Influences of Organic Compounds on Laccase Activity Tests

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Organic compounds oxalic acid and ethylenediaminetetraacetic acid disodium salt-2-hydrate (EDTA Na2) were described as laccase inhibitors by forming complex compounds with the metal ions of the laccase. Their influence on laccase from Trametes hirsuta lg-9 and Rhus vernificera in different test systems utilizing 2, 2-azino-bis (3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) and 2, 6-dimethoxyphenol (DMP) as enzyme substrates were tested. Our study indicated that oxalic acid can influence the laccase activity determination mainly by changing the pH of the reaction system. The influences of both oxalic acid and EDTA on the laccase activity determination with different substrates were different. The results indicated that both oxalic acid and EDTA could influence the laccase activity determination by influencing and the binding of laccases substrates but not by chelating metal of the laccase. The organic compounds can also influence the laccase activity determination by changing the pH of the reaction system.

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1702-1707

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September 2013

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[1] Mayer A. M, Staples R.C. Laccase: new functions for an old enzyme. Phytochemistry. 60(2002), pp.551-565.

DOI: 10.1016/s0031-9422(02)00171-1

Google Scholar

[2] Alexandre G, Zhulin I.B. Laccases are widespread in bacteria. Trends Biotechnol. 18(2000), pp.41-42.

DOI: 10.1016/s0167-7799(99)01406-7

Google Scholar

[3] Bourbonnais R, Paice M.G. Oxidation of non-phenolic substrates, An expanded role for laccase in lignin biodegradation. FEBS Lett. 267(1990), pp.99-102.

DOI: 10.1016/0014-5793(90)80298-w

Google Scholar

[4] Galli C, Gentili P. Chemical messengers: mediated oxidations with the enzyme laccase. Journal of Physical Organic Chemistry. 17(2004) , pp.973-977.

DOI: 10.1002/poc.812

Google Scholar

[5] Baldrian P. Fungal laccases - occurrence and properties. FEMS Microbiol Rev. 30(2006), pp.215-242.

DOI: 10.1111/j.1574-4976.2005.00010.x

Google Scholar

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

DOI: 10.1016/j.tibtech.2006.03.006

Google Scholar

[7] Nina Hakulinen, Laura-Leena Kiiskinen, Kristiina Kruus, Markku Saloheimo, Arja Paananen,. Anu Koivula, Juha Rouvinen. Crystal structure of a laccase from Melanocarpus albomyces with an intact trinuclear copper site. Nat Struct Biol. 9(2002).

DOI: 10.1038/nsb823

Google Scholar

[8] . Kyung-Lyum Mina, Yong-Hak Kimb, Young Woon Kimb, Hack Sung Jungb, Yung Chil Hahb. Characterization of a Novel Laccase Produced by the Wood-Rotting Fungus Phellinus ribis. rchives of Biochemistry and Biophysics. 392(2001), pp.279-286.

DOI: 10.1006/abbi.2001.2459

Google Scholar

[9] Harkin J. M, Obst J.R. Syringaldazine: an effective reagent for detecting laccase and peroxidase in fungi. Cellular and Molecular Life Sciences (CMLS). 29 (1973), pp.381-387.

DOI: 10.1007/bf01926734

Google Scholar

[10] Childs R.E., Bardsley W.G. The steady-state kinetics of peroxidase with 2, 2'-azino-di-(3-ethyl-benzthiazoline-6-sulphonic acid) as chromogen. Biochem. J. 145(1975) , pp.93-103.

DOI: 10.1042/bj1450093

Google Scholar

[11] Xu F. Effects of Redox Potential and Hydroxide Inhibition on the pH Activity Profile of Fungal Laccases. J. Biol. Chem. 272(1997), pp.924-928.

DOI: 10.1074/jbc.272.2.924

Google Scholar

[12] Johannes C, Majcherczyk A. Laccase activity tests and laccase inhibitors. Journal of Biotechnology. 78(2000), pp.193-199.

DOI: 10.1016/s0168-1656(00)00208-x

Google Scholar