Journal Articles

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    Unveiling anti-inflammatory peptides from Lion's Mane mushroom (Hericium erinaceus): Preparation, bioactivity assessment, and peptides identification
    (Elsevier B V, 2025-12-01) Silva B; Sringarm K; Potikanond S; Tangjaidee P; Buacheen P; Rachtanapun P; Donlao N; Singh J; Kaur L; Issara U; Kingwascharapong P; Phongthai S
    Lion's Mane mushroom (Hericium erinaceus) is acknowledged worldwide for its substantial contribution of medicinal compounds and nutrients, including protein. The efficient extraction and hydrolysis of proteins are essential for revealing their bioactive properties. This study demonstrates that the optimal pulsed electric field (PEF)-assisted extraction achieved a 42.44 % increase in protein extraction efficiency relative to traditional alkaline extraction (p < 0.05). H. erinaceus protein contained 44.59 % essential amino acids and exhibited 71.33 % in vitro digestibility. Pepsin-trypsin hydrolysis produced the most significant anti-inflammatory activity, resulting in a 36.2 % reduction in nitric oxide and a 31.8 % decrease in interleukin-6 levels (p < 0.05). Subsequent fractionations employing membrane ultrafiltration and size exclusion chromatography effectively purified the peptides, resulting in enhanced anti-inflammatory activity (p < 0.05). This research discovered nine important peptide sequences containing 50–100 % hydrophobic amino acids in Lion's Mane mushroom proteins, which could aid in the synthesis of natural anti-inflammatory peptides.
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    Partial hydrolyzed protein as an alternative stabilizer for peanut (Arachis hypogaea) butter
    (Elsevier Ltd, 2025-07-01) Thongkong S; Rakairyatham K; Tangjaidee P; Unban K; Klangpetch W; Phimolsiripol Y; Rachtanapun P; Rawdkuen S; Singh J; Kaur L; Issara U; Kingwascharapong P; Phongthai S
    Peanut protein hydrolysates with varying degrees of hydrolysis (DH) were prepared by using Alcalase and Flavourzyme. The enzymatic hydrolysis highly influenced a transformation of protein secondary structures, particularly from β-sheet to β-turn structures (11–21 %). The DH impacted functional properties and anti-free radicals' activity of peanut protein hydrolysates. Flavourzyme-derived protein hydrolysate (FPH) with DH5% had the maximum potential as an emulsifier (54.50 ± 0.71 %, p < 0.05). The effectiveness of protein hydrolysates in preventing the oil separation and enhancing the oxidative stability of peanut butter was dependent on the type of enzyme and DH. The inclusion of partial hydrolyzed protein (DH5%) produced by the Alcalase (APH) substantially decreased the occurrence of oil separation; whereas FPH with DH5% significantly retarded increment of PV, TBARs, CD in peanut butter during the storage period (p < 0.05). This study indicated the possible use of partial hydrolyzed proteins as a stabilizer in peanut butter by slowing lipid oxidation and increasing oil entrapment.