Plant
protein-based fibrous structures have recently attracted
attention because of their potential as meat replacer formulations.
It is, however, unclear how the process conditions and fortification
with micronutrients may affect the chemical stability of such products.
Therefore, we aimed to investigate the effects of process conditions
and the incorporation of iron (free and encapsulated) on protein oxidation
in a soy protein-based fibrous product. First, the physicochemical
stability of iron-loaded pea protein particles, used as encapsulation
systems, was investigated when exposed to 100 or 140 °C. Second,
protein oxidation was measured in the iron-fortified soy protein-based
fibrous structures made at 100 or 140 °C. Exposure to high temperatures
increased the carbonyl content in pea protein particles. The incorporation
of iron (free or encapsulated) did not affect carbonyl content in
the fibrous product, but the process conditions for making such products
induced the formation of carbonyls to a fairly high extent.
Process
conditions that are applied to make structured soy-protein-based
food commonly include high temperatures. Those conditions can induce
protein oxidation, leading to a decrease in their susceptibility to
proteolysis by digestive enzymes. We aimed to investigate the effects
of thermomechanical processing on oxidation and in vitro gastric digestion
of commercial soy protein ingredients. Samples were sheared at 100
to 140 °C and characterized for acid uptake, carbonyl content,
electrophoresis, and surface hydrophobicity. The enzymatic hydrolysis
was determined in simulated gastric conditions. Protein ingredients
were already oxidized and showed higher surface hydrophobicity and
hydrolysis rate compared with those of the processed matrices. However,
no clear correlation between the level of carbonyls and the hydrolysis
rate was found. Therefore, we conclude that gastric digestion is mostly
driven by the matrix structure and composition and the available contact
area between the substrate and proteolytic enzymes.
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