Proteins from plant-based biomass: effects of post-harvest conditions on protein retention and quality : Part II Yellow pea (original) (raw)
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The Current Situation of Pea Protein and Its Application in the Food Industry
Molecules
Pea (Pisum sativum) is an important source of nutritional components and is rich in protein, starch, and fiber. Pea protein is considered a high-quality protein and a functional ingredient in the global industry due to its low allergenicity, high protein content, availability, affordability, and deriving from a sustainable crop. Moreover, pea protein has excellent functional properties such as solubility, water, and oil holding capacity, emulsion ability, gelation, and viscosity. Therefore, these functional properties make pea protein a promising ingredient in the food industry. Furthermore, several extraction techniques are used to obtain pea protein isolate and concentrate, including dry fractionation, wet fractionation, salt extraction, and mild fractionation methods. Dry fractionation is chemical-free, has no loss of native functionality, no water use, and is cost-effective, but the protein purity is comparatively low compared to wet extraction. Pea protein can be used as a food...
2005
Pea seeds were tempered at moisture contents of 12.0±0.1, 13.0±0.1, 14.0±0.1 and 15.0±0.3%. The seeds with different moisture contents were then milled and fractioned according to the particle size of 53, 106, 212, 425 and 850 µm. Tempering the pea seeds (12.0±0.1, 13.0±0.1, 14.0±0.1 and 15.0±0.3%) did not significantly affect the mass and protein fraction in comparison with the pea seeds that are not tempered (11.45±0.05%). v For the production of pea protein isolate, aqueous-solvent extraction method was used. The protein was extracted with an alkali solution from the ground pea-seeds and precipitated from the extract by bringing the pH down to isoelectric point (pH=4.5). The precipitated protein was separated from the supernatant by centrifugation. The effects of extraction parameters on the yield of extraction such as pH, particle size, temperature, solvent to solid ratio, and salt were studied. The maximum yields were obtained at these conditions; pH: 12.0 for the alkalinity of the extraction medium, 53 µm for the particle size, 40°C for the extraction temperature, 5.0 for the solvent to solid ratio and 0.0 M for the saline concentration. At these extraction conditions, the maximum protein recovery was 72.75% resulting in a product containing 93.29% protein on a dry basis.
2021
The food industry has seen shifting trends towards the use of plant proteins due to a variety of factors including consumer´s perception of health, ethical and religious purposes, as well as environmental considerations. Pulses are good sources of proteins and other nutrients such as resistant starch, dietary fiber, vitamins, minerals, and polyphenols, and therefore have gained particular interest. Among the pulse family, field pea (Pisum sativum) is a widely produced legume that has high nutritional value and low allergenicity. Though a lot of research has been focused on the applications of pea protein, the effect of genotype on the protein structure and functional properties has not been clearly investigated. This research intended to fill the gap by extracting and characterizing pea proteins from seven pea genotypes, consisting of high and regular protein genotypes. After extracting the pea protein, the protein molecular structures were systematically studied such as protein compositions, amino acid profiles, secondary structure, molecular weight by an array of advanced analytical tools including SDS-PAGE, Fourier-transform infrared (FTIR) spectroscopy, HPLC-Size exclusive chromatography (SE) and Differential Scanning Calorimetry (DSC). The protein solubility and functional properties including water and oil holding capacity, foaming and emulsifying properties and gelling capacity were compared between high and regular protein genotype. Pea protein concentrates were successfully extracted from pea grains of all 7 genotype with the protein content ranging from 76.5 % to 86.2 %. Globulins are major storage proteins in pea grains with legumin (11S) and vicilin (7S) as the major globulin fractions. It is interesting to notice that the protein extracts from different pea genotype possess a wide range of 11S/7S ratio from 1.5 to 8.7. While the high protein genotype P0540-41 and P1142-6195 show relatively low 11S/7S ratio (1.5-1.9), the other high protein line P1141-5085 demonstrated an extremely high 11S/7S ratio of 8.6 5± iii 0.65, which is also high when compared to regular protein containing line. In this study, it was observed that the 11S/7S ratio significantly impact the pea protein denaturation temperature. For example, protein extracts from P0540-41 and P1142-6195 with lower 11S/7S ratios had relatively lower denaturation temperatures. When analyzing nutritive value, protein concentrates from Earlystar, Greenwater and P0540-41 show higher sulfur-containing amino acids than other pea genotype, which is a known limiting essential amino acid in pea protein. The protein concentrates from Lacombe and P0540-41 have higher digestibility values of 86.3 % and 88.45 %, respectively compared to those from other pea genotype. In general, the pea protein extracts show good foaming and emulsifying properties, and their foaming stability values are especially high. Among the protein extract samples, those from Cooper and P1142-6195 had relatively low foaming capacity at all tested pHs and the lowest 11S/7S ratio as compared to other samples. It is interesting to notice that the pea protein gelling properties are influenced by the genotypesgenotypes. The protein samples from Earlystar and P0540-41 possess better gelling capacity and their gels showed significantly increased mechanical strength. Among all the pea genotype tested, the high protein line P0540-41presents a better source to generate pea protein concentrate with good overall functional properties to support food applications. This research is the first of its kind to compare not only the protein content of different pea genotype, but also the protein structure and functional properties between high protein genotype and regular protein genotype. Although, it is an initial study with few samples, the results demonstrate that high protein genotype are comparable, and in some instances, superiors to regular protein genotype in terms of protein functionality and nutritive value. This opens the possibility of breeding genotypesgenotypes in order to achieve not only high protein content, but also to target specific protein physical-chemical and functional properties for desirable industry processing and food applications. Preface This thesis is an original work by Rani Lopes Lorenzetti under the supervision of Dr. Lingyun Chen. No part of this thesis has been previously published. v Dedication This thesis is dedicated to my grandfather, who left this earth too earlier to see it completed.
Pilot scale isolation of proteins from field peas (Pisum sativum L.) for use as food ingredients
International Journal of Food Science and Technology, 1999
The protein and starch fractions of field pea (Pisum sativum L.) are potentially a source of novel ingredients for food processing. As part of research to elucidate the functional properties of field pea proteins, the pilot scale extraction of proteins has been undertaken. Two different approaches have been used and the recoveries of protein compared. The first involved extraction with a salt solution followed by decanting and clarification to remove solids. The solution was then further concentrated and salt removed by ultrafiltration and diafiltration. The second procedure was based upon alkaline extraction followed by decanting and recovery by isoelectric precipitation and neutralisation. Both spray drying and freeze drying methods were employed. The protein isolates have been compared and characterised with respect to solubility, chemical composition and to electrophoretic patterns. Overall, the proteins extracted with salt exhibited better physical properties than proteins extracted with alkali, in terms of colour and particle size. The solubilities showed little variation and the electrophoretic patterns were similar. Freeze drying resulted in isolates with darker colour compared with spray drying.
Characterization of pea (Pisum sativum) seed protein fractions
Journal of the Science of Food and Agriculture, 2013
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.
Characterization of pea (Pisum sativum) seed protein fractions
2014
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.
Techno-functional properties of pea (Pisum sativum) protein isolates: A review
Acta Periodica Technologica, 2015
Due to high nutritive quality, good techno-functional properties and low cost, legume protein products are becoming the most appropriate alternative to protein products of animal origin. In food industries, these products are usually used as techno-functional additives which provide specific characteristics of final food products. Legume proteins are commonly used as flour, concentrates, and isolates. The greatest application on industrial scale has soy proteins, and to a lesser extent, in the past 20 years, pea protein isolates. The modest use of pea protein is partly a result of insufficient information relating to their techno-functional properties. This paper is an overview of techno-functional properties of pea proteins and their isolates. Also, the paper deals with the possible use of limited enzymatic hydrolysis as a method for the improvement of their techno-functional properties.
Profile and Functional Properties of Seed Proteins from Six Pea (Pisum sativum) Genotypes
International Journal of Molecular Sciences, 2010
Extractability, extractable protein compositions, technological-functional properties of pea (Pisum sativum) proteins from six genotypes grown in Serbia were investigated. Also, the relationship between these characteristics was presented. Investigated genotypes showed significant differences in storage protein content, composition and extractability. The ratio of vicilin:legumin concentrations, as well as the ratio of vicilin + convicilin: Legumin concentrations were positively correlated with extractability. Our data suggest that the higher level of vicilin and/or a lower level of legumin have a positive influence on protein extractability. The emulsion activity index (EAI) was strongly and positively correlated with the solubility, while no significant correlation was found between emulsion stability (ESI) and solubility, nor between foaming properties and solubility. No association was evident between ESI and EAI. A moderate positive correlation between emulsion stability and foam capacity was observed. Proteins from the investigated genotypes expressed significantly different emulsifying properties and foam capacity at different pH values, whereas low foam stability was detected. It appears that genotype has considerable influence on content, composition and
Food Chemistry, 2011
Commercial pea protein isolate was separated into water-soluble (WS), salt-soluble (SS), alkaline-soluble (AS) and ethanol-soluble (ES) fractions. AS fraction was the most abundant, constituting about 87% of the proteins in PPI followed by WS, SS and ES fractions in decreasing order. ES fraction consistently formed emulsions with a narrow range of smaller oil droplet sizes (0.6-19 lm) at pH 4.0, 7.0 or 9.0 compared to a wider range of sizes for emulsions stabilised by WS, SS and AS fractions. Emulsions formed with ES fraction were also the most stable (p < 0.05) over the 3 h test period at all the pH values used in this work. The WS fraction had significantly highest (p < 0.05) protein solubility and foaming capacity at all the pH values when compared to solubility of PPI, SS, and ES. Except for AS and ES fractions, foaming capacities of the protein fractions were higher at pH 9.0 than at pH 4.0 or 7.0.
Food Research International, 2011
Functional properties of commercial and membrane processed pea protein isolates (PPI) prepared from yellow peas were investigated. Four protein isolates were prepared from yellow pea flour using water and KCl extractions at 25°C followed by ultrafiltration and diafiltration (UF and DF) at pHs of 7.5 and 7.5 or 6 respectively. Following assessment of compositional attributes; solubility, foaming, flow and dynamic rheology, emulsification ability and heat-induced textural and rheological properties of prepared PPIs and a commercially available PPI were tested and compared. Membrane purification of proteins resulted in 28% to 68% reduction in phytic acid and enhanced, comparatively, the tested functional properties. Solubility of membrane processed PPIs, at all tested pHs, was superior and the lowest foaming stability and apparent viscosity were associated with commercial PPI. Gelling temperatures of water and KCl extracted PPIs, DF treated at pH 6, trimmed down to 75.7 ± 0.63°C and 81.6 ± 0.55°C in contrast to that of commercial PPI at above 90°C. Similarly, the formation of firm gels, after 1 h heating at 90°C, was associated with membrane processed PPIs whereas commercial PPI did not develop any gel.