Search

Poster presentado en: 7th International Conference on Food Digestion. Cork, Irlanda; 3-5 mayo (2022), The increasing demand on food production to meet the needs of a growing population, coupled to the need to protect the environment, makes it necessary to change the food production system. Legume crops are a great choice as food crops to fulfil many needs, including nurturing the human population and reducing the impact of agriculture on the planet. Peas are an excellent source of proteins, carbohydrates and micronutrients, but the presence of so-called anti-nutritional factors can reduce the bioavailability of nutrients. Among the anti-nutritional proteins are lectin, pea albumin 2 (PA2) and trypsin inhibitors (TI). We have investigated the impact of these proteins on protein digestibility and amino acid availability, using pea seeds lacking these proteins. Three genetic variants were used: i) wild type (WT); ii) seeds lacking trypsin/chymotrypsin inhibitors (TI mutant); and iii) seeds lacking TI, lectin and PA2 (Triple null mutant). In vitro digestions following the INFOGEST protocol were carried out. Significant differences in the degree of hydrolysis, protein profile and amino acid availability were found among pea variants. Proteins resistant to digestion were identified by LC-MS/MS. Our results indicate that pea seeds lacking certain proteins can be used in the development of novel foods with improved digestibility.

Bowman-Birk inhibitors and their variants (BBI) from legumes, such as soybean, pea, lentil and chickpea, are a class of naturally-occurring protease inhibitors which have potential health-promoting properties within the gastrointestinal tract. BBI can resist both acidic conditions and the action of proteolytic enzymes, and transit through the stomach and small intestine without major degradation, permitting significant amounts to reach the large intestine in active form to exert their reported anti-carcinogenic and anti-inflammatory properties. These potential pharmacological benefits have been linked recently to the intrinsic ability of BBI to inhibit serine proteases, and the data suggest that both trypsin- and chymotrypsin-like proteases involved in carcinogenesis should be considered as potential targets of BBI. However, the therapeutic targets and the action mechanisms of BBI remain unknown. Their elucidation will provide insights into the properties of these plant protease inhibitors as colorectal chemopreventive agents, providing a strong base for the development of legume crops and their products as pro-nutritional, health-promoting food. The deployment of modern genomic tools and genome sequence information are underpinning studies of natural and induced polymorphism in BBI. Genetic markers for BBI variants with improved properties can be exploited ultimately in legume breeding programmes to assist the introgression of such variant genes and the development of superior genotypes for human nutrition.

International audience

International audience; Despite their low contents in seeds, protease inhibitors in pea (Pisum sativum L.) have been shown to be important in negatively affecting the performance of pig or poultry. The quantification of these inhibitors by chemical methods is time-consuming and expensive, prompting the development of simple markers to boost progress in breeding programs. Gene polymorphism linked to variation in seed trypsin inhibitor activity has allowed the definition of primers for polymerase chain reaction (PCR) assays, which can be exploited in breeding programs and offer an efficient and cheap pre-screening procedure.

International audience

International audience