Formation of protein nanoparticles by controlled heat treatment of lactoferrin: Factors affecting particle characteristics

Bengoechea, Carlos, Peinado Pardo, Irene and McClements, David (2011) Formation of protein nanoparticles by controlled heat treatment of lactoferrin: Factors affecting particle characteristics. Food Hydrocolloids, 25 (5). pp. 1354-1360. ISSN 0268-005X

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Official URL: http://dx.doi.org/10.1016/j.foodhyd.2010.12.014

Abstract

Lactoferrin is a globular protein from milk that has considerable potential as a functional ingredient in
food, cosmetic and pharmaceutical applications. In this study, we examined the possibility of preparing food-grade bovine lactoferrin (bLf) nanoparticles using a simple thermal processing method. Differential Scanning Calorimetry (DSC), light scattering, and z-potential techniques were used to provide information about the conformational changes, aggregation, and electrical charge of bLf in aqueous solutions. DSC studies indicated that the protein had two thermal denaturation temperatures (61 and 93 �C), which were associated with two different lobes of the protein. Protein denaturation was found to be irreversible, which was attributed to the formation of protein nanoparticles, whose size depended on the
temperature and duration of the thermal treatment. Higher holding temperatures produced faster protein aggregation and larger protein nanoparticles: 85 > 80 > 75 > 70 �C. The protein nanoparticles produced by thermal treatment were resistant to subsequent changes in pH (from 3 to 11) and to salt addition (0e200 mM NaCl). The lactoferrin nanoparticles produced in this study may be useful as
function ingredients in commercial products.

Item Type: Article
Uncontrolled Keywords: lactoferrin, nanoparticles, DSC, ζ-potential, aggregation, denaturation
Subjects: B400 Nutrition
D600 Food and Beverage studies
Department: Faculties > Health and Life Sciences > School of Life Sciences > Applied Sciences
Depositing User: Irene Peinado-Pardo
Date Deposited: 21 Dec 2012 10:31
Last Modified: 10 Aug 2015 11:38
URI: http://nrl.northumbria.ac.uk/id/eprint/10865

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