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Relationship between Protein Digestibility and the Proteolysis of Legume Proteins during Seed Germination

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MOLECULES
卷 28, 期 7, 页码 -

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MDPI
DOI: 10.3390/molecules28073204

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plant proteins; legumes; protein digestibility; germination; peptidomics; proteomics

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Legume seed protein is less digestible than animal protein, possibly due to defenses against herbivores. Germination increases proteolysis and digestibility by reducing anti-nutrient protease inhibitors, activating proteases, and breaking down storage proteins. Further research is needed to understand the mechanisms behind improved digestibility and guide the development of more digestible food preparations.
Legume seed protein is an important source of nutrition, but generally it is less digestible than animal protein. Poor protein digestibility in legume seeds and seedlings may partly reflect defenses against herbivores. Protein changes during germination typically increase proteolysis and digestibility, by lowering the levels of anti-nutrient protease inhibitors, activating proteases, and breaking down storage proteins (including allergens). Germinating legume sprouts also show striking increases in free amino acids (especially asparagine), but their roles in host defense or other processes are not known. While the net effect of germination is generally to increase the digestibility of legume seed proteins, the extent of improvement in digestibility is species- and strain-dependent. Further research is needed to highlight which changes contribute most to improved digestibility of sprouted seeds. Such knowledge could guide the selection of varieties that are more digestible and also guide the development of food preparations that are more digestible, potentially combining germination with other factors altering digestibility, such as heating and fermentation. Techniques to characterize the shifts in protein make-up, activity and degradation during germination need to draw on traditional analytical approaches, complemented by proteomic and peptidomic analysis of mass spectrometry-identified peptide breakdown products.

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