This study was conducted to investigate the effect of dietary multi-enzyme (MCPC) supplementation on synergistically enhancing the functions of both the foregut and hindgut, ultimately improving the nutrient digestion and utilization throughout the gastrointestinal tract. results demonstrated that MCPC increased the phosphorus and reducing sugar levels in the supernatant during enzymatic hydrolysis. Furthermore, during the fermentation of the enzymatic hydrolysis products, MCPC significantly increased the FRD value of the enzymatic hydrolysis products from both the positive control (PC) and negative control 1 (NC1) diets ( < 0.05). MCPC reduced the T value of fermentation products from the PC diet ( < 0.01), and decreased the V ( = 0.082) and K ( < 0.05) values for the NC1 diet. Additionally, 72 crossbred barrows [Duroc × (Landrace × Yorkshire)], weighing 25 kg, were fed one of six diets until their live weight approached 50 kg. The basal diets consisted of PC, NC1 and negative control 2 (NC2), while the remaining three diets were prepared by adding 100 mg/kg MCPC to the respective basal diets. The results showed that MCPC supplementation significantly upregulated the expression of solute carrier family 17 member 4 () and vitamin D receptor () genes in the duodenum ( < 0.05), while downregulating the expression of Calbindin-D28k () and solute carrier family 1 member 4 () genes ( < 0.05) in growing pigs. Moreover, MCPC supplementation significantly upregulated the expression of , glucose transporter 2 () and intestinal fatty acid binding protein () genes in the jejunum of growing pigs. Furthermore, MCPC supplementation significantly increased the relative abundances of , and ( < 0.05), while reducing the relative abundances of and ( < 0.05) in the colon of growing pigs. In conclusion, MCPC enhances nutrient digestion and absorption in the foregut, provides fermentable substrates for hindgut microbial fermentation, and improves gut microbiota composition. This improves hindgut fermentation and supports the synergistic interaction between the foregut and hindgut, ultimately improving nutrient utilization and benefiting animal health.
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http://dx.doi.org/10.3389/fvets.2025.1554919 | DOI Listing |
Front Vet Sci
February 2025
Key Laboratory for Animal Disease Resistance Nutrition of the Ministry of Education, Animal Nutrition Institute, Sichuan Agricultural University, Chengdu, Sichuan, China.
This study was conducted to investigate the effect of dietary multi-enzyme (MCPC) supplementation on synergistically enhancing the functions of both the foregut and hindgut, ultimately improving the nutrient digestion and utilization throughout the gastrointestinal tract. results demonstrated that MCPC increased the phosphorus and reducing sugar levels in the supernatant during enzymatic hydrolysis. Furthermore, during the fermentation of the enzymatic hydrolysis products, MCPC significantly increased the FRD value of the enzymatic hydrolysis products from both the positive control (PC) and negative control 1 (NC1) diets ( < 0.
View Article and Find Full Text PDFFEBS J
March 2025
Laboratório de Síntese e Análise de Biomoléculas - LSAB, Instituto de Química, Universidade de Brasília, Brazil.
Membrane-active peptides are useful tools in the design of multifunctional molecules. For example, peptide chimeras may release, after proteolysis of membrane-adsorbed molecules, pharmacologically active fragments. In previous work, Chim2, an antimicrobial peptide composed of a membrane-active module, an enzymatic hydrolysis site, and an agonist moiety for type 2 formyl peptide receptors (FPR2), was conceptualized.
View Article and Find Full Text PDFChembiochem
March 2025
Queen's University, Chemistry, 90 Bader Lane, K7L3N6, Kingston, CANADA.
Enzymatic hydrolysis of polyethylene terephthalate (PET) is a promising technology for advancing a circular PET economy. Several PET-degrading α/β hydrolases have been identified, but the full potential of this enzyme family to catalyze PET hydrolysis remains largely unexplored. To address this, sequence similarity networks were employed to investigate the α/β hydrolase fold-5 subfamily (IPR029059) for new PETases.
View Article and Find Full Text PDFFood Chem
March 2025
Grupo de NeuroGastroBioquímica, Laboratorio de Química Biológica, Instituto de Química, Pontificia Universidad Católica de Valparaíso, Av. Universidad 330, Curauma-Placilla, Valparaíso, Chile.
This study proposed investigates the role of forced aeration flow and humidification pulses during solid-state fermentation (SSF) of spent coffee grounds (SCG) in optimizing fungal growth, metabolic activity, and bioactive compound release. Five fermentation conditions with aeration flows (0.5-1.
View Article and Find Full Text PDFInt J Biol Macromol
March 2025
State Key Laboratory of Biocatalysis and Enzyme Engineering, Environmental Microbial Technology Center of Hubei Province, College of Life Sciences, Hubei University, Wuhan 430062, PR China. Electronic address:
Alkaline protease has been commercially used in the areas of detergents, food and agriculture, and improving the performance and production of alkaline protease serves as an important role in promoting its market expansion. Here, an alkaline protease AE0 from Alkalihalobacillus clausii FYX was firstly characterized in Bacillus licheniformis DW2△aprE, the optimal temperature and pH of AE0 were 60 °C and 10.5, the K and K values for casein were 17.
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