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Isolation of proanthocyanidins from Pinus thunbergii needles and tyrosinase inhibition activity
Process Biochemistry ( IF 4.4 ) Pub Date : 2021-01-01 , DOI: 10.1016/j.procbio.2020.10.003
Haibo Yang , Zhe Wang , Wei Song , Zhenli Zhao , Yong Zhao

Abstract In the present work, we investigated the anti-tyrosinase activity, mechanism and antioxidant activity of proanthocyanidins (PAs) isolated from Pinus thunbergii needles. The results showed that PAs mainly consisted of catechin/epicatechin and had a strong inhibitory effect on the monophenolase and diphenolase activity of tyrosinase. PAs could reduce the steady state activity of tyrosinase monophenolase while prolonging the reaction delay time in a dose-dependent manner. The inhibitory effect of PAs on tyrosinase diphenolase was reversible, with the IC50 value of 37.64 μg/mL. The inhibition kinetic analysis by Lineweaver-Burk plots showed that PAs were a mixed-type inhibitor of tyrosinase diphenolase, with inhibition constants KI and KIS of 29.92 μg/mL and 128.27 μg/mL, respectively. Further, determination of the metal chelating ability, scanning study, fluorescence quenching, and DOPA (dihydroxyphenylalanine) oxidation were used to study the potential inhibition mechanism of PAs on tyrosinase. The results confirmed that PAs could chelate with copper ions in the active site of tyrosinase to inhibit tyrosinase activity. Moreover, ABTS [2,2′-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)] and FRAP (ferric reducing antioxidant power) assay showed good antioxidant capacity of PAs. This study revealed the possibility of Pinus thunbergii needle PAs as a new tyrosinase inhibitor in the fields of food, medicine, and cosmetics industries.

中文翻译:

松柏针叶原花青素的分离及酪氨酸酶抑制活性

摘要 在目前的工作中,我们研究了从松树针叶中分离的原花青素 (PAs) 的抗酪氨酸酶活性、机制和抗氧化活性。结果表明,PAs主要由儿茶素/表儿茶素组成,对酪氨酸酶的单酚酶和双酚酶活性有较强的抑制作用。PAs可以降低酪氨酸酶单酚酶的稳态活性,同时以剂量依赖性方式延长反应延迟时间。PAs对酪氨酸酶二酚酶的抑制作用是可逆的,IC50值为37.64 μg/mL。Lineweaver-Burk 图抑制动力学分析表明,PAs 是酪氨酸酶二酚酶的混合型抑制剂,抑制常数 KI 和 KIS 分别为 29.92 μg/mL 和 128.27 μg/mL。此外,测定金属螯合能力,通过扫描研究、荧光猝灭和DOPA(二羟基苯丙氨酸)氧化研究PAs对酪氨酸酶的潜在抑制机制。结果证实PAs可与酪氨酸酶活性位点的铜离子螯合,抑制酪氨酸酶活性。此外,ABTS [2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)] 和 FRAP(铁还原抗氧化能力)试验显示 PA 具有良好的抗氧化能力。该研究揭示了松柏针PAs在食品、医药和化妆品行业作为新型酪氨酸酶抑制剂的可能性。结果证实PAs可与酪氨酸酶活性位点的铜离子螯合,抑制酪氨酸酶活性。此外,ABTS [2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)] 和 FRAP(铁还原抗氧化能力)试验显示 PA 具有良好的抗氧化能力。该研究揭示了松柏针PAs在食品、医药和化妆品行业作为新型酪氨酸酶抑制剂的可能性。结果证实PAs可与酪氨酸酶活性位点的铜离子螯合,抑制酪氨酸酶活性。此外,ABTS [2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)] 和 FRAP(铁还原抗氧化能力)试验显示 PA 具有良好的抗氧化能力。该研究揭示了松柏针PAs在食品、医药和化妆品行业作为新型酪氨酸酶抑制剂的可能性。
更新日期:2021-01-01
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