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Reaction characteristics of 4-methylcatechol 2,3-dioxygenase from Pseudomonas putida SU10

Authors
Ha, YMJung, YHKwon, DYKim, YKim, CKMin, KH
Issue Date
Feb-2000
Publisher
SPRINGER-VERLAG SINGAPORE PTE LTD
Keywords
4-methylcatechol 2,3-dioxygenase; catechol; catechol 2,3-dioxygenase; inactivation; reactivation
Citation
JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, v.10, no.1, pp.35 - 42
Journal Title
JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY
Volume
10
Number
1
Start Page
35
End Page
42
URI
https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/16787
ISSN
1017-7825
Abstract
Reaction characteristics of 4-methylcatechol 2,3-dioxygenase (4MC23O) 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 degrees C, 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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