가공 과정 중 갈변에 관여하는 돼지감자의 peroxidase가 ammonium sulfate, DEAE-cellulose column, Sephacryl S-200 column chromatography에 의하여 36.65배로 정제되었다. 이 효소는 p-phenylenediamine을 기질로 사용하였을 때 pH5.0가 활성 최적 pH이었으며 pH $5.0{sim}6.0$의 범위에서 비교적 안정하였다. 열 불활성화 곡선은 1차 곡선에서 벗어났고 60, 70, $80^{circ}C$에서의 D값은 각각 86, 45, 33초이었으며 활성화에너지는 4,111 J/mole이었다. 이 효소의 기질특이성은 amine류 중에서 p-phenylenediamine과 가장 친화력이 좋았고 potassium cyanate, sodium diethyldithiocarbamate, L-ascorbic acid, sodium hydrosulfite, L-cysteine에 의해 활성이 완전히 억제되었으며 $Ca^{2+},;Cu^{2+}$에 의해서는 활성이 촉진되었다.
Peroxidase from Jerusalem artichoke tubers, which might be related to browning reaction, was purified by ammonium sulfate precipitation, DEAE-cellulose and Sephacryl S-200 chromatography. The optimum pH of the purified peroxidase was 5.0 and relatively stable at pH $5.0{sim}6.0$ using substrate of p-phenylenediamine and $H_2O_2$. D-values for thermal inactivation at 60, 70 and $80^{circ}C$ were 86, 45 and 33 sec, respectively. Activation energy was 4,111 J/mole. The enzyme showed the most sensitive specificity of substrate for p-phenylenediamine. The compounds such as 1mM potassium cyanide, 10mM sodium diethyldithiocarbamate, L-ascorbic acid, sodium hydrosulfite and L-cysteine inhibited completely while 1mM of $Ca^{2+};and;Cu^{2+}$ activated the purified peroxidase.
