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- 학술저널
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- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제24권 제12호
- 발행연도
- 2014.1
- 수록면
- 1,673 - 1,678 (6page)
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The interactive inhibitory effects of pH and chloride on the catalysis of laccase from Trametes versicolor were investigated by studying the alteration of inhibition characteristics of sodium chloride at different pHs for the oxidation of 2,2’-azino-bis (3-ethylbenzthiazoline-6-sulfonic acid). At pH 3.0, the addition of sodium chloride (50 mM) brought about a 40-fold increase in Km app and a 4-fold decrease in Vmax app. As the pH increased to 7.0, the inhibitory effects of sodium chloride became significantly weakened. The mixed-inhibition mechanism was successfully used to quantitatively estimate the competitive and uncompetitive inhibition strengths by chloride at two different pHs (pH 3.0 and 6.0). At pH 3.0, the competitive inhibition constant, Ki, was 0.35 mM, whereas the uncompetitive inhibition constant, Ki', was 18.1 mM, indicating that the major cause of the laccase inhibition by chloride is due to the competitive inhibition step. At a higher pH of 6.0, where the inhibition of the laccase by hydroxide ions takes effect, the inhibition of the laccase by chloride diminished to a great extent, showing increased values of both the competitive inhibition constant (Ki = 23.7 mM) and uncompetitive inhibition constant (Ki' = 324 mM). These kinetic results evidenced that the hydroxide anion and chloride share a common mechanism to inhibit the laccase activity.
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참고문헌 (23)
참고문헌 신청
Birhanli E / 2010 / Enhanced production of laccase in repeated-batch cultures of Funalia trogii and Trametes versicolor / Biochem. Eng. J 52 : 33 ~ 37
Cornish-Bowden A. / 1974 / A simple graphical method for determining the inhibition constants of mixed, uncompetitive and non-competitive inhibitors / Biochem. J 137 : 143 ~
Desai SS / 2011 / Microbial laccases and their applications: a review / Asian J. Biotechnol 3 : 98 ~ 124
Dooley DM / 1979 / Spectroscopic studies of Rhus vernicifera and Polyporus versicolor laccase. Electronic structures of the copper sites / J. Am. Chem. Soc 101 : 5038 ~ 5046
Enaud E / 2011 / Laccase chloride inhibition reduction by an anthraquinonic substrate / Enzyme Microb. Technol 49 : 517 ~ 525
Cornish-Bowden A. / 1974 / A simple graphical method for determining the inhibition constants of mixed, uncompetitive and non-competitive inhibitors / Biochem. J 137 : 143 ~
Desai SS / 2011 / Microbial laccases and their applications: a review / Asian J. Biotechnol 3 : 98 ~ 124
Dooley DM / 1979 / Spectroscopic studies of Rhus vernicifera and Polyporus versicolor laccase. Electronic structures of the copper sites / J. Am. Chem. Soc 101 : 5038 ~ 5046
Enaud E / 2011 / Laccase chloride inhibition reduction by an anthraquinonic substrate / Enzyme Microb. Technol 49 : 517 ~ 525
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