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Horseradish Peroxidase Isozyme C: A Comparative Study of Native and Recombinant Enzyme Produced by E. coli Transformants a
Author(s) -
EGOROV A. M.,
GAZARYAN I. G.,
KIM B. B.,
DOSEYEVA V. V.,
KAPELJUCH J. L.,
VERYOVKIN A. N.,
FECHINA V. A.
Publication year - 1994
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.1994.tb47378.x
Subject(s) - horseradish peroxidase , recombinant dna , peroxidase , chemistry , abts , substrate (aquarium) , enzyme , isozyme , biochemistry , escherichia coli , microbiology and biotechnology , biology , antioxidant , ecology , dpph , gene
The purification and refolding of the recombinant horseradish peroxidase produce by E. coli transformants are described. The recombinant enzyme is of 34 kDa and has an isozyme spectrum similar to Sigma type VI horseradish peroxidase. The specific activity of the refolded peroxidase is of about 2000 U/mg with ABTS as a substrate. The recombinant and native enzyme are similar with respect to their catalytic properties in the reaction of enhanced chemiluminescence. Operational and thermal stability of the refolded peroxidase is two to three times lower than for the native one.