Alternative proteins: Structure and functional properties

The speedy growth of population and continued deterioration of the environment put the world under not completely relying on conventional protein sources. The study of alternative proteins has emerged as a transformative avenue in addressing the growing demand for sustainable food sources amidst environmental, economic, and health challenges. Thus, it has remained the focus of many academics and the industry for research into the possibility of using plants, algae, fungi, and insect-based proteins, which may be more viable, inexpensive, and friendly to the environment. The glycinin, beta-conglycinin, legumin, albumins, glutenins, globulins, and oryzenin from plant sources, phycobiliproteins, phycoerythrin and rubisco from algae sources, mycoprotein from fungi sources, and, vitellogenin and troponins from insect sources are some of the alternative proteins that are shown to have nutritional values. Most of these sources also possess high protein content and overall good amino acid composition; they are, therefore, rated as nutritious and healthy protein sources. These alternative novel proteins though superior in nutritional aspects, are at a preliminary stage on various aspects of research about structure and their function, especially insect algae, bacteria, and fungi proteins. The investigation into their molecular architecture and physicochemical interactions will reveal their function in a variety of food systems. Exploring the protein solubility, emulsification, gelation, and foaming properties will influence their application in the formulation of novel food products. Thus, this book chapter will provide a comprehensive overview of the structural and functional properties of various alternative proteins.