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- W2029250237 abstract "Capsaicinoids are the pungent compounds in Capsicum fruits (i.e., hot peppers). Peroxidases catalyze capsaicinoid oxidation and may play a central role in their metabolism. However, key kinetic aspects of peroxidase-catalyzed capsaicinoid oxidation remain unresolved. Using transient-state methods, we evaluated horseradish peroxidase compound I and II reduction by two prominent capsaicinoids (25 degrees C, pH 7.0). We determined rate constants approaching 2 x 10(7) and 5 x 10(5)M(-1)s(-1) for compound I and compound II reduction, respectively. We also determined k(app) values for steady-state capsaicinoid oxidation approaching 8 x 10(5)M(-1)s(-1) (25 degrees C, pH 7.0). Accounting for stoichiometry, these are in excellent agreement with constants for compound II reduction, suggesting that this reaction governs capsaicinoid-dependent peroxidase turnover. Ascorbate rapidly reduced capsaicinoid radicals, assisting in the determination of the kinetic constants reported. Because ascorbate accumulates in Capsicum fruits, it may also be an important determinant for capsaicinoid content and preservation in Capsicum fruits and related products." @default.
- W2029250237 created "2016-06-24" @default.
- W2029250237 creator A5043881366 @default.
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- W2029250237 date "2003-09-01" @default.
- W2029250237 modified "2023-09-26" @default.
- W2029250237 title "Peroxidase-catalyzed oxidation of capsaicinoids: steady-state and transient-state kinetic studies." @default.
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- W2029250237 doi "https://doi.org/10.1016/s0003-9861(03)00321-7" @default.
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