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Synthesis and characterization of glycosaminoglycans, oligo- andpolysaccharides using a recombinant 4-O-sulfatase


Key words Polysaccharide, oligosaccharide, glycosaminoglycan, sulfate, sulfatase, desulfation, glycosylation site
Latest version 2013/09/05
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)

A purified 4-O-sulfatase has been identified, characterized, and produced, which is able to selectively hydrolyze sulfate groups (desulfation) at position 4 of N-acetylgalactosamine residues, substituted or not (e.g. chondroitin-4-sulfate). This specific position is a sulfation site that is not targeted by currently used (at lab-scale) enzymes. (2)

- 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

selective desulfation

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

Further Information

Institutes INRA - MICALIS
Companies INRA Transfert
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.

reaction medium (aqueous), temperature (moderate), reactant and product concentrations

Fermentors 2.1.3 biological other biotechnology Inra Transfert database of technological offers; contact WikiSysop :Template:Review document :Template:Review status

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Created by Hte inra on 7 December 2012, at 19:57