Research has shown various hydrolyzed proteins possessed beneficial physiological functions; however, the mechanism of how hydrolysates influence metabolism is unclear. Therefore, the current study aimed to examine the effects of different sources of protein hydrolysates, being the main dietary protein source in extruded diets, on metabolism in healthy adult dogs. Three complete and balanced extruded canine diets were formulated: control chicken meal diet (CONd), chicken liver and heart hydrolysate diet (CLHd), mechanically separated chicken hydrolysate diet (CHd). A replicated 3 × 5 Latin rectangle design was used with 10 adult beagles. Within each period, the assigned diets were fed to the beagles for 28 days after a 7-day wash out period. Plasma and fresh fecal samples were collected at day 28. Samples of diets, plasma, and feces were analyzed for global metabolomics with ultra-performance liquid chromatography and quadrupole-Orbitrap high-resolution mass spectrometer interfaced with a heated electrospray ionization source and mass analyzer. In general, there were lower fecal concentrations of dipeptides and protein degradation metabolites, indicating higher protein digestibility, in dogs fed protein hydrolysate diets in contrast with CONd (q < 0.05). Higher plasma pipecolate and glutamate, higher fecal spermidine and indole propionate, and lower phenol-derived products in both plasma and feces were found in CLHd group than CONd (q < 0.05), indicating lower oxidative stress and inflammation levels. The main difference in lipid metabolism between CHd and CONd was the bile acid metabolism, showing lower circulating bile acid, lower unconjugated bile acid excretion and higher taurine-conjugated bile acid excretion in the CHd group (q < 0.05). In conclusion, using chicken hydrolysates as the main protein source in extruded canine diets showed potential for physiological benefits in healthy adult dogs, especially protein hydrolysate from chicken heart and liver demonstrated effects on lowering inflammation and oxidation levels.
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http://dx.doi.org/10.1038/s41598-024-80176-w | DOI Listing |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11685506 | PMC |
J Agric Food Chem
January 2025
Faculty of Mechanical and Process Engineering, Hochschule Offenburg, 77652 Offenburg, Germany.
Protein hydrolysis under acidic conditions can improve the product quality, nutrient availability, and cost efficiency, particularly when neutral or alkaline enzymes are ineffective. Six fungal aspartic endopeptidases (FAPs) were recombinantly expressed as active enzymes in , with peak activity between 30-50 °C and pH 3.0-4.
View Article and Find Full Text PDFSci Rep
January 2025
Tianjin Key Laboratory of Intelligent Breeding of Major Crops, College of Agronomy & Resources and Environment, Tianjin Agricultural University, Tianjin, 300384, China.
Rice is susceptible to cold temperatures, especially during the seedling stage. Despite extensive research into the cold tolerance mechanisms of rice, the number of cloned genes remains limited. Plant subtilisin-like proteases (SUBs or SBTs) are protein-hydrolyzing enzymes which play important roles in various aspects of plant growth as well as the plant response to biotic and abiotic stress.
View Article and Find Full Text PDFmLife
December 2024
State Key Laboratory of Mycology, Institute of Microbiology Chinese Academy of Sciences Beijing China.
Glycosylphosphatidylinositol (GPI) anchoring is one of the conserved posttranslational modifications in eukaryotes that attach proteins to the plasma membrane. In fungi, in addition to plasma membrane GPI-anchored proteins (GPI-APs), some GPI-APs are specifically released from the cell membrane, secreted into the cell wall, and covalently linked to cell wall glucans as GPI-anchored cell wall proteins (GPI-CWPs). However, it remains unclear how fungal cells specifically release GPI-CWPs from their membranes.
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December 2024
Gujarat Biotechnology Research Centre, Gandhinagar - 382011, Gujarat, India. Electronic address:
Plant glucanases, including potato glucanase, are pivotal in biological processes such as cell growth, development, and defense against pathogens. These enzymes hold substantial promises in biotechnological applications, especially genetic engineering for enhancing crop disease resistance and stress tolerance. In this study, from Solanum tuberosum, glycosyl hydrolases family 17 (GH-17) β-1,3-glucanase (Stglu) was cloned, expressed, characterized and its antifungal activity was evaluated.
View Article and Find Full Text PDFJ Agric Food Chem
January 2025
School of Chemistry and Life Sciences, Suzhou University of Science and Technology, Suzhou 215009, PR China.
Rapeseed meal (RSM), a protein-rich byproduct, holds potential as a high-quality animal feed, but nitrile compounds derived from glucosinolates (GSLs) in RSM pose a toxicity risk. Nitrilases, enzymes that hydrolyze toxic nitriles to carboxylic acids, offer a potential solution for detoxification. However, the low thermal stability of nitrilases restricts their industrial applicability.
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