Plant proteins and their colloidal state |
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| Affiliation: | 1. Chalmers University of Technology, Industrial and Materials Science, SE 412 96, Gothenburg, Sweden;2. Research Institutes of Sweden, RISE, Bioscience and Materials, SE 402 29, Gothenburg, Sweden;1. Department of Food Science, The Pennsylvania State University, University Park, PA, 16802, USA;2. Department of Animal and Food Science, University of Wisconsin – River Falls, River Falls, WI, 54022, USA;3. Stack Family Center for Biopharmaceutical Education and Training, Albany College of Pharmacy and Health Sciences, Albany, NY, 12203, USA |
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| Abstract: | Plant proteins are characterized by a complex colloidal state in their physiological environment. The main reasons are related to the multiple functions of plant proteins as well as the different architectures encountered in the plant cells from various sources. During extraction process to produce ingredients, plant proteins reorganize in several native or denatured colloidal states depending on the energy and the physico–chemical changes applied to the system. In most cases, an equilibrium between the native (soluble monomers or oligomers) and denatured (mostly insoluble) oligomeric/aggregated states is reached. Further, processing of the plant protein ingredients during food production, introducing new hydrophobic phases (e.g., gas, oil), energy (pressure, temperature, shear), and physico–chemical conditions (pH, ionic salts) will lead to a final colloidal state, specific to the structural features of the considered final food product. |
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| Keywords: | Aggregation Denaturation Entropy Extraction Extrusion Gel Emulsion Foam |
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