foods
Article
WPI Gel Microstructure and Mechanical Behaviour and Their
Influence on the Rate of In Vitro Digestion
Stephen Homer * , Roderick Williams, Allison Williams and Amy Logan
Citation: Homer, S.; Williams, R.;
Williams, A.; Logan, A. WPI Gel
Microstructure and Mechanical
Behaviour and Their Influence on the
Rate of In Vitro Digestion. Foods 2021,
10, 1066. https://doi.org/10.3390/
foods10051066
Academic Editor: Didier Dupont
Received: 29 March 2021
Accepted: 4 May 2021
Published: 12 May 2021
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Attribution (CC BY) license (https://
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4.0/).
CSIRO Agriculture & Food, 671 Sneydes Road, Werribee, VIC 3030, Australia; roderick.williams@csiro.au (R.W.);
allison.williams@csiro.au (A.W.); amy.logan@csiro.au (A.L.)
* Correspondence: stephen.homer@csiro.au
Abstract: The influence of microstructure and mechanical properties on the in vitro digestibility of
15% whey protein isolate (WPI) gels was investigated. Gels were prepared via heat set gelation at
three pH values (pH 3, 5 and 7), which produced gels with distinct microstructures and mechanical
properties. The gels were minced to simulate an oral/chewing phase, which led to the formation
particles of various sizes and textures. The minced gels were passed through either an Infogest
(pre-set pH of 3) or Glass stomach (dynamic pH) protocol. Gels were digested in the gastric phase
for up to 120 min, at which point the extent of digestion was measured by the amount of filterable
nitrogen passing through a sieve. The digesta from both gastric methods were passed through an
in vitro simulated intestinal phase. A strong link was found between the elasticity of the initial gel
and the gel particle size following simulated oral processing, which significantly (p < 0.01) affected
the rate of digestion in the gastric phase. A weaker correlation was also found between the pH
of the gels and the extent of gastric digestion. This work highlights the differences in the rate of
gastric digestion, arising from oral processing, which can be attributed to the material properties of
the substrate.
Keywords: whey protein; gels; microstructure; particle size; digestion; pH
1. Introduction
Commercial whey protein isolate (WPI) is a highly refined product derived from the
bovine serum (whey) proteins of milk. The behaviour of WPI in water is strongly gov-
erned by the principle constituent protein β-lactoglobulin (β-lg), which usually comprises
more than 50% of the total protein, with the remainder consisting of the other serum pro-
teins found in milk, which includes α-lactalbumin, immunoglobulins, proteose peptones,
serum albumin and lactoferrin [1,2]. Whey protein structure and functionality has been
reviewed earlier by Guyomarc’h et al. [3] and Nicolai et al. [4]. This behaviour is heavily
influenced by electrostatics, with the iso-electric point (IEP) of β-lg generally quoted as
pH 5.2 [5]. At pH values close to the IEP, β-lg and WPI solutions form a white suspension
of spherical aggregates without the need for heating, which can be redispersed back into
solution by adjusting the pH away from the IEP [6,7].
Heating native WPI solutions or suspensions at temperatures above the denatura-
tion temperature of β-lg leads to the formation of irreversible protein aggregates [8,9].
The morphology of the aggregates following heating was shown to be related to that of
the suspension/solution prior to heating [6]. When heated at pH values away from the
IEP, fine-stranded protein aggregates are formed [10,11]. At pH values close to the IEP,
spherical aggregates become irreversibly fixed [12,13]. The types of aggregates have been
discussed in detail in the literature [3,14,15].
If heating is performed at concentrations above the critical gelation concentration
(C
g
), the aggregates form a percolating network and gels are formed. The value of C
g
is
linked with pH and ionic strength and the trends in behaviour of WPI as a function of pH
Foods 2021, 10, 1066. https://doi.org/10.3390/foods10051066 https://www.mdpi.com/journal/foods