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Título: Effect to different treatments on the ability of a-lactalbumin to form nanoparticles
Autor(es): ARROYO MAYA, IZLIA JAZHEEL
RODILES LOPEZ, J.O.
CORNEJO MAZON, MARIBEL
GUTIERREZ LOPEZ, GUSTAVO FIDEL
HERNANDEZ ARANA, ANDRES
TOLEDO NUÑEZ, C.
BARBOSA CANOVAS, G. V.
FLORES FLORES, J. O
HERNANDEZ SANCHEZ, HUMBERTO
Temas: Nanopartículas - Análisis
Asociación molecular
Lactalbúmina
Fecha: 2012
Editorial: Champaign, Ill. : American Dairy Science Association
Citation: Journal of Dairy Science, vol. 95, núm. 11, november, 2012
Resumen: Nanoparticles of bovine α-lactalbumin (α-LA) prepared by desolvation and glutaraldehyde crosslinking are promising carriers for bioactive compounds in foods. The objective of this work was to study the effect of changes in hydrophobic interactions by using different desolvating agents (acetone, ethanol, or isopropanol) and the use of a heat or high-pressure treatment step before the desolvation process on the size, structure, and properties of α-LA nanoparticles. In all cases, a high average particle yield of 99.63% was obtained. Smaller sizes (152.3 nm) can be obtained with the use of acetone as the desolvating agent and without any pretreatment. This is the first time that α-LA nanoparticles in the size range of 100 to 200 nm have been obtained. These nanoparticles, with an isoelectric point of 3.61, are very stable at pH values >4.8, based on their ζ-potential, although their antioxidant activity is weak. The use of the desolvating agent with the smallest polarity index (isopropanol) produced the largest particles (293.4 to 324.9 nm) in all cases. These results support the idea that controlling hydrophobic interactions is a means to control the size of α-LA nanoparticles. No effect of pretreatment on nanoparticle size could be detected. All types of nanoparticles were easily degraded by the proteolytic enzymes assayed.
URI: http://ilitia.cua.uam.mx:8080/jspui/handle/123456789/379
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