Glycoprotein Cleaving Enzyme Isolated from Bifidobacteria

Abstract

Researchers at the University of California, Davis have developed deglycosylating enzymes that enable efficient cleavage of diverse N-glycans from glycoproteins with broad substrate specificity and heat stability for applications in food, pharmaceuticals, and biotechnology.

Full Description

This technology provides novel endoglycosidase enzymes from Bifidobacteria that cleave the core pentasaccharide of N-glycans from glycoproteins. Unlike previously known enzymes, these enzymes display broad substrate specificity, being capable of cleaving high mannose, complex, and hybrid N-glycans, including those with terminal and core fucosylation and sialylation. The enzymes are heat resistant and can be recombinantly expressed in food-grade bacteria, enabling their use in various industrial, pharmaceutical, and analytical applications.

Applications

• Food and beverage industry: inclusion in dairy, infant formula, plant-based foods to enhance protein digestibility and reduce allergenicity. 
• Prebiotic and probiotic products: production and supplementation with free N-glycans to promote beneficial gut microbiota growth.
• Pharmaceuticals: formulation of deglycosylated therapeutic proteins with improved efficacy and reduced immunogenicity; immune system modulation via free glycans. 
• Analytical biochemistry: streamlined glycoprotein characterization and glycomics via enzymatic deglycosylation. 
• Cosmetics and personal care: addition to lotions and topical products for improved protein stability and potentially enhanced bioactivity.
• Biotechnology and industrial enzyme markets: recombinant enzyme production for broad use in glycoprotein modification and processing. 
• Research reagents and kits: supplied with reagents and protocols for efficient and broad-range deglycosylation applications.

Features/Benefits

• Covers all major N-glycan types (high mannose, complex, hybrid) with broad substrate specificity. 
• Maintains activity after heat exposure up to 95°C for 5 minutes. 
• Cleaves glycans with terminal or core fucosylation and sialylation. 
• Uses enzymes from GRAS organisms (Bifidobacteria) to facilitate regulatory approval. 
• Improves digestibility, reduces allergenicity, and stimulates beneficial gut bacteria in food applications. 
• Modulates immune responses and therapeutic protein properties in pharmaceuticals. 
• Streamlines proteomics and glycoproteomics with efficient, single-step deglycosylation. 
• Provides recombinant forms for expression in multiple host cells as either transmembrane or soluble enzymes. 
• Eliminates the need for multiple or sequential enzyme treatments due to limited substrate specificity. 
• Increases efficiency and stability compared to commercial enzymes under high temperature or denaturing conditions. 
• Reduces allergenic potential of glycoproteins in food and pharmaceuticals. 
• Simplifies production of free glycans and deglycosylated proteins for research, nutrition, and therapy. 
• Meets the requirement for regulatory-compliant enzymes suitable for food and medicinal products.

Patent Status