Microorganisms play a primary role in regulating biogeochemical cycles and are a valuable source of enzymes that have biotechnological applications, such as carbohydrate-active enzymes (CAZymes). However, the inability to culture the majority of microorganisms that exist in natural ecosystems using common culture-dependent techniques restricts access to potentially novel cellulolytic bacteria and beneficial enzymes. The development of molecular-based culture-independent methods such as metagenomics enables researchers to study microbial communities directly from environmental samples, and presents a platform from which enzymes of interest can be sourced. We outline key methodological stages that are required as well as describe specific protocols that are currently used for metagenomic projects dedicated to CAZyme discovery.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1007/978-1-4939-6899-2_20 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
CAZymes ( C arbohydrate A ctive En Zymes ) degrade, synthesize, and modify all complex carbohydrates on Earth. CAZymes are extremely important to research in human health, nutrition, gut microbiome, bioenergy, plant disease, and global carbon recycling. Current CAZyme annotation tools are all based on sequence similarity.
View Article and Find Full Text PDFMetagenome-based diversity and functional analysis of culturable microbes in sugarcane.
Microbiol Spectr
November 2024
State Key Laboratory for Conservation and Utilization of Subtropical Agro-Bioresources, Guangxi University, Nanning, China.
Unlabelled: Sugarcane is a key crop for sugar and energy production, and understanding the diversity of its associated microbes is crucial for optimizing its growth and health. However, there is a lack of thorough investigation and use of microbial resources in sugarcane. This study conducted a comprehensive analysis of culturable microbes and their functional features in different tissues and rhizosphere soil of four diverse sugarcane species using metagenomics techniques.
View Article and Find Full Text PDFA cellulose-binding domain specific for native crystalline cellulose in lytic polysaccharide monooxygenase from the brown-rot fungus Gloeophyllum trabeum.
Carbohydr Polym
January 2025
Faculty of Agriculture, Tokyo University of Agriculture and Technology, Tokyo, Japan; United Graduate School of Agricultural Science, Tokyo University of Agriculture and Technology, Tokyo, Japan; Institute of Agriculture, Tokyo University of Agriculture and Technology, Tokyo, Japan. Electronic address:
Cellulose-binding domains (CBDs) play a vital role in cellulose degradation by enzymes. Despite the strong ability of brown-rot fungi to degrade cellulose in wood, they have been considered to lack or have a low number of enzymes with CBD. Here, we report the C-terminal domain of a lytic polysaccharide monooxygenase from the brown-rot fungus Gloeophyllum trabeum (GtLPMO9A-2) functions as a CBD, classified as a new family of carbohydrate-binding module, CBM104.
View Article and Find Full Text PDFA "terminal" case of glycan catabolism: Structural and enzymatic characterization of the sialidases of Clostridium perfringens.
J Biol Chem
October 2024
Department of Biochemistry & Microbiology, University of Victoria, Victoria, British Columbia, Canada. Electronic address:
Sialic acids are commonly found on the terminal ends of biologically important carbohydrates, including intestinal mucin O-linked glycans. Pathogens such as Clostridium perfringens, the causative agent of necrotic enteritis in poultry and humans, have the ability to degrade host mucins and colonize the mucus layer, which involves removal of the terminal sialic acid by carbohydrate-active enzymes (CAZymes). Here, we present the structural and biochemical characterization of the GH33 catalytic domains of the three sialidases of C.
View Article and Find Full Text PDFFrom Mechanism-Based Retaining Glycosidase Inhibitors to Activity-Based Glycosidase Profiling.
J Am Chem Soc
September 2024
Leiden Institute of Chemistry, Leiden University, 2300 RA, Leiden, The Netherlands.
Activity-based protein profiling (ABPP) is an effective technology for the identification and functional annotation of enzymes in complex biological samples. ABP designs are normally directed to an enzyme active site nucleophile, and within the field of Carbohydrate-Active Enzymes (CAZymes), ABPP has been most successful for those enzymes that feature such a residue: retaining glycosidases (GHs). Several mechanism-based covalent and irreversible retaining GH inhibitors have emerged over the past sixty years.
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!