Purification and biochemical characterization of polyphenol oxidase of African bush mango (Irvingia gabonensis) fruit peel

Adeseko, Catherine Joke; Sanni, David Morakinyo; Salawu, S.O.; Kade, Ige Joseph; Bamidele, Samuel Olufemi; Lawal, Olusola Tosin

doi:10.1016/j.bcab.2021.102119

Cited by 16 publications

(7 citation statements)

References 46 publications

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“…PPO’s molecular weight from different sources has been reported to vary in the range of 14.2 kDa to 220 kDa [ 14 , 15 ]. These results might be due to species gene diversity and signal peptide cleavage [ 16 ].…”

Section: Resultsmentioning

confidence: 99%

“…As a result of a 50 mM concentration, the lowest inhibition effects were observed with urea and oxalic acid at 29.07% and 16.31% inhibition, respectively. Conversely, a stronger inhibition effect was observed for urea at 5 mM with 100% inhibition from the inhibition studies with African bush mango fruit peel PPO [ 16 ]. Oxalic acid at 5 mM was defined as a medium effective inhibitor for fennel seed PPO with 41% inhibition [ 11 ], which had a stronger inhibitory effect than in the inhibition results of this study.…”

Section: Resultsmentioning

confidence: 99%

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Purification and Biochemical Characterization of Polyphenol Oxidase Extracted from Wheat Bran (Wan grano)

Yu,

He,

et al. 2024

Molecules

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Currently, little is known about the characteristics of polyphenol oxidase from wheat bran, which is closely linked to the browning of wheat product. The wheat PPO was purified by ammonium sulfate precipitation, DEAE-Sepharose ion-exchange column, and Superdex G-75 chromatography column. Purified wheat PPO activity was 11.05-fold higher, its specific activity was 1365.12 U/mg, and its yield was 8.46%. SDS-PAGE showed that the molecular weight of wheat PPO was approximately 21 kDa. Its optimal pH and temperature were 6.5 and 35 °C for catechol as substrate, respectively. Twelve phenolic substrates from wheat and green tea were used for analyzing the substrate specificity. Wheat PPO showed the highest affinity to catechol due to its maximum Vmax (517.55 U·mL−1·min−1) and low Km (6.36 mM) values. Docking analysis revealed strong affinities between catechol, gallic acid, EGCG, and EC with binding energies of −5.28 kcal/mol, −4.65 kcal/mol, −4.21 kcal/mol, and −5.62 kcal/mol, respectively, for PPO. Sodium sulfite, ascorbic acid, and sodium bisulfite dramatically inhibited wheat PPO activity. Cu2+ and Ca2+ at 10 mM were considered potent activators and inhibitors for wheat PPO, respectively. This report provides a theoretical basis for controlling the enzymatic browning of wheat products fortified with green tea.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Purification and Biochemical Characterization of Polyphenol Oxidase Extracted from Wheat Bran (Wan grano)

Yu,

He,

et al. 2024

Molecules

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“…The polyphenol and contaminant free enzyme solution were sufficiently suitable for further analysis. In the work of Adeseko et al [ 36 ], a purification fold of 6.85 with a recovery of 20% was obtained for polyphenol oxidase from African bush mango after being subjected to three-step purification process.…”

Section: Resultsmentioning

confidence: 99%

Biochemical properties of purified polyphenol oxidase from bitter leaf (Vernonia amygdalina)

Ilesanmi

Adedugbe

Oyegoke

et al. 2023

Heliyon

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“…The molecular weights of the PPO isozymes range from 27 to 144 kDa depending upon their source (Panadare & Rathod, 2018). Some PPO molecular weight values reported from various sources are 20, 45 and 64 kDa for royal date fruits (Farouk et al ., 2020), 50 kDa for potato (Bayrak et al ., 2019); and 53.22 kDa for African bush mango ( Irvingia gabonensis ) fruit peel (Adeseko et al ., 2021). These are similar, yet differ from those of purslane PPO (163 kDa) (Gul‐Guven et al ., 2017) and fennel seeds PPO (27.8 kDa) (Yonca et al ., 2021).…”

Section: Resultsmentioning

confidence: 99%

In vitro enzymatic synthesis of a monomeric theaflavin using a polyphenol oxidase isozyme from tea (Camellia sinensis) leaf

Teng

Liu

Zeng

et al. 2021

Int J of Food Sci Tech

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Polyphenol oxidase (PPO) plays an important role in tea production, and there are many studies on the enzymatic synthesis of theaflavins using PPO; however, using a purified PPO isozyme (PPOI) instead of a crude PPO enzyme to obtain monomeric theaflavin in vitro is a novel approach that has rarely been previously reported. In the present study, a tea PPOI was purified and used for the enzymatic synthesis of theaflavin monomers. Tea leaf PPOI was purified 12.90-fold, with recovery yield of 1.30% via the sequential use of precipitation with 30%À80% saturated (NH 4 ) 2 SO 4 , Q-Sepharose Fast Flow anion exchange chromatography and Sephadex G-75 gel filtration chromatography. Subsequently, PPOI was used in the enzymatic synthesis of theaflavins: under various pH, temperatures, reaction times and catechin substrate composition and concentration, only the amount of theaflavin components produced was changed, and no other theaflavin component apart from the theaflavin monomer was produced. These results highlight the importance of monomeric theaflavin synthesis using purified PPOI isozyme and provide insight into PPO in the context of tea production.

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Purification and biochemical characterization of polyphenol oxidase of African bush mango (Irvingia gabonensis) fruit peel

Cited by 16 publications

References 46 publications

Purification and Biochemical Characterization of Polyphenol Oxidase Extracted from Wheat Bran (Wan grano)

Purification and Biochemical Characterization of Polyphenol Oxidase Extracted from Wheat Bran (Wan grano)

Biochemical properties of purified polyphenol oxidase from bitter leaf (Vernonia amygdalina)

In vitro enzymatic synthesis of a monomeric theaflavin using a polyphenol oxidase isozyme from tea (Camellia sinensis) leaf

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