Isolation of bovine β-lactoglobulin from complexes with chitosan
A simple, economical and non-toxic method is described for the solubilization of undenatured β-lactoglobulin (β-lg) from complexes with chitosan. The effect of pH (8-10), ionic strength (0.08-0.3 m) and volume ratio between sodium acetate solutions and whey on the dissociation of β-lg-chitosan compl...
| Authors: | , , , , , |
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| Format: | article |
| Status: | Versión enviada para evaluación y publicación |
| Publication Date: | 2007 |
| Country: | España |
| Institution: | Consejo Superior de Investigaciones Científicas (CSIC) |
| Repository: | DIGITAL.CSIC. Repositorio Institucional del CSIC |
| OAI Identifier: | oai:digital.csic.es:10261/155043 |
| Online Access: | http://hdl.handle.net/10261/155043 |
| Access Level: | Open access |
| Keyword: | Electrostatic interactions Cheese whey β-lactoglobulin Chitosan |
| Summary: | A simple, economical and non-toxic method is described for the solubilization of undenatured β-lactoglobulin (β-lg) from complexes with chitosan. The effect of pH (8-10), ionic strength (0.08-0.3 m) and volume ratio between sodium acetate solutions and whey on the dissociation of β-lg-chitosan complexes was evaluated. Following a single extraction step with the addition of 10 mL of 0.1 m sodium acetate solution at pH 9 to the β-lg-chitosan complexes obtained from 1 mL of cheese-whey, a recovery of 90% of β-lg with a protein purity of 95% was achieved, suggesting that electrostatic interactions play a key role in the complexation of β-lg with chitosan. The presence of free chitosan in solution was ruled out according to gas chromatography with flame-ionization detector analysis after acid hydrolysis. NMR spectroscopy showed that the recovered β-lg after further dialysis had structural features very similar to the native protein. |
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