2016
DOI: 10.1007/s11738-016-2339-8
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Subcellular extraction and enzyme characterisation of polyphenol oxidase and peroxidase in Cinnamon myrtle

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Cited by 9 publications
(6 citation statements)
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“…As shown in Figure 5a, the different PPO optimal inhibitors types were found and it depends on substrate used. For mPPO, the best inhibitor GSH, which exhibited an non‐competitive inhibition mechanism with catechol as substrate, and GSH will not compete for the active sites between mPPO and substrates (Figure 5a (c)), which was similar to cinnamon myrtle (Sommano, Kumpoun, & Yusuf, 2017), while an anti‐competitive inhibition for GSH using 4‐methylcatechol (Figure 5b (c)). Ascorbic acid‐induced mixed‐type inhibition on sPPO1 with chlorogenic acid as substrate and may bind to both sPPO1 and enzyme‐substrate complex (Figure 5a (a)), which was close to faba bean (Choudhary & Mishra, 2018).…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…As shown in Figure 5a, the different PPO optimal inhibitors types were found and it depends on substrate used. For mPPO, the best inhibitor GSH, which exhibited an non‐competitive inhibition mechanism with catechol as substrate, and GSH will not compete for the active sites between mPPO and substrates (Figure 5a (c)), which was similar to cinnamon myrtle (Sommano, Kumpoun, & Yusuf, 2017), while an anti‐competitive inhibition for GSH using 4‐methylcatechol (Figure 5b (c)). Ascorbic acid‐induced mixed‐type inhibition on sPPO1 with chlorogenic acid as substrate and may bind to both sPPO1 and enzyme‐substrate complex (Figure 5a (a)), which was close to faba bean (Choudhary & Mishra, 2018).…”
Section: Resultsmentioning
confidence: 99%
“…As shown in Figure 5a, the different PPO optimal inhibitors types were found and it depends on substrate used. For mPPO, the best inhibitor GSH, which exhibited an non-competitive inhibition mechanism with catechol as substrate, and GSH will not compete for the active sites between mPPO and substrates (Figure 5a (c)), which was similar to cinnamon myrtle (Sommano, Kumpoun, & Yusuf, 2017),…”
Section: Inhibition Kineticsmentioning
confidence: 99%
“…As presented in Table 1, enzyme-assisted extraction exhibited considerably higher RA content than conventional extractions (no enzyme), indicating that enzymes increased the extraction efficiency. This result could be because phenolic compounds, including RA, are localized in the cell walls, vacuoles of the plant cells, and associated with the cell nucleus (Pinelo et al, 2006;Sommano et al, 2017). The enzymes are, therefore, required to hydrolyze the structures of plant cell walls and cell membranes (Liu et al, 2019;Su et al, 2020), thus enhancing the release of RA from the cells.…”
Section: Enzyme Screeningmentioning
confidence: 99%
“…The bound phenolics present in rice bran amounted to more than 70% of the total phenolic and are having a higher antioxidant capacity than free phenolics. These bound phenolics are not easily extracted in aqueous or organic solvents, and to improve their extractability, chemical degradation or disruption of plant cell wall matrices has been commonly employed by acid or base hydrolysis [49]. However, those treatments are not desired to be practiced at a commercial scale because the degradation often results in increasing viscosity due to fiber dissolution and thus inhibiting the extraction of phenolic compounds [25].…”
Section: Free and Bound Phenolic Compounds In Rice Branmentioning
confidence: 99%