Improved heat stability by whey protein–surfactant interaction

• Published in: Food hydrocolloids Vol. 25; no. 4; pp. 594 - 603
• Main Authors: Tran Le, T., Sabatino, P., Heyman, B., Kasinos, M., Dinh, H. Hoang, Dewettinck, K., Martins, J., Van der Meeren, P.
• Format: Journal Article
• Language: English
• Published: Elsevier Ltd 01-06-2011; [New York, NY]: Elsevier Science
• Subjects: Agglomeration; Chains; Heat coagulation; Heat treatment; Lysophospholipids; Molecular structure; NMR; Nuclear magnetic resonance; Proteins; Rheology; Surfactants; Whey; Whey protein isolate (WPI); Whey protein isolate (WPI); Lysophospholipids; NMR; Heat coagulation; Surfactants; Rheology
• ISSN: 0268-005X; 1873-7137
• DOI: 10.1016/j.foodhyd.2010.07.012

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.
[Display omitted]