CAJ | 학술논문

对三疣梭子蟹酚氧化酶的生化特性进行研究.结果表明:以邻苯二酚为底物,酚氰化酶在pH7.8～8.4时最稳定,最适pH值为8.2.温度55℃时,酚氧化酶活力最大,在25～40℃时,热稳定性最好.酶促褐变反应动力学符合米氏方程,温度为30℃,pH7.2时,米氏常数K_m=0.531mol/L,最大反应速率0.049 A_(530nm)/min.选用的12种抑制剂对三疣梭子蟹酚氧化酶均有一定的抑制效果,以植酸抑制效果最强,焦亚硫酸钠、L-半胱氨酸、草酸次之,抗坏血酸效果较好.
대삼우사자해분양화매적생화특성진행연구.결과표명:이린분이분위저물,분청화매재pH7.8～8.4시최은정,최괄pH치위8.2.온도55℃시,분양화매활력최대,재25～40℃시,열은정성최호.매촉갈변반응동역학부합미씨방정,온도위30℃,pH7.2시,미씨상수K_m=0.531mol/L,최대반응속솔0.049 A_(530nm)/min.선용적12충억제제대삼우사자해분양화매균유일정적억제효과,이식산억제효과최강,초아류산납、L-반광안산、초산차지,항배혈산효과교호.
Crude phenoloxidase (PO) was extracted from Portunus trituberculatus and characterized biochemically. This enzyme exhibited an optimal pH of 8.2 and temperature of 55 ℃ for catalyzing the oxidation of pyrocatechol as a substrate. Optimal enzyme stability was observed in the ranges ofpH 7.8-8.4 and 25-40 ℃. Browning reaction catalyzed by this enzyme obeyed the Michaelis-Menten equation. The values of K_m and V_(max) at 30 ℃ and pH 7.2 were calculated to be 0.531 mol/L and 0.049 A_(530nm)/min, respectively. Twelve inhibitors tested all had a certain inhibitory effect against this enzyme, among which phytic acid was the strongest inhibitor, followed in turn by sodium metabisulfite, L-cysteine, oxalic acid and ascorbic acid.