Synthesis and characterization of glycosaminoglycans, oligo- andpolysaccharides using a recombinant 4-O-sulfatase
- How does it work?
- What can it be used for?
- What can it not be used for?
- Related Facilities
- Further Information
|Key words||Polysaccharide, oligosaccharide, glycosaminoglycan, sulfate, sulfatase, desulfation, glycosylation site|
|Completed by||INRA - IATE|
How does it work?
|Primary objective||Simple method for synthesis and characterization of glycosaminoglycans, oligo- and polysaccharides|
|Working principle|| Sulfate groups are essential to the physical, chemical and biological properties of various molecules such as polysaccharides, and amongst them the glycosaminoglycans (GAGs). The GAGs encompass 5 sub-families of molecules, namely: chondroïtins, hyaluronic acid, dermatan, keratan and heparan sulfates / heparins.
Not only the number of the sulfate groups, but also their specific positions within the molecule, are critical for the functionality of these molecules. For example, chondroitins are mainly located in the human articulations and play a mechanical role, whereas heparins are located in the arteries, where they act as anti-coagulant agents.
Today, GAGs are widely used in pharmacy and cosmetics, and the food applications are developing. However, there are no simple methods of synthesis and physico-chemical characterization of sulfated sugars, which greatly limits their industrial development (currently only a few heparins and chondroitins, and hyaluronic acid are commercially available). (1)
- This recombinant enzyme can be used in synthesis methods of oligo- and polysaccharides, including GAGs. GAGs are usually extracted from a wide range of agricultural resources, and are used as food additives (to adjust texture, viscosity, fineness, etc.)
- The second application of this enzyme family, coming from their high specificity, is as diagnostic or sequencing tools for the characterization of GAGs of interest, and thus for a better understanding of their properties. Indeed, determining the type of sulfation of an oligo- or polysaccharide may be performed by testing desulfation with this 4-O-sulfatase in combination with methods of detection/quantification of desulfated monosaccharides or sulfates released after hydrolysis.
|Additional effects||The synthesised saccharides can also be used in pharmaceutical and cosmetic industries|
|Important process parameters||reaction medium (aqueous), temperature (moderate), reactant and product concentrations|
|Important product parameters|
What can it be used for?
|Products||glycosaminoglycans, oligo- and polysaccharides|
|Operations||enzymatic processing of sugars|
|Solutions for short comings|| sulfatases with new features / properties
Characterization of sugars
Currently, some molecules are commercially available for pharmacy and cosmetic applications, but they are not suitable for food purposes because of religious and philosophical matters, as they are extracted from animal tissues (pork and/or beef: restrictions for Jews, Muslims, Hindus, vegetarians and vegans).
What can it NOT be used for?
|Products||Any other than polysaccharides|
|Operations||any other than enzymatic modification of sugars / synthesis of GAGs|
|Other limitations||Reaction speed|
|Risks or hazards||no|
|Maturity||The technology is currently available at lab-scale. Licences are available from the patent through INRA Transfert, which will lead to upscaling|
|Modularity /Implementation||This technology comes in addition to the existing production lines|
|Consumer aspects||not known|
|Legal aspects|| The technology is patented with a worldwide application territory, and licenses are commercially available through INRA Transfert.
Currently GAGs do not have E-numbers for their use as food additives. They will need approval from the European Food Safety Authority.
|Environmental aspects||enzymes work at low temperature and pressure compared to conventional chemical synthesis reactions|
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|Institutes||INRA - MICALIS|
|References|| 1. Berteau, O., A. Benjdia, D. Bonnaffe, C. Le Narvor, A. Malleron, 2011. Sulfatase selectively modifying glycosaminoglycans. WO2011086293 (A1) (FR 2954349).
2. Uniprot database: putative uncharacterized protein XP002583121; putative uncharacterized protein XP002583122; arylsulfatase A or predicted protein XP002583123.