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KMID : 0545120000100010035
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Journal of Microbiology and Biotechnology
2000 Volume.10 No. 1 p.35 ~ p.42
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Reaction Characteristics of 4-Methylcatechol 2,3-Dioxygenase from Pseudomonas putida SU10
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Ha, You Mee
Jung, Young Hee/Kwon, Dae Young/Kim, Young Soo/Kim, Chy Kyung/Min, Kyung Hee
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Abstract
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Reaction characteristics of 4-methylcatechol 2,3-dioxygenase (4MC230) purified from Pseudomonas putida SU10 with a higher activity toward 4-methylcatechol than catechol or 3-methylcatechol were studied by altering their physical and chemical properties. The enzyme exhibited a maximum activity at pH 7.5 and approximately 40% at pH 6.0 for 4-methylcatechol hydrolysis. The optimum temperature for the enzyme was around 35℃, since the enzyme was unstable at higher temperature. Acetone (10%) stabilized the 4MC230. The effects of solvent and other chemicals (inactivator or reactivator) for the reactivation of the 4MC230 were also investigated. Silver nitrate and hydrogen peroxide severely deactivated the enzyme and the deactivation by hydrogen peroxide was mainly due to the oxidation of ferrous ion to ferric ion. Some solvents acted as an activator and protector for the enzyme from deactivation by hydrogen peroxide. Ascorbate, cysteine, or ferrous ion reactivated the deactivated enzyme by hydrogen peroxide. The addition of ferrous ion together with a reducing agent fully recovered the enzyme activity and increased its activity about 2 times.
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