Search Results (3)

Immunodeficiency can disrupt normal physiological activity and function. In this study, donkey bone collagen peptide (DP) and its iron chelate (DPI) were evaluated their potential as immunomodulators in cyclophosphamide (Cytoxan^®, CTX)-induced Balb/c mice. The femoral tissue, lymphocytes, and serum from groups of mice were subjected to hematoxylin and eosin (H&E) staining, methylthiazolyldiphenyl-tetrazolium bromide (MTT) cell proliferation assays, and enzyme-linked immunosorbent assay (ELISA), respectively. Furthermore, a non-targeted metabolomics analysis based on UPLC–MS/MS and a reverse transcription polymerase chain reaction (RT-qPCR) technology were used to explore the specific metabolic pathways of DPI regulating immunocompromise. The results showed that CTX was able to significantly reduce the proliferative activity of mouse splenic lymphocytes and led to abnormal cytokine expression. After DP and DPI interventions, bone marrow tissue damage was significantly improved. In particular, DPI showed the ability to regulate the levels of immune factors more effectively than Fe²⁺ and DP. Furthermore, metabolomic analysis in both positive and negative ion modes showed that DPI and DP jointly regulated the levels of 20 plasma differential metabolites, while DPI and Fe²⁺ jointly regulated 14, and all 3 jointly regulated 10. Fe²⁺ and DP regulated energy metabolism and pyrimidine metabolism pathways, respectively. In contrast, DPI mainly modulated the purine salvage pathway and the JAK/STAT signaling pathway, which are the key to immune function. Therefore, DPI shows more effective immune regulation than Fe²⁺ and DP alone, and has good application potential in improving immunosuppression. Full article

Freeze dried protein powders (Fresh minced meat, FMM and Hot water dip, HWD) from tilapia (Oreochromis niloticus) were hydrolyzed by Alcalase 2.4 L (Alc), Flavourzyme (Flav) and Neutrase (Neut), and investigated for antioxidant activity and their functional properties. FMM and HWD hydrolysed by Alc, exhibiting superior antioxidant activity, had estimated degrees of hydrolysis (DH) of 23.40% and 25.43%, respectively. The maximum values of the 1,1-diphenyl-2-picrylhydrazyl (DPPH), 2,2-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt (ABTS), 3-(2-pyridyl) 5,6-bis(4-phenyl-sulphonic acid)-1,2,4-triazine (ferrozine), radical scavenging activities and metal chelating properties were 86.67%, 91.27% and 82.57%, and 84.67%, 92.60% and 78.00% for FMM and HWD, respectively, with a significant difference (P < 0.05) between the samples. Essential amino acids were above the amounts recommended by the Food and Agricultural Organization/World Health Organization (FAO/WHO/UNU) for humans. Lower molecular weight sizes <3,000 Da were more predominant in FMM and HWD hydrolysed by Alc, while in hydrolysed by Flav and Neut they were >8,000 Da. At pH 2, FMM and HWD hydrolysates have varying solubilities above 85% (Alc FMM; 91.33%, Flav FMM; 79.5%, Neut FMM; 83.8% and Alc HWD; 90.45%, Flav HWD; 83.5%, and Neut HWD; 85.8%). They have ‘U’ shaped solubility curves, water holding capacity was in the range of 2.77 and 1.77 mL/g, while oil holding capacity ranged between 3.13 and 2.23 mL/g. FMM and HWD have the highest bulk density of 0.53 and 0.53 for Neutrase and Alcalase 2.4 L, respectively. Foam capacity and stability ranged from 125.5 to 61.4, 138.5 to 45.2, 130.0 to 62.5, and 124.5 to 55.0, 137.5 to 53.3, 129.6 to 62.7 for FMM and HWD hydrolyzed with Alcalase 2.4 L, Flavourzyme and Neutrase, respectively. Tilapia fish protein hydrolysates are thus potential functional food ingredients. Full article

Two varieties of foxtail millet protein concentrates (white and yellow) were characterized for in vitro trypsin digestibility, functional and physicochemical properties. Millet protein concentrate was easily digested by trypsin in vitro. Essential amino acids were above the amounts recommended by the Food Agricultural Organization/World Health Organization (FAO/WHO/UNU) for humans. Yellow millet protein concentrate (YMPC) possessed the highest differential scanning calorimetry result (peak temperature of 88.98 °C, delta H = 0.01 J/g), white millet protein concentrate (WMPC) had the lowest (peak temperature 84.06 °C, delta H = 0.10 J/g). The millet protein concentrates had molecular sizes around 14.4 and 97.4 kDa. They have U-shape solubility curves. Waterbinding capacity was in the range of 5.0 and 7.0 g/g, while oil absorption capacity ranged between 4.8 and 5.9 g/g. WMPC had higher bulk density (0.22 g/mL) and emulsifying capacity than YMPC and Soy Protein Concentrate (SPC). Foam capacity and foam stability ranged from 137 to 73 g/mL for WMPC, from 124 to 61 g/mL SPC and from 124 to 46 g/mL for YMPC. Millet protein concentrates are potential functional food ingredients. Full article