Evaluation of casein as a binding ligand protein for purification of alpha-lactalbumin from beta-lactoglobulin under high hydrostatic pressure
| Autor: | Yves Pouliot, Alain Doyen, Michel Britten, Shyam Suwal, Alice Marciniak, Guillaume Brisson |
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| Rok vydání: | 2019 |
| Předmět: |
Hydrostatic pressure
Centrifugation Lactoglobulins Fractionation Chemical Fractionation Protein aggregation 01 natural sciences Analytical Chemistry 0404 agricultural biotechnology Casein Hydrostatic Pressure Pressure Beta-lactoglobulin Chromatography biology Chemistry 010401 analytical chemistry Caseins 04 agricultural and veterinary sciences General Medicine Ligand (biochemistry) 040401 food science 0104 chemical sciences Lactalbumin biology.protein Alpha-lactalbumin Food Science |
| Zdroj: | Food Chemistry. 275:193-196 |
| ISSN: | 0308-8146 |
| Popis: | Fractionation of β-lactoglubulin (β-lg) and α-lactalbumin (α-la) using conventional separation technologies remains challenging mainly due to similar molecular weight. Herein, casein (CN) was used as ligand protein to specifically aggregate β-lg under high hydrostatic pressure (HHP) in order to separate α-la after acidification to pH 4.6. Specifically, we studied the effect of different concentration of CN on α-la purity and recovery. Model solutions of α-la, β-lg and CN (from 0 to 5 mg/mL) were pressurized (600 MPa–5 min). After acidification and centrifugation of pressure-treated solutions, purity of α-la was increased up to 78% with a recovery of 88% for solution without CN. In contrast with our initial hypothesis, the presence of CN decreased β-lg pressure-induced aggregation and co-precipitation upon acidification and significantly reduced purity (∼71%). Therefore, our results suggest a chaperone-like activity of CN on β-lg pressure-induced aggregation which needs further investigation. |
| Databáze: | OpenAIRE |
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