Low protein digestibility causes intestinal flora imbalance, wet litter, and nitrogen pollution. The present study aimed to explore the optimal zymogram of exogenous acid protease (ACP), neutral protease (NEP), alkaline protease (ALP), and keratinase (KEA) in corn-soybean based diets for broilers. The hydrolysis performances of the four monocomponent proteases were presented by enzymatic hydrolysate gross energy (EHGE) and improved dry matter digestibility (IDMD), which were tested via the in vitro simulated digestion method. The optimal combination of the four proteases was predicted by the response surface method. Results showed that the optimal zymogram for 1 to 3-wk-old broiler diet was 1.80 U/g ACP, 2.30 U/g NEP, 29.30 U/g ALP, and 2.80 U/g KEA, and the EHGE and IDMD reached 94.65 Cal/g and 2.54%. The optimal zymogram for 4 to 6-wk-old broiler diet was 1.50 U/g ACP, 1.90 U/g NEP, 31.53 U/g ALP, and 3.10 U/g KEA, and the EHGE and IDMD reached 92.29 Cal/g and 2.47%. The performances of the predicted optimal zymogram were further verified by in vitro simulated digestion method. Collectively, the combined use of four proteases could improve the protein digestibility in broiler diets, which had better effect than monocomponent protease.
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http://dx.doi.org/10.1038/s41598-025-88954-w | DOI Listing |
Sci Rep
February 2025
Department of Animal Nutrition, Hunan Institute of Animal Husbandry and Veterinary Medicine, Changsha, 410125, China.
Low protein digestibility causes intestinal flora imbalance, wet litter, and nitrogen pollution. The present study aimed to explore the optimal zymogram of exogenous acid protease (ACP), neutral protease (NEP), alkaline protease (ALP), and keratinase (KEA) in corn-soybean based diets for broilers. The hydrolysis performances of the four monocomponent proteases were presented by enzymatic hydrolysate gross energy (EHGE) and improved dry matter digestibility (IDMD), which were tested via the in vitro simulated digestion method.
View Article and Find Full Text PDFInt J Biol Macromol
January 2025
Department of Biotechnology, University of North Bengal, Raja Rammohunpur, Darjeeling, West Bengal 734013, India. Electronic address:
Xylooligosaccharides (XOS) are excellent prebiotic which improve health through selective modulation of beneficial gut microbiome. Its production from agroresidues using microbial xylanase is considered as sustainable and economic approach. In this study a xylanase producing bacterium isolated from decaying wood soil was phylogenetically identified and designated as Bacillus stercoris DWS1.
View Article and Find Full Text PDFAMB Express
November 2024
Department of Microbiology and Immunology, Faculty of Pharmacy, Ain Shams University, Organization of African Unity St., POB: 11566, Abbassia, Cairo, Egypt.
A high cellulase-producing bacterial isolate TS4 was recovered from an Egyptian soil sample and identified using 16S rRNA gene sequencing as Streptomyces thermodiastaticus. One-factor-at-a-time (OFAT) preliminary studies were carried out to determine the key factors affecting cellulase production by S. thermodiastaticus and their optimum ranges.
View Article and Find Full Text PDFMicrob Cell Fact
October 2024
Botany and Microbiology Department, Faculty of Science, Tanta University, Tanta, 31527, Egypt.
Background: Hazardous synthetic dye wastes have become a growing threat to the environment and public health. Fungal enzymes are eco-friendly, compatible and cost-effective approach for diversity of applications. Therefore, this study aimed to screen, optimize fermentation conditions, and characterize laccase from fungal endophyte with elucidating its ability to decolorize several wastewater dyes.
View Article and Find Full Text PDFInt J Biol Macromol
July 2024
Department of Basic Medical Sciences, Vision College in Riyadh, Saudi Arabia. Electronic address:
Wound healing involves several cellular and molecular pathways. Tridax procumbens activates genetic pathways with antibacterial, antioxidant, anticancer, and anti-inflammatory properties, aiding wound healing. This study purified Procumbenase, a serine protease from T.
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