Characterization of different commercial soybean peroxidase preparations and use of the enzyme for N-demethylation of methyl N-methylanthranilate To produce the food flavor methylanthranilate.
The potential of different peroxidase preparations for the N-demethylation of methyl N-methylanthranilate to produce the food flavor methylanthranilate (MA) was investigated. All tested peroxidase preparations were able to catalyze the N-dealkylation. The tested soybean preparations vary widely with respect to their heme content. Furthermore, the operational stability of purified soybean peroxidase (SP) is at least 25-fold lower than that of horseradish peroxidase and only 5-fold higher than that of microperoxidase 8. Thus, the presence of a large protein chain around a porphyrin cofactor in a peroxidase is, by itself, insufficient to explain the observed differences in operational stability. Despite its relatively low operational stability, SP proved to be the most efficient biocatalyst for the production of MA with high yield and purity, especially observed at the high temperature and low pH values at which SP appeared to be optimally active.
Van Haandel
M J
MJ
Department of Biomolecular Sciences, Laboratory of Biochemistry, Wageningen University, Dreijenlaan 3, 6703 HA Wageningen, The Netherlands.
Sarabèr
F C
FC
Boersma
M G
MG
Laane
C
C
Fleming
Y
Y
Weenen
H
H
Rietjens
I M
IM
D005421:Flavoring Agents / Q000378:metabolism*; D008745:Methylation; D010544:Peroxidases / Q000737:chemistry / Q000378:metabolism*; D013025:Glycine max / Q000201:enzymology*; D062367:ortho-Aminobenzoates / Q000378:metabolism*
D005421:Flavoring Agents; D062367:ortho-Aminobenzoates; C098239:6-methylanthranilic acid; C412492:methyl N-methylanthranilate; D010544:Peroxidases