Change in molecular structure and dynamics of protein in milk protein concentrate powder upon ageing by solid-state carbon NMR. (February 2015)

• Record Type: Journal Article
• Authors: Haque, Enamul; Bhandari, Bhesh R.; Gidley, Michael J.; Deeth, Hilton C.; Whittaker, Andrew K.
• Is Part Of: Food hydrocolloids. Volume 44(2015:Feb.)
• Page Start: 66
• Page End: 70
• Publication Date: 2015-02
• Subjects: Solid-state carbon NMR -- Milk protein concentrate -- Water activity -- Molecular mobility -- Solubility; Hydrocolloids -- Periodicals; Food additives -- Periodicals; Colloïdes -- Périodiques; Aliments -- Additifs -- Périodiques; Colloids; Food additives; Periodicals; Electronic journals; 664.06
• DOI: 10.1016/j.foodhyd.2014.09.022
• Languages: English
• ISSNs: 0268-005X

Abstract

Abstract: Instability of proteins in dry form causes solubility loss of milk protein concentrate (MPC) powder upon ageing. High resolution solid state NMR techniques were used to investigate the changes in molecular structure and dynamics of proteins in MPC with varying moisture content (5.5–16.5% w/w) and storage period. The results indicate a slight higher rigidity of molecular domains of protein molecules of non-aged MPC compared to that of the long aged (at 25 °C) MPC. It could be suggested from this observation that long-term storage at high relative humidity (RH) may reduce rigidity of the molecular domains due to interaction with water rather than short-term storage at high RH. This may indicate increased molecular mobility of backbone and side chains of protein molecules due to plasticization during ageing which could facilitate protein–protein interaction and protein denaturation. Graphical abstract: Highlights: Change in molecule structure and dynamics of protein in MPC upon storage evaluated. Long-term storage at high water activity may reduce rigidity of molecular domains. No effects on Protein structure or dynamics upon short-term storage at varying a w . No Correlation between solubility loss and change in molecular structure/dynamics found.