Open AccessAlcohol Oxidase and Catalase in Peroxisomes of Methanol‐Grown Candida boidinii
Author(s) -
ROGGENKAMP Rainer,
SAHM Hermann,
WAGNER Fritz,
HINKELMANN Wilhelm
Publication year - 1975
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1975.tb02446.x
Subject(s) - peroxisome , alcohol oxidase , catalase , microbody , biochemistry , oxidase test , urate oxidase , mitochondrion , chemistry , enzyme , aspergillus niger , biology , pichia pastoris , gene , recombinant dna
Microbodies, designated as peroxisomes because of their enzyme complement, have been isolated from methanol‐grown cells of Candida boidinii . Spheroplast lysates were separated on non‐continuous Ficoll density gradients, resulting in a mitochondrial fraction and a peroxisome fraction. Estimates of purity using the mitochondrial enzyme markers suggested that the contamination of mitochondria in the peroxisome fraction was about 2‐3 %. As shown by electron microscopy the peroxisomes were 0.4‐0.6 μm in diameter and contained crystalloid inclusions. Alcohol oxidase and catalase, which catalyse the oxidation of methanol to formaldehyde in Candida boidinii , could be localized within the peroxisomes. Gel‐electròphoretic studies of the peroxisome fraction demonstrated that it contained only two predominant protein bands consistent with alcohol oxidase and catalase. No alcohol oxidase and catalase activity was found in mitochondria.