Formation of Plant Derived Bioactive Peptides During Simulated Gastro-Intestinal Digestion: A Systematic Review.

Dietary proteins are known to contain bioactive peptides that are released during digestion. Endogenous proteins secreted into the gastrointestinal tract represent a quantitatively greater supply of protein to the gut lumen than those of dietary origin. Many of these endogenous proteins are digested in the gastrointestinal tract but the possibility that these are also a source of bioactive peptides has not been considered. An in silico prediction method was used to test if bioactive peptides could be derived from the gastrointestinal digestion of gut endogenous proteins. Twenty six gut endogenous proteins and seven dietary proteins were evaluated. The peptides present after gastric and intestinal digestion were predicted based on the amino acid sequence of the proteins and the known specificities of the major gastrointestinal proteases. The predicted resultant peptides possessing amino acid sequences identical to those of known bioactive peptides were identified. After gastrointestinal digestion (based on the in silico simulation), the total number of bioactive peptides predicted to be released ranged from 1 (gliadin) to 55 (myosin) for the selected dietary proteins and from 1 (secretin) to 39 (mucin-5AC) for the selected gut endogenous proteins. Within the intact proteins and after simulated gastrointestinal digestion, angiotensin converting enzyme (ACE)-inhibitory peptide sequences were the most frequently observed in both the dietary and endogenous proteins. Among the dietary proteins, after in silico simulated gastrointestinal digestion, myosin was found to have the highest number of ACE-inhibitory peptide sequences (49 peptides), while for the gut endogenous proteins, mucin-5AC had the greatest number of ACE-inhibitory peptide sequences (38 peptides). Gut endogenous proteins may be an important source of bioactive peptides in the gut particularly since gut endogenous proteins represent a quantitatively large and consistent source of protein.

Phytate and Kidney Health: The Roles of Dietary Phytate in Inhibiting Intestinal Phosphorus Absorption and Intravenous Phytate in Decreasing Soft Tissue Calcification

The development of novel protein sources to compensate for the expected future shortage of traditional animal proteins due to their high carbon footprint is a major contemporary challenge in the agri-food industry currently. Therefore, both industry and consumers are placing a greater emphasis on plant proteins as a sustainable source of protein to meet the growing nutritional demand of ever increasing population. In addition to being key alternatives, many plant-based foods have biological properties that make them potentially functional or health-promoting foods, particularly physiologically active peptides and proteins accounting for most of these properties. This review discusses the importance of plant-based protein as a viable and sustainable alternative to animal proteins. The current advances in plant protein isolation and production and characterization of bioactive hydrolysates and peptides from plant proteins are described comprehensively. Furthermore, the recent research on bioactivities and bioavailability of plant protein-derived bioactive peptides is reviewed briefly. The limitations of using bioactive peptides, regulatory criteria, and the possible future applications of plant protein-derived bioactive peptides are highlighted. This review may help understand plant proteins and their bioactive peptides and provide valuable suggestions for future research and applications in the food industry.

Demand for plant-based proteins and plant-based food products is increasing globally. This trend is driven mainly by global population growth and a consumer shift towards more sustainable and healthier diets. Existing plant-based protein foods and meat mimetics often possess undesirable flavor and sensory properties and there is a need to better understand the formation of desirable meat-like flavors from plant precursors to improve acceptance of novel high-protein plant foods. This study aimed to comprehensively characterize the non-volatile flavor metabolites and the volatiles generated in grilled meat (beef, chicken, and pork) and compare these to commercially available meat substitutes and traditional high-protein plant-based foods (natto, tempeh, and tofu). Solid phase microextraction with gas-chromatography mass-spectrometry was used for elucidation of the flavor volatilome. Untargeted characterization of the non-volatile metabolome was conducted using Orbitrap mass spectrometry and Compound DiscovererTM datamining software. The study revealed greater diversity and higher concentrations of flavor volatiles in plant-based foods in comparison to grilled meat, although the odor activity of specific volatiles was not considered. On average, the total amount of volatiles in plant-based products were higher than in meat. A range of concentrations of free amino acids, dipeptide, tripeptides, tetrapeptides, nucleotides, flavonoids, and other metabolites was identified in meat and plant-based foods.

Bioactive peptides from amaranth seed protein hydrolysates induced apoptosis and antimigratory effects in breast cancer cells

The effect of molecular weights on the survivability of casein-derived antioxidant peptides after the simulated gastrointestinal digestion

Potential bioactive peptides obtained after in vitro gastrointestinal digestion of wine lees from sequential fermentations

Bioactive peptides, short chains of amino acids encrypted within food proteins, have emerged as significant biofunctional components with a wide range of physiological benefits. Released during enzymatic hydrolysis, microbial fermentation, or gastrointestinal digestion, these peptides exhibit diverse biological activities, including antihypertensive, antioxidant, antimicrobial, antidiabetic, and immunomodulatory effects. With growing interest in functional foods and natural health-promoting agents, bioactive peptides are increasingly utilized in the food, nutraceutical, and pharmaceutical industries. This review explores the primary sources and advanced extraction techniques of bioactive peptides, elaborates on their mechanisms of action and associated health benefits, and evaluates their industrial applications. Furthermore, the article discusses the current challenges in standardization, bioavailability, and regulatory validation, while highlighting future directions in peptide-based functional product development. As scientific interest and technological capabilities advance, bioactive peptides hold promise for personalized nutrition, preventive healthcare, and sustainable food innovation.

The impact of the world's growing population on food systems and the role of dietary patterns in the management of non-communicable diseases underscore the need to explore sustainable and dietary protein sources. Although microalgae have stood out as alternative sources of proteins and bioactive peptides, some species such as Nannochloropsis gaditana remain unexplored. This study aimed to characterize N. gaditana's proteome and evaluate its potential as a source of bioactive peptides by using an in silico approach. A total of 1955 proteins were identified and classified into functional groups of cellular components, molecular functions, and biological processes. In silico gastrointestinal digestion of identified proteins demonstrated that 202 hydrophobic and low-molecular-size peptides with potential bioactivity were released. Among them, 27 exhibited theorical antioxidant, antihypertensive, antidiabetic, anti-inflammatory, and/or antimicrobial activities. Seven of twenty-seven peptides showed ≥20% intestinal absorption, suggesting potential systemic effects, while the rest could act at local level. Molecular docking demonstrated strong affinities with key enzymes such as MPO, ACE, and DPPIV. Resistance to the digestion, capacity to be absorbed, and multifunctionality were demonstrated for peptide FIPGL. This study highlights N. gaditana's potential as a sustainable source of novel potential bioactive peptides with promising local and systemic biological effects.

Chia (Salvia hispanica) is a well-known pseudo-cereal whose consumption is increasing due to its content of healthy omega-3 and polyunsaturated fatty acids, dietary fiber, antioxidants, vitamins, carotenoids, and minerals, and also because of its high concentration and quality of proteins and a better balance of essential amino acids. This chapter focuses on the potential nutraceutical properties of proteins from chia seeds as a source of bioactive peptides with benefits on human health. An introduction to the main storage protein fractions in chia seeds (prolamin, glutelin, albumin, and globulin) is presented, showing that the last two proteins are found in higher concentrations. Bioactive peptides encrypted in these proteins and released by enzymatic proteolysis with digestive enzymes, microbial or plant enzymes, or by fermentation with starter cultures are also described. Based on its composition and amino acid sequences, we go through different biological activities as reported in the literature: antihypertensive, antithrombotic, hypocholesterolemic, antimicrobial, anti-inflammatory, and antioxidant effects, highlighting the importance of consuming chia seeds as a functional food with potential benefits for health. Finally, the proteins recovered from the oil extraction process are considered, adding value to this by-product as a source of potential bioactive peptides.

Perspective: Unpacking the Wicked Challenges for Alternative Proteins in the United States: Can Highly Processed Plant-Based and Cell-Cultured Food and Beverage Products Support Healthy and Sustainable Diets and Food Systems?

Increasing amounts of data demonstrate a bioactive role of proteins and peptides above and beyond their nutritional impact. The focus of the investigations has mainly been on vitamin- and mineral-binding proteins, on antimicrobial, immunosuppressing/-modulatory proteins, and on proteins with enzyme inhibitory activity as well as on hormones and growth factors from different food proteins; most research has been performed on milk proteins. Because of their molecular size, intact absorption of proteins in the human gastrointestinal tract is limited. Therefore, most of the proteins with biological functions show physiological activity in the gastrointestinal tract by enhancing nutrient absorption, inhibiting enzymes, and modulating the immune system to defend against pathogens. Peptides are released during fermentation or digestion from food proteins by proteolytic enzymes; such peptides have been found mainly in milk. Some of these released peptides exert biological activities such as opiate-like, antihypertensive, mineral-binding, antioxidative, antimicrobial, immuno-, and cytomodulating activity. Intact absorption of these smaller peptides is more likely than that of the larger proteins. Consequently, other organs than the gastrointestinal tract are possible targets for their biological functions. Bioactive proteins as well as bioactive peptides are part of a balanced diet. It is possible to accumulate bioactive peptides in food, for example by using specific microorganisms in fermented dairy products. Although bioactive peptides have been the subject of several studies in vitro and in vivo, their health potential is still under investigation. Up to now, the Commission of European Communities has not (yet) authorized any health claims for bioactive proteins and peptides from food.

Peptide profiling and the bioactivity character of yogurt in the simulated gastrointestinal digestion

Bioactive peptides (BAPs) represent a unique class of peptides known for their extensive physiological functions and their role in enhancing human health. In recent decades, owing to their notable biological attributes such as antioxidant, antihypertensive, antidiabetic, and anti-inflammatory activities, BAPs have received considerable attention. Simulated gastrointestinal digestion (SGD) is a technique designed to mimic physiological conditions by adjusting factors such as digestive enzymes and their concentrations, pH levels, digestion duration, and salt content. Initially established for analyzing the gastrointestinal processing of foods or their constituents, SGD has recently become a preferred method for generating BAPs. The BAPs produced via SGD often exhibit superior biological activity and stability compared with those of BAPs prepared via other methods. This review offers a comprehensive examination of the recent advancements in BAP production from foods via SGD, addressing the challenges of the method and outlining prospective directions for further investigation.

In addition to supplying essential nutrients, some food proteins can confer additional health benefits beyond nutrition. The presence of bioactive proteins and peptides in different foods is a factor not currently taken into consideration when assessing the dietary quality of food proteins. The range of described physiological benefits attributed to bioactive proteins and peptides is diverse. Multiple factors can potentially impact on the ability of a bioactive peptide or protein to elicit an effect. Although some food proteins act directly in their intact form to elicit their effects, generally it is peptides derived from digestion, hydrolysis or fermentation that are of most interest. The levels of bioactive peptides generated must be sufficient to elicit a response, but should not be so high as to be unsafe, thus causing negative effects. In addition, some peptides cause systemic effects and therefore must be absorbed, again in sufficient amounts to elicit their action. Many studies to date have been carried out in vitro; therefore it is important that further trials are conducted in vivo to assess efficacy, dose response and safety of the peptides, particularly if health related claims are to be made. Therefore, methods must be developed and standardised that enable the measurement of health benefits and also the level of bioactive peptides which are absorbed into the bloodstream. Once standardised, such methods may provide a new perspective and an additional mechanism for analysing protein quality which is currently not encompassed by the use of the protein digestibility-corrected amino acid score (PDCAAS).