4.7 Article

Investigating casein gel structure during gastric digestion using ultra-small and small-angle neutron scattering

Journal

JOURNAL OF COLLOID AND INTERFACE SCIENCE
Volume 594, Issue -, Pages 561-574

Publisher

ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jcis.2021.03.087

Keywords

Protein dairy protein gel; Casein; Structure; Digestion; Neutron scattering; Electron microscopy; Solubilised protein

Funding

  1. Australian Nuclear Science and Technology Organization (ANSTO) [7399]
  2. AINSE Limited
  3. RMIT Vice Chancellor's Senior Research Fellowship

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This study investigated the structural devolution of RG and TG gels during simulated gastric digestion, finding that gel firmness and disintegration behavior are closely related. Gel firmness and brittleness were greater in D2O samples compared to H2O.
This study aimed to understand the structural devolution of 10% w/w rennet-induced (RG) and transglutaminase-induced acid (TG) gels in H2O and D2O under in vitro gastric conditions with and without pepsin. The real-time devolution of structure at a nano- (e.g. colloidal calcium phosphate (CCP) and micelle) and micro- (gel network) level was determined using ultra-small (USANS) and small-angle neutron scattering (SANS) with electron microscopy. Results demonstrate that gel firmness or elasticity determines disintegration behaviour during simulated mastication and consequently the particle size entering the stomach. Shear of mixing in the stomach, pH, and enzyme activity will also affect the digestion process. Our results suggest that shear of mixing primarily results in erosion at the particle surface and governs gel disintegration behaviour during the early stages of digestion. Pepsin diffusivity, and hence action, occur more readily in the latter stages of gastric digestion via access to the particle interior. This occurs via the progressively larger pores of the looser gel network and channels created within the larger, less dense casein micelles of the RG gels. Gel firmness and brittleness were greater in the D2O samples compared to H2O, facilitating gel disintegration. Despite the higher strength and elasticity of RG compared to TG, the protein network strands of the RG gels become more compact when exposed to the acidic gastric environment with comparatively larger pores observed through SEM imaging. This led to a higher degree of digestibility in RG gels compared to TG gels. This is the first study to examine casein gel structure during simulated gastric digestion using scattering and highlights the benefits of neutron scattering to monitor structural changes during digestion at multiple length scales. (c) 2021 The Authors. Published by Elsevier Inc. This is an open access article under the CC BY license (http:// creativecommons.org/licenses/by/4.0/).

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