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  1. Hau EH, Teh SS, Yeo SK, Mah SH
    J Sci Food Agric, 2022 Jan 15;102(1):233-240.
    PMID: 34081335 DOI: 10.1002/jsfa.11350
    BACKGROUND: The oil palm tree produces 90% of wastes and the limited usage of these wastes causes a major disposal problem in the mills. Nevertheless, these by-products have a large amount of nutritional components. Thus, the present study aimed to determine the physicochemical and functional properties of protein hydrolysates (PH) from oil palm leaves (OPL) extracted using different concentrations of Alcalase (0-10%) at 2 h of hydrolysis time.

    RESULTS: Fourier transform infrared spectral analyses showed that the enzymatic hydrolysis altered functional groups of OPL where a secondary amine was present in the PH. Changes were also observed in the thermal stability where the enthalpy heat obtained for PH (933.93-1142.57 J g-1 ) was much lower than OPL (7854.11 J g-1 ). The results showed that the PH extracted by 8% Alcalase exhibited absolute zeta potential, as well as a high emulsifying activity index (70.64 m2  g-1 of protein) and emulsion stability index (60.58 min). Furthermore, this PH showed higher solubility (96.32%) and emulsifying properties compared to other PHs. It is also comparable with commercial plant proteins, indicating that 8% Alcalase is an optimum concentration for hydrolysis.

    CONCLUSION: In summary, the physicochemical and functional properties of PH extracted from OPL showed good functional properties, suggesting that it can be used as an alternative plant protein in food industries. © 2021 Society of Chemical Industry.

  2. Hau EH, Chew LY, Yeo SK, Owatworakit A, Teh SS, Mah SH
    Int J Biol Macromol, 2024 Dec 17.
    PMID: 39701231 DOI: 10.1016/j.ijbiomac.2024.138897
    Diabetes, particularly type II, is a global health concern, with current treatments like α-glucosidase inhibitors often causing gastrointestinal side effects. This study explored the antihyperglycemic potential of crude protein hydrolysate from oil palm leaves (OPL) as a plant-based α-glucosidase inhibitor. OPL protein hydrolysate was extracted under acidic, neutral, and alkaline conditions, and their α-glucosidase inhibitory activity was assessed. OPL hydrolysate obtained under neutral conditions for 2 h showed the highest inhibitory activity, comparable to the standard drug, acarbose. Bioassay-guided fractionation of the most potent extract revealed that peptides from sub-fractions C1 and C9 exhibited stronger inhibition, with IC50 values of 66.3 and 62.0 μg/mL, respectively. Seven novel peptides were identified from these fractions, and molecular docking confirmed stable interactions between these peptides and the α-glucosidase enzyme via hydrogen bonds and salt bridges. These findings suggest that OPL protein hydrolysate is a plant-based promising natural α-glucosidase inhibitor with potential as an antidiabetic agent. Future studies should focus on in vivo validation of its efficacy and safety for therapeutic use.
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