International Journal of Food Properties · 2023 · 12 citations · 30 references
Life SciencesBiochemistryBiotechnologyEnzymologyLipid BiochemistryMetabolismEnzyme InhibitionFatty Acid MetabolismLipid Hydrolysis In FoodsLipid MetabolismProteolytic EnzymesProteolytic ProcessingEnzymatic HydrolysisHepatic Lipid AccumulationLipasesLipid AccumulationLipid Metabolism RegulationPancreatic Lipase ActionTriglyceride HydrolysisTriglyceride Lowering
To effectively utilize the by-products of skipjack tuna (Katsuwonus Pelamis) for the preparation of peptides with lipid-lowering activity, alkaline proteinase was selected from six commercial proteases to hydrolyze dark muscle. An L16 (54) orthogonal design was employed to optimize the hydrolysis conditions, resulting in the production of a high-peptide-content hydrolyzate named KPHs-AL. This hydrolyzate exhibited the ability to significantly reduce TG content. KPHs-AL also showed higher persuasive pancreatic lipase (PL) and cholesterol esterase (CEase) inhibitory potential than various molecular weight (Mw) fractions and other enzymatic hydrolyzates, with IC50 values of 5.14 and 8.51 mg/mL, respectively. Furthermore, KPHs-AL exerted a combined effect of regulating lipid accumulation in FAA-induced steatosis HepG2 cells, leading to decreased total cholesterol (TC) and total triglyceride (TG). Based on the high binding likelihood and interaction with specific binding sites predicted by Pepsite2, 38 peptide sequences were identified as potential PL and CEase inhibitors. Hence, KPHs-AL holds promise as a beneficial component of functional food and exhibits the potential for anti-obesity effects through the alleviation of lipid accumulation
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Yumei Wang, Xinyi Li, Jiao Wang et al. · Process Biochemistry · 2022 · 145 citations
Antioxidant peptides from corn gluten meal: Orthogonal design evaluation
Cunshan Zhou, Jiali Hu, Haile Ma et al. · Food Chemistry · 2015 · 113 citations