infection can induce necrotic enteritis and lead to significant economic loss to the chicken industry. In this study, a xylanase (Xyn10C), which effectively promotes the growth of probiotics, and a protease, which degrades the biofilm of were analyzed for their ability to alleviate -induced necrotic enteritis in broiler chickens. A total of 300 male AA chickens were divided into five treatment groups (control, no enzyme and no challenge; Cp, no enzyme, challenge; Xyn, Xyn10C plus challenge; Xyn+Am, Xyn10C+Amylase plus challenge; Xyn+Ap, Xyn10C+Alkaline protease plus challenge). The CVCC 60102 was administered orally on a daily basis to the chickens from 14 to 20 days. In comparison with Cp, Xyn+Ap significantly reduced intestinal damage in the duodenum, jejunum, and ileum of chickens challenged with ( < 0.05). The enzymes, and particularly Xyn+Ap, notably enhanced the expression of key intestinal barrier genes, reduced the IL-6 level, and decreased the DAO (diamine oxidase) level. Not unexpectedly, feeding enzymes influenced the abundance of and bacteria in the intestine. These results indicated that Xyn10C and protease can be used to alleviate intestinal damage caused by infection.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.3390/ani15020123 | DOI Listing |
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11758347 | PMC |
Publication Analysis
Top Keywords
Similar Publications
Clustered surface amino acid residues modulate the acid stability of GH10 xylanase in fungi.
Appl Microbiol Biotechnol
February 2024
Jiangsu Provincial Key Lab for Organic Solid Waste Utilization, National Engineering Research Center for Organic-Based Fertilizers, Jiangsu Collaborative Innovation Center for Solid Organic Waste Resource Utilization, Nanjing Agricultural University, Nanjing, 210095, China.
Article Synopsis
- Five highly acidic and thermostable GH10 xylanases were identified, with optimal temperatures between 70-90°C and stability at pH 2.0.
- Key amino acid sites responsible for acid stability were located in two main surface regions behind the enzyme's active center.
- The study provides insights into the interactions of amino acids that can improve both acid stability and thermostability in GH10 xylanases, offering targets for future genetic modifications.
A Novel Multifunctional Arabinofuranosidase/Endoxylanase/β-Xylosidase GH43 Enzyme from Paenibacillus curdlanolyticus B-6 and Its Synergistic Action To Produce Arabinose and Xylose from Cereal Arabinoxylan.
Appl Environ Microbiol
November 2021
School of Bioresources and Technology, King Mongkut's University of Technology Thonburi, Bangkok, Thailand.
PcAxy43B is a modular protein comprising a catalytic domain of glycoside hydrolase family 43 (GH43), a family 6 carbohydrate-binding module (CBM6), and a family 36 carbohydrate-binding module (CBM36) and found to be a novel multifunctional xylanolytic enzyme from Paenibacillus curdlanolyticus B-6. This enzyme exhibited α-l-arabinofuranosidase, endoxylanase, and β-d-xylosidase activities. The α-l-arabinofuranosidase activity of PcAxy43B revealed a new property of GH43, via the release of both long-chain cereal arabinoxylan and short-chain arabinoxylooligosaccharide (AXOS), as well as release from both the C(O) and C(O) positions of AXOS, which is different from what has been seen for other arabinofuranosidases.
View Article and Find Full Text PDFStructural and Functional Analysis of a Multimodular Hyperthermostable Xylanase-Glucuronoyl Esterase from .
Biochemistry
July 2021
Division of Industrial Biotechnology, Department of Biology and Biological Engineering, Chalmers University of Technology, SE-412 96 Gothenburg, Sweden.
The hyperthermophilic bacterium encodes an unusual enzyme, Xyn10C-GE15A, which incorporates two catalytic domains, a xylanase and a glucuronoyl esterase, and five carbohydrate-binding modules (CBMs) from families 9 and 22. The xylanase and glucuronoyl esterase catalytic domains were recently biochemically characterized, as was the ability of the individual CBMs to bind insoluble polysaccharides. Here, we further probed the abilities of the different CBMs from Xyn10C-GE15A to bind to soluble poly- and oligosaccharides using affinity gel electrophoresis, isothermal titration calorimetry, and differential scanning fluorimetry.
View Article and Find Full Text PDFMultimodularity of a GH10 Xylanase Found in the Termite Gut Metagenome.
Appl Environ Microbiol
January 2021
TBI, Université de Toulouse, CNRS, INRAE, INSA, Toulouse, France
The functional screening of a termite gut metagenomic library revealed an array of xylan-degrading enzymes, including 25 (25), a multimodular glycoside hydrolase family 10 (GH10). Sequence analysis showed details of the unusual domain organization of this enzyme. It consists of one catalytic domain, which is intercalated by two carbohydrate binding modules (CBMs) from family 4.
View Article and Find Full Text PDFThe hemicellulose-degrading enzyme system of the thermophilic bacterium : comparative characterisation and addition of new hemicellulolytic glycoside hydrolases.
Biotechnol Biofuels
August 2018
1Department of Microbiology, TUM School of Life Sciences Weihenstephan, Technical University of Munich, Emil-Ramann-Str. 4, 85354 Freising, Germany.
Background: The bioconversion of lignocellulosic biomass in various industrial processes, such as the production of biofuels, requires the degradation of hemicellulose. is a thermophilic bacterium, well known for its outstanding hemicellulose-degrading capability. Its genome comprises about 50 genes for partially still uncharacterised thermostable hemicellulolytic enzymes.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!