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Forster, C.; North, Helen; Afzal, Naureen; Domoney, Claire; Hornostaj, Andrzej R.; Robinson, David S.; Casey, R.

doi:10.1023/a:1006173313548

Cited by 30 publications

(9 citation statements)

References 28 publications

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“… 42 The studied genotypes show noticeable variation in the intensity of lipoxygenase bands ( Figure S2 ), but establishing the significance of this variation requires further scrutiny. In other legumes such as soybean 43 and pea, 44 efforts to develop genotypes lacking the major seed protein lipoxygenase have been successful.…”

Section: Results and Discussionmentioning

confidence: 99%

Identification and Quantification of Major Faba Bean Seed Proteins

Warsame

Michael

O’Sullivan

et al. 2020

J. Agric. Food Chem.

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Faba bean ( Vicia faba L. ) holds great importance for human and animal nutrition for its high protein content. However, better understanding of its seed protein composition is required in order to develop cultivars that meet market demands for plant proteins with specific quality attributes. In this study, we screened 35 diverse Vicia faba genotypes by employing the one-dimensional sodium dodecyl sulfate–polyacrylamide gel electrophoresis (1D SDS-PAGE) method, and 35 major protein bands obtained from three genotypes with contrasting seed protein profiles were further analyzed by mass spectrometry (MS). Twenty-five of these protein bands (MW range: ∼ 9–107 kDa) had significant (p ≤ 0.05) matches to polypeptides in protein databases. MS analysis showed that most of the analyzed protein bands contained more than one protein type and, in total, over 100 proteins were identified. These included major seed storage proteins such as legumin, vicilin, and convicilin, as well as other protein classes like lipoxygenase, heat shock proteins, sucrose-binding proteins, albumin, and defensin. Furthermore, seed protein extracts were separated by size-exclusion high-performance liquid chromatography (SE-HPLC), and percentages of the major protein classes were determined. On average, legumin and vicilin/convicilin accounted for 50 and 27% of the total protein extract, respectively. However, the proportions of these proteins varied considerably among genotypes, with the ratio of legumin:vicilin/convicilin ranging from 1:1 to 1:3. In addition, there was a significant (p < 0.01) negative correlation between the contents of these major fractions (r = −0.83). This study significantly extends the number of identified Vicia faba seed proteins and reveals new qualitative and quantitative variation in seed protein composition, filling a significant gap in the literature. Moreover, the germplasm and screening methods presented here are expected to contribute in selecting varieties with improved protein content and quality.

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Section: Results and Discussionmentioning

confidence: 99%

Identification and Quantification of Major Faba Bean Seed Proteins

Warsame

Michael

O’Sullivan

et al. 2020

J. Agric. Food Chem.

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“…As such, both mutants provide opportunities for the combination of mutations in order to reduce the content of anti-nutritional proteins in seeds. Null mutations have been reported for albumin 2 [ 41 ] and a lipoxygenase enzyme [ 42 ] previously in pea. More recently, several null mutations were identified following high-throughput screens of a population generated by fast neutron mutagenesis of pea [ 43 ].…”

Section: Discussionmentioning

confidence: 99%

Eliminating Anti-Nutritional Plant Food Proteins: The Case of Seed Protease Inhibitors in Pea

et al. 2015

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Several classes of seed proteins limit the utilisation of plant proteins in human and farm animal diets, while plant foods have much to offer to the sustainable intensification of food/feed production and to human health. Reduction or removal of these proteins could greatly enhance seed protein quality and various strategies have been used to try to achieve this with limited success. We investigated whether seed protease inhibitor mutations could be exploited to enhance seed quality, availing of induced mutant and natural Pisum germplasm collections to identify mutants, whilst acquiring an understanding of the impact of mutations on activity. A mutant (TILLING) resource developed in Pisum sativum L. (pea) and a large germplasm collection representing Pisum diversity were investigated as sources of mutations that reduce or abolish the activity of the major protease inhibitor (Bowman-Birk) class of seed protein. Of three missense mutations, predicted to affect activity of the mature trypsin / chymotrypsin inhibitor TI1 protein, a C77Y substitution in the mature mutant inhibitor abolished inhibitor activity, consistent with an absolute requirement for the disulphide bond C77-C92 for function in the native inhibitor. Two further classes of mutation (S85F, E109K) resulted in less dramatic changes to isoform or overall inhibitory activity. The alternative strategy to reduce anti-nutrients, by targeted screening of Pisum germplasm, successfully identified a single accession (Pisum elatius) as a double null mutant for the two closely linked genes encoding the TI1 and TI2 seed protease inhibitors. The P. elatius mutant has extremely low seed protease inhibitory activity and introgression of the mutation into cultivated germplasm has been achieved. The study provides new insights into structure-function relationships for protease inhibitors which impact on pea seed quality. The induced and natural germplasm variants identified provide immediate potential for either halving or abolishing the corresponding inhibitory activity, along with associated molecular markers for breeding programmes. The potential for making large changes to plant protein profiles for improved and sustainable food production through diversity is illustrated. The strategy employed here to reduce anti-nutritional proteins in seeds may be extended to allergens and other seed proteins with negative nutritional effects. Additionally, the novel variants described for pea will assist future studies of the biological role and health-related properties of so-called anti-nutrients.

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“…Lipoxygenase (LOX)-promoted oxidation of lipids contributes some of the VOCs in protein ingredients. Forster et al (1999) reported a lower concentration of hydroperoxides were formed in a pea seed free of the enzyme LOX-2. Thus, the contribution of LOX in the generation of VOCs starts with hydroperoxide formation.…”

Section: Volatile Organic Compoundsmentioning

confidence: 98%

Plant protein flavor chemistry fundamentals and techniques to mitigate undesirable flavors

Vatansever,

Chen,

Hall

2024

Sustainable Food Proteins

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Many plant protein ingredients have unpleasant flavor (e.g., green, beany, bitterness) characteristics. Isolation of the protein fraction will reduce the intensity of the undesirable flavors but in most cases the flavor issue is not eliminated. The objective of this review is to provide information about undesirable flavors associated with plant proteins and approaches to mitigate these flavors. The focus of the review will be on flavor associated with plant proteins from pulses, soybean, and oilseeds (e.g., hempseed, flaxseed). While other plant proteins exist, they will not be covered extensively in this limited review. The undesirable flavors are defined as volatile organic compounds (VOCs) and non‐volatile organic compounds (non‐VOCs). Example VOCs include aldehydes, ketones, and isobutyl pyrazines whereas saponins, bitter peptides, and phenolics are among the most common non‐VOCs. The raw material used as the source for the protein dictates the undesirable flavors remaining in the protein ingredient. The intensity of the binding of the VOCs and non‐VOCs to protein serves as the basis for the detection and difficulty in removing these compounds from the protein. A discussion about flavor binding and processing methods to mitigate unwanted flavors in protein ingredients will be provided. Methods presented will focus on extraction and thermal treatment. Although flavor masking is an approach to minimize undesirable, this topic will not be covered. Understanding the compounds responsible for the flavor issues and methods to minimize their impacts on sensory characteristic of protein ingredients can provide manufacturers with solutions to addressing flavor issues inherent to plant proteins.

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Cited by 30 publications

References 28 publications

Identification and Quantification of Major Faba Bean Seed Proteins

Identification and Quantification of Major Faba Bean Seed Proteins

Eliminating Anti-Nutritional Plant Food Proteins: The Case of Seed Protease Inhibitors in Pea

Plant protein flavor chemistry fundamentals and techniques to mitigate undesirable flavors

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