Reversible phosphorylation is a major post-translational mechanism by which cells transduce cellular signals. The functional significance of the seed storage proteins phosphorylation is presently unknown. It has been suggested that phosphorylation have implications with respect to allergenicity and digestibility; metal binding capacity and enhancing bioavailability is the commonly accepted functional properties for many phosphoproteins, that may have value in the prevention of osteoporosis, dental caries, hypertension and anemia. Moreover, the presence of phosphorylated food proteins improved a number of technological properties, including solubility, heat stability, water absorption, emulsifying, foaming and gelling properties. White lupin is a leguminous grain crop that represents an important source of proteins for human and animal nutrition, since its seed is one of the richest in protein content. The present study was undertaken with the goal of identifying proteins that are phosphorylated in mature seeds of L. albus and during seed filling and germination. The results indicated a dynamic phosphorylation pattern: during these three stages an increase of the protein phosphorylation was observed. During the seed development, only polypeptides belonging to vicilin family appear to be phosphorylated. In mature seed, polypeptides either of vicilins and legumins are phosphorylated. After two days from the onset of germination, legumins increase their phosphorylation level, whereas vicilin are not further modified. δ-Conglutin, a 2S protein, is phosphorylated at germination but not during the seed development. These results make a contribution to better understand the structure of globulin-like seed storage proteins and represent the background to their potential applications in lupin-based products.

Proteomic studies on the lupin seed storage proteins phosphorylation / J. Capraro, A. Scarafoni, A. Ronchi, C. Magni, A. Consonni, M. Duranti. ((Intervento presentato al 2. convegno International Conference on Food-omics tenutosi a Cesena nel 2011.

Proteomic studies on the lupin seed storage proteins phosphorylation

J. Capraro
Primo
;
A. Scarafoni
Secondo
;
C. Magni;A. Consonni
Penultimo
;
M. Duranti
Ultimo
2011

Abstract

Reversible phosphorylation is a major post-translational mechanism by which cells transduce cellular signals. The functional significance of the seed storage proteins phosphorylation is presently unknown. It has been suggested that phosphorylation have implications with respect to allergenicity and digestibility; metal binding capacity and enhancing bioavailability is the commonly accepted functional properties for many phosphoproteins, that may have value in the prevention of osteoporosis, dental caries, hypertension and anemia. Moreover, the presence of phosphorylated food proteins improved a number of technological properties, including solubility, heat stability, water absorption, emulsifying, foaming and gelling properties. White lupin is a leguminous grain crop that represents an important source of proteins for human and animal nutrition, since its seed is one of the richest in protein content. The present study was undertaken with the goal of identifying proteins that are phosphorylated in mature seeds of L. albus and during seed filling and germination. The results indicated a dynamic phosphorylation pattern: during these three stages an increase of the protein phosphorylation was observed. During the seed development, only polypeptides belonging to vicilin family appear to be phosphorylated. In mature seed, polypeptides either of vicilins and legumins are phosphorylated. After two days from the onset of germination, legumins increase their phosphorylation level, whereas vicilin are not further modified. δ-Conglutin, a 2S protein, is phosphorylated at germination but not during the seed development. These results make a contribution to better understand the structure of globulin-like seed storage proteins and represent the background to their potential applications in lupin-based products.
2011
Settore BIO/10 - Biochimica
Proteomic studies on the lupin seed storage proteins phosphorylation / J. Capraro, A. Scarafoni, A. Ronchi, C. Magni, A. Consonni, M. Duranti. ((Intervento presentato al 2. convegno International Conference on Food-omics tenutosi a Cesena nel 2011.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/159613
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