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Characterization of Pea (Pisum Sativum) Seed Protein Fractions

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Characterization of Pea (Pisum Sativum) Seed Protein Fractions Research Article Received: 8 March 2013 Revised: 24 May 2013 Accepted article published: 6 June 2013 Published online in Wiley Online Library: (wileyonlinelibrary.com) DOI 10.1002/jsfa.6250 Characterization of pea (Pisum sativum) seed protein fractions Luis A Rubio,∗ Alicia Perez,´ Raquel Ruiz, M Angeles´ Guzman,´ Isabel Aranda-Olmedo and Alfonso Clemente Abstract BACKGROUND: Legume seed proteins have to be chemically characterized in order to properly link their nutritional effects with their chemical structure. RESULTS: Vicilin and albumin fractions devoid of cross-contamination, as assessed by mass peptide fingerprinting analysis, were obtained from defatted pea (Pisum sativum cv. Bilbo) meal. The extracted protein fractions contained 56.7–67.7 g non-starch polysaccharides kg−1. The vicilin fraction was higher than legumins in arginine, isoleucine, leucine, phenylalanine and lysine. The most abundant amino acids in the albumin fraction were aspartic acid, glutamic acid, lysine and arginine, and the amounts of methionine were more than double than those in legumins and vicilins. The pea albumin fraction showed a clear enrichment of protease inhibitory activity when compared with the seed meal. In vitro digestibility values for pea proteins were 0.63 ± 0.04, 0.88 ± 0.04 and 0.41 ± 0.23 for legumins, vicilins and albumins respectively. CONCLUSION: Vicilin and albumin fractions devoid of cross-contamination with other proteins were obtained from pea seed meal. The vicilin fraction also contained low amounts of soluble non-starch polysaccharides and was enriched in isoleucine, leucine, phenylalanine and lysine. In vitro digestibility values for pea proteins were similar or even numerically higher than those for control proteins. c 2013 Society of Chemical Industry Keywords: albumins; legumins; Pisum sativum; protease inhibitors; protein digestibility; vicilins INTRODUCTION as approximately 25 million hectares are grown annually 6 It is at present acknowledged that food proteins are not only worldwide. a source of constructive and energetic compounds such as It is generally recognized that grain legumes contribute amino acids (AA) but may also play a bioactive role and/or effectively to a balanced diet and can prevent non-communicable 7 can be precursors of biologically active peptides with various diseases, including type II diabetes and cardiovascular diseases. physiological functions. The best-known examples of this are However, which chemical components are responsible for the probably casein-derived peptides, which have been proved to observed protective effects, their mechanism(s) of action and possess immunomodulating, antihypertensive, antithrombotic even the nutritional properties of seed constituents (proteins, and opioid activities.1 In this context, plant proteins and their carbohydrates, ether extract, fiber) in vivo are still unclear. −1 derived protein hydrolysates are increasingly being used as an Proteins in legume seeds represent from about 200 g kg −1 alternative to proteins from animal sources in human nutrition.2 (dry weight) in pea and beans up to 380–400 g kg in Among plants, legume seeds such as soybean (Glycine max), soybean and lupin. Traditionally, the classification of legume beans (Phaseolus spp.), peas (Pisum sativum), lupins (Lupinus proteins is based on their solubility properties: albumins are spp.) and lentils (Lens culinaris) represent rich sources of proteins, soluble in water, globulins are soluble in salt water solutions 8 carbohydrates, several water-soluble vitamins and minerals.3 The and prolamins are soluble in ethanol/water solutions. Most of dietary importance of legume seeds is expected to grow in the them are storage proteins, with the most abundant in grain coming years owing to the protein (and other nutrients) demand legumes being globulins. These are generally classified as 7S of the increasing world population and to the need to reduce the and 11S globulins according to their sedimentation coefficients risks related to consumption of animal food sources, especially in (S). The 7S and 11S globulins of pea are named vicilin and developed countries.4 Moreover, there is at present great interest legumin respectively, so that the corresponding proteins of in the use of home-grown protein sources such as legume seeds because of the high market price of soybean meal, which is entirely ∗ imported from non-European markets. Moreover, the forbidden Correspondence to: Luis A Rubio, Physiology and Biochemistry of Animal use of genetically modified organism (GMO) feed ingredients Nutrition (EEZ, CSIC), Profesor Albareda 1, E-18008 Granada, Spain. E-mail: [email protected] and solvent-extracted oil seeds in organic farming increases the interest in alternative protein sources.5 In this context, field pea Physiology and Biochemistry of Animal Nutrition (EEZ, CSIC), Profesor Albareda constitutes a significant sector of agricultural grain production, 1, E-18008 Granada, Spain J Sci Food Agric (2013) www.soci.org c 2013 Society of Chemical Industry www.soci.org L A Rubio et al. DEFATTED PEA SEED MEAL (PM) Extract with borate buffer (pH 8) at 4 °C Centrifuge (12 000 × g, 30 min, 4 °C) RESIDUE EXTRACT (E) Extract with borate buffer (pH 8) at 4 °C Adjust pH to 4.5 at 4 °C Centrifuge (30 074 × g, 30 min, 4 °C) Stir for 30 min Centrifuge (30 074 × g, 30 min, 4 °C) RESIDUE (PR) EXTRACT SEDIMENT SUPERNATANT A (Freeze-dry) (Combine with E) Resuspend in borate buffer (pH 8) Dialyse (water) Adjust pH to 4.5 Centrifuge (30 074 × g, Stir for 30 min 30 min, 4 °C) Centrifuge (30 074 × g, 30 min, 4 °C) SEDIMENT SUPERNATANT B SEDIMENT SUPERNATANT B Vicilins (7S) (Albumins + soluble NSP) -1 Legumins (11S) Combine with supernatant A (Freeze-dry) (NH4)2SO4 (608 g L ) Dialysis and freeze-dry) Centrifuge SEDIMENT SUPERNATANT C Extensive Extensive dialysis dialysis Freeze-dry Freeze-dry Albumins (Alb) Soluble NSP Figure 1. Procedure for extraction of pea (Pisum sativum cv. Bilbo) seed meal protein fractions. other seeds are often indicated as vicilin- and legumin-like MATERIALS AND METHODS globulins.9 Both albumins and globulins have been claimed to Materials induce a number of health beneficial effects (anticarcinogenic, Trypsin (type III) and α-chymotrypsin (type VII) from bovine antihypertensive, hypoglycemic, hypocholesterolemic, etc.) upon pancreas, N-α-benzoyl-DL-arginine-p-nitroanilide (BAPNA) and N- 4 dietary consumption. Efforts towards large-scale procedures for benzoyl-L-tyrosine ethyl ester (BTEE) were obtained from Sigma- 10 11,12 protein fractionation from pea or chickpea seeds have Aldrich (Alcobendas, Spain). been mainly focused on globulins and albumins. Albumin separation from globulins has not always been successfully achieved owing to the intermediate solubility behaviors of Fractionation procedures some proteins.13 Several physicochemical methods have been Peas (P. sativum cv. Bilbo) were a gift from Limagrain UK Ltd developed for the fractionation of 7S and 11S proteins, (Rothwell, UK). Seeds were ground in a Retsch hammer mill including ultracentrifugation, fractionation and reverse phase (Biometa SA, Llanera, Spain) fitted with a 1 mm mesh screen. The high-performance liquid chromatography (HPLC); however, the meal was treated twice with chloroform/methanol (2:1 v/v) for lipid yields and purities of isolated fractions were usually low, with extraction and then air dried. The protein extraction procedure cross-contamination among fractions being a main drawback.11,14 (Fig. 1) was as in Rubio et al.15 with some modifications. Defatted When the nutritional or functional properties of purified legume meal was extracted (1:10 w/v) with 0.2 mol L−1 borate buffer (pH 8) globulins have been evaluated, complex mixtures of 11S and containing 0.5 mol L−1 NaCl and centrifuged (30 074 × g,30min,4 ◦ 7S proteins have generally been used, and only a few nutritional C). The supernatant was retained (supernatant A) and the borate- studies with protein fractions have been reported so far. Given that insoluble sediment was re-extracted as above and centrifuged. The 7S and 11S protein fractions differ in both protein composition and new sediment (pea residue, PR) was recovered by freeze-drying. potential nutritional applications, it is clear that the establishment The extract (supernatant B) was combined with supernatant A, ofareliableprotocolforfractionationofsufficientamountsofthese adjusted to pH 4.5 with glacial acetic acid in the cold, stirred for 30 ◦ proteins would open up novel opportunities to investigate the use min and centrifuged (30 074 × g,30min,4 C). The sediment was of these fractions in preventive and/or therapeutic medicine. redissolved in borate buffer, dialysed extensively against distilled In order to be tested in vivo and for their nutritional or water and freeze-dried (legumins 11S). The supernatant was also physiological effects to be properly addressed, proteins from dialysed extensively against distilled water and centrifuged (30 074 ◦ legume seeds have to be (1) extracted in sufficient amounts for × g,30min,4 C). The new sediment was freeze-dried (vicilins 7S). −1 their inclusion in diets for experimental animals and (2) chemically The supernatant was treated with 608 g L (NH4)2SO4, stirred for ◦ characterized so that their putative effects in vivo can be related 2 h in the cold and centrifuged (30 074 × g,30min,4 C). The to their chemical structure. Accordingly, pea (P. sativum cv. Bilbo) sediment (albumins, Alb) was dialysed extensively against distilled seed meal was subjected to a chemical
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