Oxidative polymerization process of hydroxytyrosol catalysed by polyphenol oxidases or peroxidase: Characterization, kinetics and thermodynamics

文献类型： 外文期刊

第一作者： Xie, Pujun

作者： Xie, Pujun;Huang, Lixin;Zhang, Caihong;Xie, Pujun;Huang, Lixin;Zhang, Caihong;Fan, Linlin

作者机构：

关键词： Olive mill wastewater; Laccase and tyrosinase; Enzymatic oxidative polymerization; Hydroxytyrosol oligomers; Nuclear magnetic resonance; Isothermal titration calorimetry; Circular dichroism

期刊名称：FOOD CHEMISTRY （ 影响因子：7.514； 五年影响因子：7.516 ）

ISSN： 0308-8146

年卷期： 2021 年 337 卷

页码：

收录情况： SCI

摘要： Hydroxytyrosol oligomer prepared by bioenzyme shows stronger health-promoting properties than its monomer. However, the polymerization process carried out by laccase, tyrosinase or horseradish peroxidase is still lacking in term of product characterization, kinetics and thermodynamics. To achieve these aspects, ATR-FT-IR, NMR, the Michaelis-Menten equation and isothermal titration calorimetry were explored. The results showed that the identified polymers presented a C-C bond and a degree of polymerization less than six. Laccase showed the greatest affinity to hydroxytyrosol via comparison of K-m and V-m. All of these polymerization processes were spontaneous and exothermic behaviuors ranging from 30 to 50 degrees C, and were driven by hydrogen bonds, van der Waals interactions and hydrophobic interactions. Furthermore, circular dichroism spectroscopy was used to reveal the enzymatic structural changes during the catalysis, which showed that beta-sheet levels for laccase, ahelix levels for tyrosinase, and the a-helix and random coil levels for horseradish peroxidase were dramatically decreased.

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