食品研究与开发
食品研究與開髮
식품연구여개발
FOOD RESEARCH AND CEVELOPMENT
2013年
1期
101-104
,共4页
龚盛昭%尹美娟%邰晓曦%云智勉
龔盛昭%尹美娟%邰曉晞%雲智勉
공성소%윤미연%태효희%운지면
夏酪氨酸酶%阿魏酸异辛酯%抑制作用%动力学%单酚酶%二酚酶
夏酪氨痠酶%阿魏痠異辛酯%抑製作用%動力學%單酚酶%二酚酶
하락안산매%아위산이신지%억제작용%동역학%단분매%이분매
tyrosinase%2-ethylhexy ferulate%inhibitory effect%kinetics%monophenolase%diphenolase
在30℃,pH=6.8的Na2HPO4-NaH2PO4缓冲体系中,采用酶动力学方法研究阿魏酸异辛酯对酪氨酸酶单酚酶和二酚酶活力的抑制动力学.实验结果表明,阿魏酸异辛酯对酪氨酸酶单酚酶和二酚酶活性均有良好抑制作用,对单酚酶和二酚酶活力的相对抑制率达到50%的阿魏酸异辛酯浓度(IC50)约分别为0.24 mmol/L和0.45 mmol/L,比熊果苷抑制二酚酶活性的IC50值5.3 mmol/L小得多.阿魏酸异辛酯能明显延长单酚酶的迟滞时间,0.4 mmol/L阿魏酸异辛酯能使迟滞时间由1.1 min延长至3.6 min.Lineweaver-Burk图显示阿魏酸异辛酯对二酚酶的抑制作用表现为竞争性抑制,抑制常数(KI)为0.20 mmol/L.
在30℃,pH=6.8的Na2HPO4-NaH2PO4緩遲體繫中,採用酶動力學方法研究阿魏痠異辛酯對酪氨痠酶單酚酶和二酚酶活力的抑製動力學.實驗結果錶明,阿魏痠異辛酯對酪氨痠酶單酚酶和二酚酶活性均有良好抑製作用,對單酚酶和二酚酶活力的相對抑製率達到50%的阿魏痠異辛酯濃度(IC50)約分彆為0.24 mmol/L和0.45 mmol/L,比熊果苷抑製二酚酶活性的IC50值5.3 mmol/L小得多.阿魏痠異辛酯能明顯延長單酚酶的遲滯時間,0.4 mmol/L阿魏痠異辛酯能使遲滯時間由1.1 min延長至3.6 min.Lineweaver-Burk圖顯示阿魏痠異辛酯對二酚酶的抑製作用錶現為競爭性抑製,抑製常數(KI)為0.20 mmol/L.
재30℃,pH=6.8적Na2HPO4-NaH2PO4완충체계중,채용매동역학방법연구아위산이신지대락안산매단분매화이분매활력적억제동역학.실험결과표명,아위산이신지대락안산매단분매화이분매활성균유량호억제작용,대단분매화이분매활력적상대억제솔체도50%적아위산이신지농도(IC50)약분별위0.24 mmol/L화0.45 mmol/L,비웅과감억제이분매활성적IC50치5.3 mmol/L소득다.아위산이신지능명현연장단분매적지체시간,0.4 mmol/L아위산이신지능사지체시간유1.1 min연장지3.6 min.Lineweaver-Burk도현시아위산이신지대이분매적억제작용표현위경쟁성억제,억제상수(KI)위0.20 mmol/L.
@@@@The inhibitory kinetics of 2-ethylhexy ferulate on the activity of monophenolase and diphenolase contained in tyrosinase was studied by enzymological kinetic method with Na2HPO4-NaH2PO4 buffer solution (pH=6.8) at 30℃. 2-ethylhexy ferulate was found to inhibit the monophenolase and diphenolase activity of tyrosinase well. The 2-ethylhexy ferulate concentrations leading to 50%inhibitory rate (IC50) were 0.24 mmol/L for monophenolase and 0.45 mmol/L for diphenolase, much less than that of arbutin (IC50=5.3 mmol/L for diphenolase activity). 2-ethylhexy ferulate can extend the lag time of tyrosinase for oxidation of L-tyrosine, 0.4 mmol/L of 2-ethylhexy ferulate resulted in the extension of lag time from 1.1 min to 3.6 min. The inhibition kinetics of 2-ethylhexy ferulate analyzed by Lineweaver-Burk plots demonstrated a competitive inhibitor for the oxidation of L-DOPA, the inhibition constant for inhibitor binding with enzyme, KI was determined to be 0.20 mmol/L.