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Catalase activity in methanol‐oxidizing Candida boidinii 11 Bh and its cytochemical localization
Author(s) -
Voříšek J.,
Volfová O.
Publication year - 1975
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(75)80816-7
Subject(s) - library science , citation , chemistry , microbiology and biotechnology , biology , computer science
Our previous study of methanol oxidation to formaldehyde, formic acid and CO2 by Candida boidinii 11 Bh showed the presence of catalase activity (EC 1.11.1.6) in both cells and cell-free extracts. This enzyme and methanol-oxidase (EC 1.1.3.13) transform methanol to formaldehyde [ 11. The simultaneous hydrogen peroxide reduction was previously found in methanol oxidizing bacteria [2] and in methanol oxidizing yeasts [3,4]. This communication summarizes certain kinetic properties . . . . of catalase from C. bordznzz 11Bh cells grown on mineral salt medium containing methanol and describes our attempts at cytochemical localization of this enzyme.