of Water and Wastewater, 19th ed., APHA, AWWA, WPCF, Washington, DC, 1995, pp. 185-190.[27] AWWA, Standard Methods for the Examination of Water and Wastewater, 19th ed., APHA, AWWA, WPCF, Washington, DC, 1995, pp. 185-190.

    28. [28] A. Karaliota, O. Kretsi, C. Tzougraki, Synthesis and characterization of a binuclear coumarin-3-carboxylate copper(II) complex, J. Inorg. Biochem. 84 (2001) 33-37.[28] A. Karaliota, O. Kretsi, C. Tzougraki, Synthesis and characterization of a binuclear coumarin-3-carboxylate copper(II) complex, J. Inorg. Biochem. 84 (2001) 33-37.

    29. [29] S.K. Papageorgiou, E.P. Kouvelos, E.P. Favvas, et al., Metal-carboxylate interactions in metal-alginate complexes studied with FTIR spectroscopy, Carbohydr. Res. 345 (2010) 469-473.[29] S.K. Papageorgiou, E.P. Kouvelos, E.P. Favvas, et al., Metal-carboxylate interactions in metal-alginate complexes studied with FTIR spectroscopy, Carbohydr. Res. 345 (2010) 469-473.

    30. [30] D. Filipiuk, L. Fuks, M. Majdan, Transition metal complexes with uronic acids, J. Mol. Struct. 744-747 (2005) 705-709.[30] D. Filipiuk, L. Fuks, M. Majdan, Transition metal complexes with uronic acids, J. Mol. Struct. 744-747 (2005) 705-709.

    31. [31] G.P. Lewis, Method using ortho-tolidine for the quantitative determination of haemoglobin in serum and urine, J. Clin. Pathol. 18 (1965) 235-239.[31] G.P. Lewis, Method using ortho-tolidine for the quantitative determination of haemoglobin in serum and urine, J. Clin. Pathol. 18 (1965) 235-239.

    32. [32] J.A. Jacob, S. Naumov, N. Biswas, T. Mukherjee, S. Kapoor, Comparative study of ionization of benzidine and its derivatives by free electron transfer and oneelectron oxidation, J. Phys. Chem. C 111 (2007) 18397-18404.[32] J.A. Jacob, S. Naumov, N. Biswas, T. Mukherjee, S. Kapoor, Comparative study of ionization of benzidine and its derivatives by free electron transfer and oneelectron oxidation, J. Phys. Chem. C 111 (2007) 18397-18404.

  • 加载中
计量
  • PDF下载量:  0
  • 文章访问数:  1467
  • HTML全文浏览量:  39
文章相关
  • 收稿日期:  2014-03-19
  • 网络出版日期:  2014-05-13
通讯作者: 陈斌, bchen63@163.com
  • 1. 

    沈阳化工大学材料科学与工程学院 沈阳 110142

  1. 本站搜索
  2. 百度学术搜索
  3. 万方数据库搜索
  4. CNKI搜索

/

返回文章