Effects of grinding and thermal treatments on hydrolysis susceptibility of pea proteins (Pisum sativum L.).
The effects of three particle sizes with two types of grindings and two thermal treatments on pea protein extraction (PE) and susceptibility to in vitro enzymatic hydrolysis (pepsin plus trypsin) were studied. Degrees of hydrolysis (DH) were calculated. Remaining peptides were detected by SDS-PAGE and identified by immunoblotting and MS/MS spectrometry. The increase in particle size decreased PE and DH due to a restricted access of solvents and enzymes to proteins. The thermal treatment induced a decrease in PE but did not modify DH. Heating improved legumin (alphaM) and convicilin pepsin hydrolyses but reduced the pea albumin 2 (PA2) hydrolysis. After pepsin and trypsin hydrolysis, only peptides from vicilin and lectin were identified by LC-MS/MS analyses, whatever the treatment.
Le Gall
Maud
M
Unité de Recherche sur les Protéines Végétales et leurs Interactions, Institut National de la Recherche Agronomique, rue de la Géraudière, 44372 Nantes Cedex, France.
Guéguen
Jacques
J
Séve
Bernard
B
Quillien
Laurence
L
D004591:Electrophoresis, Polyacrylamide Gel; D005511:Food Handling / Q000379:methods*; D006358:Hot Temperature; D006868:Hydrolysis; D015151:Immunoblotting; D013058:Mass Spectrometry; D010316:Particle Size; D018532:Pisum sativum / Q000737:chemistry*; D010434:Pepsin A / Q000378:metabolism; D010940:Plant Proteins / Q000378:metabolism*; D014357:Trypsin / Q000378:metabolism
D010940:Plant Proteins; D014357:Trypsin; D010434:Pepsin A