Interactions between furcellaran and the globular proteins bovine serum albumin and β-lactoglobulin

• Published in: Carbohydrate polymers Vol. 67; no. 2; pp. 116 - 123
• Main Authors: Laos, K, Brownsey, G.J, Ring, S.G
• Format: Journal Article
• Language: English
• Published: 2007
• Subjects: algae and seaweeds; biopolymers; bovine serum albumin; chemical interactions; complexation; Furcellaria; Furcellaria lumbricalis; furcellerans; galactans; lactoglobulins; mixtures; polysaccharides; proteins
• ISSN: 0144-8617

The interaction between the algal polysaccharide furcellaran and the globular proteins, bovine serum albumin and β-lactoglobulin was examined as a function of pH using potentiometric and turbidimetric titration and photon correlation spectroscopy. On decreasing pH, the furcellaran first formed a soluble complex with the globular proteins at a pH(c), which showed a maximum in its dependence on ionic strength. On further decrease in pH, the onset of a more substantial aggregation, as indicated by a marked increase in turbidity occurred in the vicinity of the isoelectric point of the protein. Between these pH's the protein/furcellaran complex had a characteristic average size which was larger than the isolated furcellaran chain in solution. Complexation occurred when the protein carried an average net charge of the same sign as the furcellaran.