Open AccessProduction of two different catalase‐peroxidases by Deinococcus radiophilus
Author(s) -
Yun Eun Jeong,
Lee Young Nam
Publication year - 2000
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2000.tb09007.x
Subject(s) - catalase , deinococcus , hydrogen peroxide , peroxidase , enzyme , biochemistry , chemistry , biology , microbiology and biotechnology , deinococcus radiodurans , gene
The production of two kinds of catalase‐peroxidase, viz. catalase‐2 and catalase‐3 of Deinococcus radiophilus varied depending upon growth phases and oxidative stress. A gradual increase in total catalase activity occurred during exponential and stationary phase. Electrophoretic resolution of these catalases in Deinococcal cell extracts revealed the uniform occurrence of catalase‐2 and the appearance of catalase‐3 only during the late exponential and stationary phase. A substantial increase in total catalase was observed in either hydrogen peroxide‐ or UV‐treated cells. Monitoring of D. radiophilus catalase activity in the oxidative stressed and non‐treated cells by gel electrophoresis followed by densitometry revealed the several‐fold increase in catalase‐3, which is above the constant level of catalase‐2. The occurrence of catalase‐3 and catalase‐2 revealed by fractionation of sucrose‐shocked cells suggests that catalase‐3 is a cytosolic inducible enzyme whereas catalase‐2 is the membrane‐associated constitutive enzyme.