Enzymatic Release of Fucose
Fucose is released from fucose-containing polymers by an enzyme found in lysosomes called α-fucosidase. CD BioGlyco has advanced Enzymatic Release methods to provide clients with high-quality fucose release services.
Overview of Fucose
Fucose is a deoxyhexose sugar with the chemical formula C6H12O5, which is present in a variety of glycoproteins and glycolipids produced by insects, plant cells, and mammals. In mammals, fucose-containing glycans play important roles in transfusion responses, host-microbe interactions, selectin-mediated leukocyte-endothelial adhesion, and many ontogenic events. Fucosylation is the transfer of fucose residues from guanosine diphosphate (GDP)-fucose donor to an acceptor molecule and is part of the ABO blood group and Lewis antigen systems. According to the different fucose addition sites, fucosylation is divided into α1-2-, α1-3/4-, α1-6-, and O-fucosylation. In humans, fucosylation is carried out by a group of 13 enzymes, each showing a specific activity.
The potential applications of fucose are becoming increasingly apparent in the fields of medicine and dietary supplements. In immunoglobulins, fucosylation of antibodies has been established to reduce binding to Fc receptors on natural killer cells, thereby reducing antibody-dependent cell-mediated cytotoxicity (ADCC). Therefore, fucosylated monoclonal antibodies have been designed to recruit the immune system to cancer cells and have been made in cell lines lacking the core fucosylase (FUT8), thereby enhancing cell killing in vivo.
Key Technologies
CD BioGlyco leverages a suite of cutting-edge technologies to ensure precise and efficient enzymatic release of fucose. Our core technological platform integrates highly specific fucosidases, including alpha-L-fucosidases and beta-D-fucosidases, tailored for various linkage types (e.g., alpha1-2, alpha1-3, alpha1-4, alpha1-6). These enzymes are meticulously selected and optimized for purity and activity to ensure complete and selective fucose removal without compromising the integrity of the remaining glycan structure.
Unlocking Glycan Insights, One Fucose at a Time
Enzymes are useful for the structural analysis of glycans and polysaccharides and for establishing structure-activity relationships in biological systems. Due to the biological importance of fucose, it is highly necessary to develop a systematic strategy to release fucose from protein. At CD BioGlyco, we have developed a Glycan Release platform to provide clients with efficient and accurate fucose release services. Fucosidase is a unique tool for hydrolyzing fucose on proteins. Under the action of fucosidase, we efficiently release α1-2, α1-3, and α1-4 linked fucose present on N-glycosylated proteins, O-glycosylated proteins, or free oligosaccharides.
Fig.1 The process of enzymatic release of fucose. (CD BioGlyco)
Our capabilities extend to various sample types, including purified glycoproteins, recombinant proteins, monoclonal antibodies (mAbs), serum, plasma, cell lysates, and tissue samples. We provide a comprehensive analysis of both N-linked and O-linked glycans, as well as glycosphingolipids, allowing for a holistic understanding of fucosylation patterns.
Workflow
Publication Data
Journal: International Journal of Molecular Sciences
IF: 5.5
Published: 2024
Results: The article describes the identification and characterization of four new α-L-fucosidases discovered through a screen of an alpaca feces metagenomic library. The authors studied the enzymatic parameters of these fucosidases using p-nitrophenyl α-L-fucopyranoside as a substrate and explored their potential for use as transglycosidases with various mono-, di-, tri-, and oligosaccharides, as well as some amino acids. The findings highlight the hydrolytic capabilities of these novel enzymes and their promising applications in transfucosylation reactions, contributing to the broader field of enzyme discovery and glycoengineering.
Applications
- Immunology and vaccine development: Crucial for understanding the role of fucosylation in immune recognition, antigenicity, and the development of more effective vaccines and immunotherapies.
- Cancer research: Provides insights into altered fucosylation patterns in cancer cells, which are often associated with metastasis, angiogenesis, and drug resistance, aiding in the development of targeted cancer therapies.
- Development of glyco-engineered therapeutics: Supports the engineering of glycoproteins with optimized fucosylation profiles to enhance their therapeutic properties, such as improved effector functions of antibodies.
- Fundamental glycobiology research: Enables the detailed structural and functional elucidation of fucosylated glycans, contributing to a deeper understanding of their biological roles in health and disease.
Advantages
- Unparalleled specificity and purity: Our commitment to using highly purified and specific fucosidases ensures that only fucose residues are targeted, preserving the integrity of the underlying glycan structures.
- Optimized protocols for diverse samples: With extensive experience across a wide range of biological samples, CD BioGlyco has developed and refined robust protocols that are adaptable to various sample matrices, ensuring consistent and reliable fucose release regardless of complexity.
- Expert data interpretation and support: Beyond generating data, our team of seasoned glycobiology specialists provides expert interpretation, helping clients translate complex analytical results into meaningful biological conclusions. We offer dedicated support throughout the project lifecycle.
Frequently Asked Questions
CD BioGlyco not only provides a systematic experimental platform and advanced technical approaches, but also provides flexible guidance to help clients complete their scientific research work in a timely and efficient manner. If you are interested in our fucose release services, please contact us for more detailed information.
Associated Services
References
- Roca, C.; et al. Exopolysaccharides enriched in rare sugars: bacterial sources, production, and applications. Frontiers in microbiology. 2015, 10(6): 288. (Open Access)
- Krupinskaitė, A.; et al.α-L-Fucosidases from an alpaca faeces metagenome: characterisation of hydrolytic and transfucosylation potential. International Journal of Molecular Sciences. 2024, 25(2): 809. (Open Access)
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- Glucose Metabolism-Microenvironment Crosstalk Analysis in Cancer
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- Discovery of Cancer Glucose Metabolism Small Molecule Inhibitor
- Discovery of Cancer Glucose Metabolism Therapeutic Monoclonal Antibodies
- Development of Gene Therapy Targeting Cancer Glucose Metabolism
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