Molecular Functionality of Plant Proteins from Low- to High-Solid Systems with Ligand and Co-Solute

Abstract

In the food industry, proteins are regarded as multifunctional systems whose bioactive hetero-polymeric properties are affected by physicochemical interactions with the surrounding components in formulations. Due to their nutritional value, plant proteins are increasingly considered by the new product developer to provide three-dimensional assemblies of required structure, texture, solubility and interfacial/bulk stability with physical, chemical or enzymatic treatment. This molecular flexibility allows them to form systems for the preservation of fresh food, retention of good nutrition and interaction with a range of microconstituents. While, animal- and milk-based proteins have been widely discussed in the literature, the role of plant proteins in the development of functional foods with enhanced nutritional profile and targeted physiological effects can be further explored. This review aims to look into the molecular functionality of plant proteins in relation to the transport of bioactive ingredients and interaction with other ligands and proteins. In doing so, it will consider preparations from low- to high-solids and the effect of structural transformation via gelation, phase separation and vitrification on protein functionality as a delivery vehicle or heterologous complex. Applications for the design of novel functional foods and nutraceuticals will also be discussed.

Improvement of structural, physicochemical, and rheological properties of porcine myofibrillar proteins by high-intensity ultrasound treatment for application as Pickering stabilizers

“…On the other hand, HIU-treated samples showed LVE at a strain of<10 %, confirming that HIU treatment expanded the LVE of the MP solution. Earlier it was found that the G' and G'' values of the sonicated soybean isolate protein dispersion were lower than that of the unsonicated control, and the LVE was more expanded [48] . Also, in all samples, G' was dominant over G'' in LVE.…”

Lupin Protein Isolate Structure Diversity in Frozen-Cast Foams: Effects of Transglutaminases and Edible Fats

“…Globular proteins, such as the ones found in lupin, create structures which characteristics are driven by the interaction of the protein with water molecules and governed by other additives [ 35 ]. The impact of TG and food grade additives on the functionality of LPI varied largely in the present study as shown in the 3-D images of reconstructured foam from X-ray tomography ( Figure 4 ; videos S1–S4; supplementary material ) and SEM ( Figure 5 ).…”

Pulse protein ingredient modification

“…Proteins solubility is typically reduced upon heating due to aggregation 61 . Protein deformation properties depend primarily on the number of disulfide bridges and ß‐sheet content 62 . For example, the high content of disulfide bridges in native 11S fraction of lupin protein isolates prevented molecular reconfigurations upon heat treatment 63 .…”

“…61 Protein deformation properties depend primarily on the number of disulfide bridges and ß-sheet content. 62 For example, the high content of disulfide bridges in native 11S fraction of lupin protein isolates prevented molecular reconfigurations upon heat treatment. 63 The proteins with a greater proportion of ⊎-sheets were thermally more stable, need a higher temperature for gel formation, and produce stronger gels due to greater intermolecular interactions between them.…”