| DC Field | Value | Language |
|---|
| dc.contributor.author | RODILES LOPEZ, J.O. | - |
| dc.contributor.author | ARROYO MAYA, IZLIA JAZHEEL | - |
| dc.contributor.author | JARAMILLO FLORES, M. | - |
| dc.contributor.author | GUTIERREZ LOPEZ, GUSTAVO FIDEL | - |
| dc.contributor.author | HERNANDEZ ARANA, ANDRES | - |
| dc.contributor.author | BARBOSA CANOVAS, G.V. | - |
| dc.contributor.author | NIRANJAN, K. | - |
| dc.contributor.author | HERNANDEZ SANCHEZ, HUMBERTO | - |
| dc.coverage.spatial | <dc:creator id="info:eu-repo/dai/mx/cvu/211759">IZLIA JAZHEEL ARROYO MAYA</dc:creator> | - |
| dc.coverage.spatial | <dc:creator id="info:eu-repo/dai/mx/cvu/9485">GUSTAVO FIDEL GUTIERREZ LOPEZ</dc:creator> | - |
| dc.coverage.spatial | <dc:creator id="info:eu-repo/dai/mx/cvu/629">ANDRES HERNANDEZ ARANA</dc:creator> | - |
| dc.coverage.spatial | <dc:creator id="info:eu-repo/dai/mx/cvu/3026">HUMBERTO HERNANDEZ SANCHEZ</dc:creator> | - |
| dc.coverage.spatial | <dc:creator id="info:eu-repo/dai/mx/cvu/16454">MARIA EUGENIA JARAMILLO FLORES</dc:creator> | - |
| dc.coverage.temporal | <dc:subject>info:eu-repo/classification/cti/2</dc:subject> | - |
| dc.date.accessioned | 2020-04-21T01:59:13Z | - |
| dc.date.available | 2020-04-21T01:59:13Z | - |
| dc.date.issued | 2010 | - |
| dc.identifier.citation | Journal of Dairy Science, vol. 93, núm. 4, april, 2010 | en_US |
| dc.identifier.uri | http://ilitia.cua.uam.mx:8080/jspui/handle/123456789/380 | - |
| dc.description.abstract | The effects of high hydrostatic pressure (HHP) processing (at 200 to 600 MPa, 25 to 55°C, and from 5 to 15 min) on some structural properties of α-lactalbumin was studied in a pH range of 3.0 to 9.0. The range of HHP processes produced a variety of molten globules with differences in their surface hydrophobicity and secondary and tertiary structures. At pH values of 3 and 5, there was a decrease in the α-helix content concomitant with an increase in β-strand content as the pressure increased. No changes in molecular size due to HHP-induced aggregation were detected by sodium dodecyl sulfate-PAGE. All samples showed higher thermostability as the severity of the treatment increased, indicating the formation of a less labile structure related to the HHP treatment. | en_US |
| dc.description.sponsorship | Journal of Dairy Science | en_US |
| dc.language.iso | Inglés | en_US |
| dc.publisher | Champaign, Ill. : American Dairy Science Association | en_US |
| dc.relation.haspart | 0022-0302 | - |
| dc.rights | https://doi.org/10.3168/jds.2009-2786 | - |
| dc.subject | Nanopartículas - Análsis | en_US |
| dc.subject | Estructura molecular | en_US |
| dc.subject | Lactalbúmina | en_US |
| dc.title | Effects of high hydrostatic pressure on the structure of bovine a-lactalbumin | en_US |
| dc.type | Artículo | en_US |
| Aparece en las colecciones: | Artículos
|
