Purification, structural characterization and bioactivity evaluation of a novel proteoglycan produced by Corbicula fluminea

• Published in: Carbohydrate polymers 2017-11, Vol.176, p.11-18
• Main Authors: Yan, Jing-Kun, Wang, Yao-Yao, Qiu, Wen-Yi, Wu, Li-Xia, Ding, Zhi-Chao, Cai, Wu-Dan
• Format: Article
• Language: English
• Subjects: Animals; Antioxidant activity; Corbicula - chemistry; Corbicula fluminea; Fresh Water; Molecular Weight; Proteoglycan; Proteoglycans - chemistry; Purification; Structural characterization
• ISSN: 0144-8617; 1879-1344
• DOI: 10.1016/j.carbpol.2017.08.063

•A novel proteoglycan, named CFPS-11, was isolated from Corbicula fluminea.•The structural feature of CFPS-11 was elucidated by physical and chemical analyses.•CFPS-11 exhibited significant antioxidant activity in a dose-dependent manner.•CFPS-11 showed remarkable inhibitory activities against α-amylase and α-glucosidase.•CFPS-11 could be explored as a potent food additive or nutritional supplement. A novel proteoglycan, named CFPS-11, was isolated from Corbicula fluminea, which is a food source of freshwater bivalve mollusk. CFPS-11 had an average molecular weight of 807.7kDa and consisted of d-glucose and d-glucosamine in a molar ratio of 12.2:1.0. The protein moiety (∼5%) of CFPS-11 was covalently bonded to the polysaccharide chain in O-linkage type through both serine and thereonine residues. The polysaccharide chain of CFPS-11 was composed of (1→4)-α-d-glucopyranosyl and (1→3,6)-α-d-glucopyranosyl residues, which branched at O-6. The branch chain consisted of (1→)-α-d-glucopyranosyl and (1→)-α-d-N-acetylglucosamine residues. CFPS-11 exhibited significant antioxidant activity in a dose-dependent manner and remarkable inhibition activities against α-amylase and α-glucosidase by in vitro assays. These findings indicated that the CFPS-11 from C. fluminea has the potential for development as a health food ingredient.