Purification and characterization of catalase from a facultative alkalophilic Bacillus.
Catalase was purified to an electrophoretically homogeneous state from the facultative alkalophilic bacterium, Bacillus YN-2000, and some of its properties were studied. Its molecular weight was 282,000 and its molecule was composed of four identical subunits. The enzyme contained two protoheme molecules per tetramer. The enzyme showed an absorption spectrum of typical high-spin ferric heme with a peak at 406 nm in the oxidized form and peaks at 440, 559, and 592 nm in the reduced form. In contrast to the typical catalases, the enzyme was reduced with sodium dithionite, like peroxidases. The enzyme showed an appreciable peroxidase activity in addition to high catalase activity. The amino acid composition of Bacillus YN-2000 catalase was very similar to those of catalase from Neurospora crassa and peroxidase from Halobacterium halobium. The catalase content in the soluble fraction from the bacterium was higher with the cells grown at pH 10 than with the cells grown at lower pHs (pH 7-9).
Yumoto
I
I
Department of Life Science, Faculty of Science, Tokyo Institute of Technology.
Fukumori
Y
Y
Yamanaka
T
T
D000596:Amino Acids / Q000032:analysis; D001407:Bacillus / Q000187:drug effects / Q000201:enzymology*; D002374:Catalase / Q000737:chemistry / Q000302:isolation & purification*; D004926:Escherichia coli / Q000187:drug effects / Q000201:enzymology; D006861:Hydrogen Peroxide / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D009492:Neurospora crassa / Q000187:drug effects / Q000201:enzymology; D016354:Rhodobacter capsulatus / Q000187:drug effects / Q000201:enzymology
D000596:Amino Acids; D006861:Hydrogen Peroxide; D002374:Catalase