Extraction, purification and characterisation of dermatan sulphate from bovine collagen waste liquor

• Published in: Food and bioproducts processing 2016-07, Vol.99, p.244-251
• Main Authors: Osborne, Simone A., Daniel, Robyn A., Chen, Wei, Stockwell, Peter, Tyrrell, Kerri, Desilva, Kirthi, Seymour, Robert B.
• Format: Article
• Language: English
• Subjects: anti-thrombotic; bovine hide; collagen waste liquor; dermatan sulphate; processing waste
• ISSN: 0960-3085; 1744-3571
• DOI: 10.1016/j.fbp.2016.05.008

•The processing of animal hide generates valuable by-products.•Bovine collagen waste liquor is a source of anti-thrombotic dermatan sulphate.•Filtration and chromatography produces dermatan sulphate with >93% purity.•Bovine hide dermatan sulphate inhibits thrombin through heparin cofactor II. The aim of this study was to extract, purify and characterise glycosaminoglycans present in bovine collagen waste liquor. Processing of bovine hides supplies collagen and gelatine to food, cosmetic and pharmaceutical industries generating abundant and unutilised waste streams that contain bioactive polysaccharides known as glycosaminoglycans. Some of these molecules, like heparin and dermatan sulphate, have known anti-thrombotic and anti-coagulant activities and are prescribed therapeutics. The predominant glycosaminoglycan in bovine collagen waste liquor, dermatan sulphate, was extracted and purified to greater than 93% w/w using only serial filtration and anion exchange chromatography. Bioactivity was measured using an in vitro assay revealing anti-thrombotic activity equivalent to commercial dermatan sulphate sourced from porcine mucosa. Fluorophore-assisted carbohydrate electrophoresis revealed a composition rich in the predominant mammalian disaccharide, uronic acid→N-acetyl-D-galactosamine-4-O-sulphate. Depolymerization and fractionation enriched for low molecular weight fragments with significantly improved anti-thrombotic activity. This study identifies an alternative source of anti-thrombotic dermatan sulphate that can be easily extracted without proteolysis or solvent precipitation that can be further processed into low molecular weight fractions with improved anti-thrombotic activity.