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This study evaluated the efficacy of a multi-protease on the performance, egg quality and digestibility of laying hen. The study had four treatments: Control (without multi-protease, CON), Pro 1.2 (CON + 0.1% multi-protease), Pro 2.4 (CON + 0.2% multi-protease) and Pro 3.6 (CON + 0.3% multi-protease). Each treatment was replicated six times (replicate = experimental unit = one pen with 15 hens) to give a total of 360 layer hens of the Hy-line breed. The study lasted for a total of 3 months (14 day adaptation period + 84 days experimental period). The effects of the additive were assessed on: the performance variables, egg quality and ileal amino acid (AA) digestibility. At the end of the study, dietary supplementation with Pro 2.4 and Pro 3.6 improved (p < 0.05) hen-day egg production, egg mass and eggshell thickness compared with CON at the peak phase. Further improvements (p < 0.05) were observed in the digestibility of crude protein and AAs such as isoleucine, lysine, threonine and cysteine at Pro 2.4 and Pro 3.6 protease supplementation levels compared with CON, while arginine and alanine were higher (p < 0.05) at Pro 3.6 compared with CON. No differences were reported for other performances such as body weight, average daily feed intake, average egg weight, feed conversion ratio, eggshell hardness and all the egg qualities measured. Overall, the results from this study showed better efficacy at Pro 2.4 and Pro 3.6 on the performance of laying hen during the peak phase.
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http://dx.doi.org/10.1111/jpn.13993 | DOI Listing |
Bioinformatics
August 2025
Department of Statistical Sciences, University of Bologna, Bologna 40126, Italy.
Motivation: Studying protein isoforms is an essential step in biomedical research; at present, the main approach for analyzing proteins is via bottom-up mass spectrometry proteomics, which return peptide identifications, that are indirectly used to infer the presence of protein isoforms. However, the detection and quantification processes are noisy; in particular, peptides may be erroneously detected, and most peptides, known as shared peptides, are associated to multiple protein isoforms. As a consequence, studying individual protein isoforms is challenging, and inferred protein results are often abstracted to the gene-level or to groups of protein isoforms.
View Article and Find Full Text PDFbioRxiv
May 2025
Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, University of Utrecht, Padualaan 8, Utrecht 3584 CH, the Netherlands and Netherlands Proteomics Center, Padualaan 8, Utrecht 3584 CH, the Netherlands.
The ability to sequence proteins without reliance on a genomic template defines a critical frontier in modern proteomics. This approach, known as protein sequencing, is essential for applications such as antibody sequencing, microbiome proteomics, and antigen discovery, which require accurate reconstruction of peptide and protein sequences. While trypsin remains the gold-standard protease in proteomics, its restricted cleavage specificity limits peptide diversity.
View Article and Find Full Text PDFJ Anim Sci Technol
May 2024
Kemin Animal Nutrition and Health, Herentals 2200, Belgium.
This study aimed to evaluate the effect of supplementing different protease enzymes on growth performance, intestinal morphology, and selected carcass traits in broilers fed diets reduced 3.5% in crude protein (CP) and amino acids (AA). One thousand one-day-old Ross 308 broilers (41 g) were assigned to five dietary treatments with ten replicates of 20 birds each: a positive control (PC) diet formulated to meet Ross 308 AA requirements, a negative control (NC) diet reformulated to provide 3.
View Article and Find Full Text PDFbioRxiv
May 2025
Department of Statistical Sciences, University of Bologna, Bologna, Italy.