CAJ | 학술논문

采用酶动力学方法，以L-多巴为底物，通过酪氨酸酶二酚酶催化反应体系，研究α-熊果苷对二酚酶活性的影响。实验结果表明：α-熊果苷对酪氨酸酶的二酚酶催化反应产生激活效应，反应过程没有迟滞时间；由Lineweaver-Burk双倒数作图得知，在一定范围内，随着催化反应系统中α-熊果苷浓度的增大，动力学参数Km逐渐减小，而最大反应速率Vmax逐渐增大，表明α-熊果苷对酪氨酸酶二酚酶的激活作用为竞争及非竞争混合型；并且从酶的构象变化及减少酶的自杀性失活的角度，阐述了α-熊果苷对酪氨酸酶二酚酶的激活机制。
채용매동역학방법，이L-다파위저물，통과락안산매이분매최화반응체계，연구α-웅과감대이분매활성적영향。실험결과표명：α-웅과감대락안산매적이분매최화반응산생격활효응，반응과정몰유지체시간；유Lineweaver-Burk쌍도수작도득지，재일정범위내，수착최화반응계통중α-웅과감농도적증대，동역학삼수Km축점감소，이최대반응속솔Vmax축점증대，표명α-웅과감대락안산매이분매적격활작용위경쟁급비경쟁혼합형；병차종매적구상변화급감소매적자살성실활적각도，천술료α-웅과감대락안산매이분매적격활궤제。
The effect of α-arbutin on the diphenolase activity of mushroom tyrosinase was investigated by the method of enzyme ki-netics. The results showed thatα-arbutin activated diphenolase activity,and there is no lag time during the reaction. The Lineweav-er-Burk double reciprocal plot shows that the Michaelis constant Km decreases with increasing concentration of α-arbutin,and the maximum reaction rate Vmax increases with increasing concentration of α-arbutin. It indicates that the activation of α-arbutin on di-phenolase activity is mixed competitive and non-competitive activation. To explain such activation,it should be mainly refered to the conformational changes in tyrosinase.