Àá½Ã¸¸ ±â´Ù·Á ÁÖ¼¼¿ä. ·ÎµùÁßÀÔ´Ï´Ù.
KMID : 0903519870300030285
Journal of the Korean Society of Agricultural Chemistry and Biotechnology
1987 Volume.30 No. 3 p.285 ~ p.290
Inactivation of Peroxidase from Fuji Apples by Heat and Chemical Treatments


Abstract
As a basic research for inhibition of enzymatic browning of apples during dehydration or processing, peroxidase was extracted from Fuji apples to investigate heat inactivation, and chemical inhibition. Peroxidase showed the highest activity at 35¡É and pH 5.5 using substrates of p-phenylenediamine and H©üO©ü. The thermal inactivation followed biphasic kinetics to have activation energy (Ea) of 48.2k§º/§ß and z value of 11.2¡É for tire heat labile fraction and Ea of 36.3k§º/§ß and z value of 14.9¡É for the heat resistant fraction. Browning by peroxidase was completely inhibited at the concentrations of l0mM for sodium diethyldithiocarbamate and potassium metabisulfite and 1mM for L-cysteine and ascorbic acid.
KEYWORD
FullTexts / Linksout information
Listed journal information