Improved heat stability by whey protein–surfactant interaction

Published Date
June 2011, Vol.25(4):594–603, doi:10.1016/j.foodhyd.2010.07.012
Food Colloids 2010: On the Road from Interfaces to Consumers

Author 

T. Tran Le ^a,c

P. Sabatino ^a,b

B. Heyman ^d

M. Kasinos ^a

H. Hoang Dinh ^c

K. Dewettinck ^d

J. Martins ^b

P. Van der Meeren ^a,,

aParticle and Interfacial Technology Group, Department of Applied Analytical and Physical Chemistry, Faculty of Bioscience Engineering, Ghent University, Coupure Links 653, B-9000 Gent, Belgium¹

bNMR-Struct Unit, Department of Organic Chemistry, Faculty of Sciences, Ghent University, Krijgslaan 281, B-9000 Gent, Belgium²

cHanoi University of Technology, Institute of Biological and Food Technology, 1-Dai Co Viet, Hanoi, Viet Nam³

dLaboratory of Food Technology and Engineering, Department of Food Safety and Food Quality, Faculty of Bioscience Engineering, Ghent University, Coupure Links 653, B-9000 Gent, Belgium⁴

Received 31 March 2010. Accepted 14 July 2010. Available online 21 July 2010. 

Abstract

One of the main changes that occur during heat treatment of milk is whey protein denaturation, which in its turn may lead to protein aggregation and gelation. In this contribution, the effect of lysophospholipids, the main components of lysolecithins, as well as alternative surfactants, on heat-induced whey protein aggregation has been studied. Hereby, attention was paid to the relation between polar lipid molecular structure (e.g. effect of alkyl chain length, effect of polar head group) and heat-stabilising properties. Residual protein determination in the supernatant obtained after centrifugation of heated whey protein solutions learned that whey protein aggregation was at least partly prevented in the presence of surfactants. As the short alkyl chain lysophospholipids were particularly effective heat stabilisers, hydrophilic surfactants seemed to be most effective, which may be ascribed to their higher critical aggregation concentration. Upon more severe heat treatment, protein aggregation was probed either in-situ by oscillatory rheology, or ex-situ by yield rheometry. As some surfactants significantly reduced the gel strength, or even prevented heat-induced gel formation, these experiments corroborated the heat-stabilising effect of hydrophilic surfactants. Nuclear Magnetic Resonance (NMR) enabled a more direct evaluation of the protein–surfactant interaction. A strong hydrophobic interaction between small molecular weight surfactants and whey proteins became obvious from the chemical shift of the surfactant hydrophobic groups in the NMR spectrum and could be quantified by pulsed field gradient NMR (pfg-NMR) diffusiometry. The results indicated that protein–surfactant interaction did not occur upon thermal denaturation, but already took place at room temperature. However, the effect of this interaction became mainly obvious during thermal treatment.

Overall, this work indicated that bound surfactants largely minimise heat-induced protein intermolecular interactions and hence prevent heat-induced protein aggregation. As the surfactant molecular structure plays a decisive role, it follows that the heat stability of whey protein containing products may be optimised by appropriate selection of ingredients such as (lyso)phospholipids.

Graphical abstract

Keywords

• Whey protein isolate (WPI)
• Heat coagulation
• Lysophospholipids
• Surfactants
• NMR
• Rheology

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