Interactions between furcellaran and the globular proteins bovine serum albumin and β-lactoglobulin
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 sol...
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Published in | Carbohydrate polymers Vol. 67; no. 2; pp. 116 - 123 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
2007
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Subjects | |
Online Access | Get full text |
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Summary: | 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. |
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Bibliography: | http://dx.doi.org/10.1016/j.carbpol.2006.04.021 |
ISSN: | 0144-8617 1879-1344 |