Review Article

Roles of Dietary Bioactive Peptides in Redox Balance and Metabolic Disorders

Table 2

Mechanisms of action of antiobesity peptides derived from various food sources.

Dietary protein sourceEnzyme used to produce peptidesPeptide sequence or molecular weightObjectDose & durationActivity/mechanisms of actionReference

Soy proteinFlavourzyme<1300 Da3T3-L1 preadipocytes100 ppm for 8 dPeptides reduced GPDH activity and inhibited adipogenesis by affecting the expression of PPAR-γ and CCAAT/enhancer binding protein-α[123]
Smooth hound (Mustelus mustelus) muscle proteinAlkaline crude enzymes from M. mustelus intestines200–2500 DaRats0.5 mL (10 mg/mL)/day/kg BW for 21 dPeptides reduced BW and food intake[5]
Soy proteinFlavourzymeILL, LLL, and VHVV3T3-L1 adipocytes4 ppm for 72 hPeptides exhibited lipolysis-stimulating activity[52]
Canola proteinAlcalase, chymotrypsin, pepsin trypsin, and pancreatin<1–10 kDaC3H10T1/2 murine mesenchymal stem cells60–100 μg/mL for 24 hPeptides showed antiobesity effects by inhibiting PPARγ expression and pancreatic lipase[54]
Common beanAlcalase, bromelain, and pepsin-pancreatin<1 kDaMature adipocytes 3T3-L10.1, 1, 10, and 100 μg/mL for 48 hPeptides inhibited lipid accumulation (28%)[53]
Salmon proteinPlacebo-controlled, randomized clinical study16 g for 42 daysPeptide supplementation for 42 days reduced the body mass index by 5.6% in overweight subjects[59]
Ark shell (Scapharca subcrenata) proteinPepsin<1 kDaMouse mesenchymal stem cells400 μg/mL for 7 dPeptides inhibited intracellular lipid accumulation and enhanced lipolysis. Peptides inhibited adipogenesis by downregulating the adipocyte-specific protein expression including PPAR-γ, C/EBP-α, SREBP-1c, downstream lipoprotein lipase, and FAS expression[51]
Yellow catfish proteinAlcalaseHFD fed mice500, 250 and 125 mg/kg BW for 84 dPeptides exhibited anti-obesity effects[124]
Sardinella (Sardinella aurita) proteinBacillus subtilis A26 and Bacillus amyloliquefaciens An6150–900 DaWistar rats fed high caloric diet400 mg/kg BW for 10 weeksPeptides reduced BW gain, food intake, and the relative epididymal adipose tissue and decreased the pancreatic lipase activity[2]
Alaska pollack proteinPepsin and pancreatinRats0, 100, and 300 mg/kg BW for 3 dPeptides reduced white adipose tissue weight and food intake[56]
Tuna skinSubcritical water hydrolysis3T3-L1 preadipocytes and obese mice fed HFD300 mg/kg/day for 8 weeksPeptides decreased HFD-induced BW gain and inhibited the expression of C/EBP-α, PPAR-γ and adipocyte protein 2[55]
Camel whey proteinPepsin, trypsin, and chymotrypsin<10 kDaIn vitro assays50 μL for 30 minPeptides exhibited antiobesity effects by inhibiting pancreatic lipase and cholesteryl esterase enzymes[125]
Skate (Raja kenojei) skin collagen1050 DaHFD-fed mice100, 200, or 300 mg/kg BW for 8 weeksPeptides showed antiobesity effects by reducing BW gain and visceral adipose tissue and improved the dyslipidemia via regulating hepatic lipid metabolism and AMPK[126]
Camel milkAlcalase, bromelin, and papain<10 kDaIn vitroPeptides inhibited the porcine pancreatic lipase[24]
Kefir>30 kDa, 3–30 kDa, and <3 kDaHFD-induced obese rats164 mg/kg BW daily for 8 weeksPeptides blocked lipogenesis by reducing FAS and increased p-acetyl-CoA carboxylase. Peptides enhanced FA oxidation via increasing the expressions of phosphorylated AMPK, PPAR-α, and hepatic carnitine palmitoyltransferase-1[127]
Spirulina platensis proteinTrypsin, alcalase, pepsin, papain, and protamexNALKCCHSCPA, LNNPSVCDCDCMMKAAR, NPVWKRK, and CANPHELPNK3T3-L1 preadipocytes1 mg/mL for 48 hPeptides exhibited antiobesity effects by inhibiting lipase (72%) and 3T3-L1 preadipocytes (72.7–88.1%) and decreased triglyceride accumulation[8]
Quinoa proteinPapain, pepsin, and pancreatinFGVSEDIAEKLQAKQDERGNIVL, AEGGLTEVWDTQDQQF, YIEQGNGISGLMIPG, AVVKQAGEEGFEW, and HGSDGNVF3T3-L1 cells0–1600 μg/mL for 48 hPeptides inhibited lipid accumulation during differentiation and suppressed cell differentiation through PPAR-γ[128]
Spirulina platensis proteinPepsin<10 kDaHFD-fed mice2 g/kg BW/d for 4 weeksPeptides showed antiobesity effects reducing BW, lowering serum glucose, and total cholesterol through modulation of expressions of Acadm, Retn, Fabp4, Ppard, and Slc27a1 in the brain and liver[57]
Pea (Pisum sativum L.) seed proteinsPepsin and pancreatin<6 kDa3T3-L1 murine preadipocytes0, 1, 2, 4, and 6 mg/mL for 24 hPeptides stimulated adipocyte differentiation through upregulation of PPAR-γ expression and ligand activity[48]
Walleye pollock skin collagenFlavourzyme and alcalase500–5000 DaHFD-fed C57BL/6J mice800 mg/kg BW for 8 weeksPeptides inhibited weight gain, adipocyte growth, adipose tissue accumulation, and liver weight and reduced the blood-lipid level[58]
Blue musselPepsin<1 kDaMouse mesenchymal stem cells100, 200, and 400 μg/mL for 7 or 21 dPeptides enhanced lipolysis and downregulated adipogenic transcription factors including PPARγ, CCAAT/enhancer-binding protein-α, and SREBP-1[10]
Hazelnut (Corylus heterophylla Fisch) proteinAlcalaseArg-Leu-Leu-Pro-His3T3-L1 adipocytes0, 20, 40, and 80 mM for 8 dPeptides decreased adipogenesis by downregulating the expression of PPAR-γ, C/EBP-α, aP2, SREBP-1c, FAS, ACC1, and 3-hydroxy-3-methylglutaryl-CoA reductase[13]
Milk β-caseinTrypsin7 kDaHepG2 cells and humans5 mg/mL for 24 hCasein oligopeptide increased FGF-21[129]

ACC1: acetyl-CoA carboxylase 1; AMPK: AMP-activated protein kinase; aP2: adipocyte fatty acid-binding protein 2; BW: body weight; C/EBP-α: CCAAT/enhancer binding protein alpha; FAS: fatty acid synthase; FGFs: fibroblast growth factors; HFD: high-fat diet; PPAR-γ: peroxisome proliferator-activated receptor-γ; SREBP-1: sterol regulatory element-binding protein 1.