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1.
J Dairy Sci ; 95(11): 6204-14, 2012 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-22939794

RESUMO

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.


Assuntos
Lactalbumina/química , Nanopartículas/química , 2-Propanol/farmacologia , Acetona/farmacologia , Animais , Bovinos , Etanol/farmacologia , Concentração de Íons de Hidrogênio , Interações Hidrofóbicas e Hidrofílicas/efeitos dos fármacos , Ponto Isoelétrico , Lactalbumina/efeitos dos fármacos , Microscopia Eletrônica de Transmissão
2.
J Dairy Sci ; 93(4): 1420-8, 2010 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-20338419

RESUMO

The effects of high hydrostatic pressure (HHP) processing (at 200 to 600 MPa, 25 to 55 degrees C, and from 5 to 15 min) on some structural properties of alpha-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 alpha-helix content concomitant with an increase in beta-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.


Assuntos
Pressão Hidrostática , Lactalbumina/química , Animais , Bovinos , Eletroforese em Gel de Poliacrilamida , Fluorescência , Concentração de Íons de Hidrogênio , Interações Hidrofóbicas e Hidrofílicas , Pressão Hidrostática/efeitos adversos , Conformação Proteica , Temperatura , Fatores de Tempo
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