Screening and Characterization of Polyphenol Oxidase Source for Protein Cross-linking
Jinyan Gao
Abstract
Jinyan Gao
Abstract
The plants and fungus with high polyphenol oxidase (PPO) activity were selected to apply to protein cross-linking, and biochemical nature of this enzyme was characterized. PPOs from Agaricus bisporus and eggplant were observed to be the highest, 11004 U/g and 9376 U/g. The optimum temperature and pH for these two kinds of PPO were found to be 20 ℃ and 7.0, while PPO from A. bisporus showed lower heat stability than that from eggplant at high temperature. Metal ions like Zn2+, Mn2+ and Ag+ showed obvious inhibition on PPOs while Cu2+ was able to promote the PPO activity from A. bisporus (140.9%) and inhibit PPO activity from 23.4%. The Km and Vmax values of PPOs from A. bisporus and eggplant were 5.5 mmol/L and 1666.7 U, 8.75 mmol/L and 2500 U, respectively.
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The plants and fungus with high polyphenol oxidase (PPO) activity were selected to apply to protein cross-linking, and biochemical nature of this enzyme was characterized. PPOs from Agaricus bisporus and eggplant were observed to be the highest, 11004 U/g and 9376 U/g. The optimum temperature and pH for these two kinds of PPO were found to be 20 ℃ and 7.0, while PPO from A. bisporus showed lower heat stability than that from eggplant at high temperature. Metal ions like Zn2+, Mn2+ and Ag+ showed obvious inhibition on PPOs while Cu2+ was able to promote the PPO activity from A. bisporus (140.9%) and inhibit PPO activity from 23.4%. The Km and Vmax values of PPOs from A. bisporus and eggplant were 5.5 mmol/L and 1666.7 U, 8.75 mmol/L and 2500 U, respectively.
Key concepts: Agaricus bisporus, Polyphenol oxidase, Chemistry, Enzyme, Food science, Polyphenol, Catechol oxidase, Metal ions in aqueous solution