Amino acid composition of pea (Pisum sativum) proteins and protein profile of pea flour

Abstract

The influence of coarse milling on the distribution of the protein jiactions in the particles was studied. The profile in proteins was the same for the diferent classes as that for the whole seed. The second part of the work was devoted to the determination of the amino acid composition of the different nitrogenous jiactions.Pea seeds (Pisum sativum L) are mostly used in pig feed because of their low content of antinutritional factors and their high nutritive value. Pea proteins are, however, deficient in Scontaining amino acids (methionine and cystine) and in tryptophan (Mosse et all987). Although pea albumins are richer in essential amino acids (AA) than globulins, no data are available about the AA profile of the insoluble proteins and the non-protein material of pea seed. As the protein fractions do not have the same nutritive value, milling can accentuate this difference in some feeds, such as cereals, because the distribution of the proteins in the seed is heterogeneous and the different particles do not have the same hardness (Taverner et a1 1981). Furthermore, Horvath et a1 (1989) have shown recently that the protein content and some functional properties of pin-milled and airclassified pea flours depend on the particle size distribution. The milling of peas intended for animal feed is coarser, and it is not known if coarse milling modifies the distribution of the protein fractions in the particles. This paper addresses this problem.A sample of peas (cv Solara) was hammermilled through a 3-mm screen with a hammer mill commonly used for pig nutrition. The sieve analysis was performed with a vibratory sieve shaker (Analysette 3, Fritsch, Idar-Obersbein, FRG). The different size fractions were passed through the 0.5-mm screen of a Pulverisette 14 (Fritsch). The procedures of extraction and quantitation of the protein fractions have been described by Gueguen and Barbot (1988). N was analysed according to the Kjeldahl method. The AA compositions were determined using ion-exchange chromatography. Performic acid treatment was used to oxidise methionine and cystine before hydrolysis. Tryptophan was determined by gel filtration

Impact of Legume Flour Addition on Pasta Structure: Consequences on Its In Vitro Starch Digestibility

“…At a lower scale, the protein network in cooked pasta was weaker in legume pasta compared with durum wheat pasta: cooked legume pasta and especially faba bean pasta presented a higher proportion of proteins linked by non-covalent interactions and a lower proportion of proteins linked by disulphide and other covalent bonds. Legume proteins, mainly composed of globulins and albumins [25][26][27][28][29] , are poor in sulphur-containing amino acids, especially cystein residues. 2,3 The lack of sulphur groups could explain the lower potential of legume proteins to bind through disulphide bonds compared with gluten proteins.…”

“…Globulins and albumins represented 45-60% and 14-30% of split pea proteins; 55-75% and 2-33% of faba bean proteins respectively. [25][26][27][28][29] Durum wheat semolina proteins were characterised by a low solubility in water (11.1%; Table 1). In comparison, legume flour proteins were highly soluble, especially faba bean flour (78.8%) which is in accordance with previous study.…”

Pulse proteins: Processing, characterization, functional properties and applications in food and feed

“…O'Kane et al (2004) found legumin: vicilin ratios varying from 0.2 to 1.5. Compared to the globulins, pea albumins contain more of the essential amino acids tryptophan, lysine, threonine, cysteine and methio- (Leterme, Monmart, & Baudart, 1990). B Unit: g/100 g protein (Khattab, Arntfield, & Nyachoti, 2009).…”

Size measuring techniques as tool to monitor pea proteins intramolecular crosslinking by transglutaminase treatment

“…Thus, our strategy to follow the intramolecular crosslinks is based on size measuring methods by using SDS-PAGE and DLS techniques. To validate our hypothesis, we first selected the pea albumin protein fraction as substrate to MTGase because pea albumin (i) is easy to extract and to purify, (ii) is rich in glutamine and lysine (Bhatty, 1982;Leterme, Monmart, & Baudart, 1990), and (iii) is a small protein composed of an abundant polypeptide (PA2 = 26 kDa) which can be easily followed by SDS-PAGE. Next, TPA was treated at decreasing protein concentration (down to 0.01% w/w) with MTGase in order to promote intramolecular crosslinks.…”