4.6 Review Book Chapter

Soy Protein: Molecular Structure Revisited and Recent Advances in Processing Technologies

Journal

Publisher

ANNUAL REVIEWS
DOI: 10.1146/annurev-food-062220-104405

Keywords

soybean; soy protein; molecular structure; recent processing technologies

Funding

  1. Excellent Young Scientists Fund of the National Natural Science Foundation of China [32022068]
  2. Fok Ying-Tung Education Foundation [171027]

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Rising health concerns and increasing obesity levels have led to a shift in consumer preferences towards plant-based proteins, with soy protein emerging as a versatile and well-balanced alternative to animal protein. Advances in processing technologies have enabled the production of a wide variety of functional foods and ingredients from soy proteins, offering consumers a diverse array of options in the modern food industry. The review also explores the structural changes induced by soy protein processing and revisits the molecular structure of soy protein, particularly the crystal structures of beta-conglycinin and glycinin.
Rising health concerns and increasing obesity levels in human society have led some consumers to cut back on animal protein consumption and switch to plant-based proteins as an alternative. Soy protein is a versatile protein supplement and contains well-balanced amino acids, making it comparable to animal protein. With sufficient processing and modification, the quality of soy protein can be improved above that of animal-derived proteins, if desired. The modern food industry is undergoing a dynamic change, with advanced processing technologies that can produce a multitude of foods and ingredients with functional properties from soy proteins, providing consumers with a wide variety of foods. This review highlights recent progress in soy protein processing technologies. Using the current literature, the processing-induced structural changes in soy protein are also explored. Furthermore, the molecular structure of soy protein, particularly the crystal structures of beta-conglycinin and glycinin, is comprehensively revisited.

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