Solubility of proteins from quail (Coturnix coturnix japonica) egg white as affected by agitation time, pH, and salt concentration
| dc.contributor.author | Santos, D. O. | |
| dc.contributor.author | Coimbra, J. S. R. | |
| dc.contributor.author | Teixeira, C. R. | |
| dc.contributor.author | Barreto, S. L. T. | |
| dc.contributor.author | Silva, M. C. H. | |
| dc.contributor.author | Giraldo- Zuniga, A. D. | |
| dc.date.accessioned | 2019-02-01T18:12:01Z | |
| dc.date.available | 2019-02-01T18:12:01Z | |
| dc.date.issued | 2015 | |
| dc.description.abstract | The solubility of proteins from quail egg white subjected to different agitation times, pH, and NaCl at 25 ◦ C was evaluated in this study. The greatest solubility achieved was obtained in the 0.05 mol/L of NaCl, pH 10.0, and under agitation for 1 h. The lowest solubility was found in the NaCl 1.0 mol/L, pH 3.0, and agitated for 2 h. Under the test conditions, aqueous solutions of NaCl 1.0 mol/L, pH 3.0, and agitated for 2 h may provide the greatest extraction index of proteins from quail egg white because these conditions promoted the protein precipitation in a large extension. | en |
| dc.format | pt-BR | |
| dc.identifier.issn | 1532-2386 | |
| dc.identifier.uri | http://dx.doi.org/10.1080/10942912.2012.654557 | |
| dc.identifier.uri | http://www.locus.ufv.br/handle/123456789/23313 | |
| dc.language.iso | eng | pt-BR |
| dc.publisher | International Journal of Food Properties | pt-BR |
| dc.relation.ispartofseries | Volume 18, Issue 2, Pages 250- 258, 2015 | pt-BR |
| dc.rights | Open Access | pt-BR |
| dc.subject | Solubility | pt-BR |
| dc.subject | Egg | pt-BR |
| dc.subject | Protein | pt-BR |
| dc.subject | Functional properties | pt-BR |
| dc.subject | Ph | pt-BR |
| dc.title | Solubility of proteins from quail (Coturnix coturnix japonica) egg white as affected by agitation time, pH, and salt concentration | en |
| dc.type | Artigo | pt-BR |
