Bioactive Peptides.

A workflow for the characterization of food-derived bioactive peptides is described in this chapter. The workflow integrates two consecutive steps: a discovery phase and a protein-based bioinformatic phase. In the first step (discovery phase), a shotgun bottom-up proteomics approach is used to create a reference data set for a selected food proteome. Afterward, in a second step (bioinformatic phase), the reference proteome is subjected to several in silico protein-based bioinformatic analyses to predict and characterize potential bioactive peptides after an in silico human gastrointestinal digestion. Using this workflow, bioactive collagen peptides, antihypertensive, antimicrobial, and antitumor peptides were predicted as potential valuable bioactive peptides from seafood and marine by-products. It is concluded that the combination of the global shotgun proteomic analysis and the analysis by protein-based bioinformatics can provide a rapid strategy for the characterization of new potential food-derived bioactive peptides.

Milk proteins have been extensively studied for their ability to yield a range of bioactive peptides following enzymatic hydrolysis/digestion. However, many hurdles still exist regarding the widespread utilization of milk protein-derived bioactive peptides as health enhancing agents for humans. These mostly arise from the fact that most milk protein-derived bioactive peptides are not highly potent. In addition, they may be degraded during gastrointestinal digestion and/or have a low intestinal permeability. The targeted release of bioactive peptides during the enzymatic hydrolysis of milk proteins may allow the generation of particularly potent bioactive hydrolysates and peptides. Therefore, the development of milk protein hydrolysates capable of improving human health requires, in the first instance, optimized targeted release of specific bioactive peptides. The targeted hydrolysis of milk proteins has been aided by a range of in silico tools. These include peptide cutters and predictive modeling linking bioactivity to peptide structure [i.e., molecular docking, quantitative structure activity relationship (QSAR)], or hydrolysis parameters [design of experiments (DOE)]. Different targeted enzymatic release strategies employed during the generation of milk protein hydrolysates are reviewed herein and their limitations are outlined. In addition, specific examples are provided to demonstrate how in silico tools may help in the identification and discovery of potent milk protein-derived peptides. It is anticipated that the development of novel strategies employing a range of in silico tools may help in the generation of milk protein hydrolysates containing potent and bioavailable peptides, which in turn may be used to validate their health promoting effects in humans. Graphical abstract The targeted enzymatic hydrolysis of milk proteins may allow the generation of highly potent and bioavailable bioactive peptides.

Production, digestibility and allergenicity of hemp (Cannabis sativa L.) protein isolates

Dietary proteins are known to carry a wide range of nutritional, functional and biological properties. Nutritionally, the proteins are a source of energy and amino acids, which are essential for growth and maintenance. Functionally, the proteins contribute to the physicochemical and sensory properties of various protein-rich foods. Furthermore, many dietary proteins possess specific biological properties which make these components potential ingredients of functional or health-promoting foods. Many of these properties are attributed to physiologically active peptides encrypted in protein molecules. Particularly rich sources of such peptides are milk and egg, but they are also found in meat of various kinds as well as many plants. These peptides are inactive within the sequence of parent protein and can be released during gastrointestinal digestion or food processing. Depending on the amino acid sequence, these peptides may exert a number of different activities in vivo, affecting, e.g., the cardiovascular, endocrine, immune and nervous systems in addition to nutrient utilization. There is increasing commercial interest in the production of bioactive peptides from various sources. Industrial-scale production of such peptides is, however, hampered by the lack of suitable technologies. Bioactive peptides can also be produced from milk proteins through fermentation of milk, by starters employed in the manufacture of fermented milks or cheese. In particular, antihypertensive peptides have been identified in fermented milk, whey and ripened cheese. A few of these peptides have been commercialised in the form of fermented milks. There is a need to develop technologies which retain or even enhance the activity of bioactive peptides in food systems. Also, it is essential to study the optimum utilization of such peptides during passage through the gastrointestinal tract.

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

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

Probiotic therapy, African fermented foods and food-derived bioactive peptides in the management of SARS-CoV-2 cases and other viral infections

Food-derived bioactive peptides (BAPs) are recently utilized as functional food raw materials owing to their potential health benefits. Although there is a huge amount of scientific research about BAPs' identification, purification, characterization, and physiological functions, and subsequently, many BAPs have been marketed, there is a paucity of review on the regulatory requirements, bioavailability, and safety of BAPs. Thus, this review focuses on the toxic peptides that could arise from their primary proteins throughout protein extraction, protein pretreatment, and BAPs' formulation. Also, the influences of BAPs' length and administration dosage on safety are summarized. Lastly, the challenges and possibilities in BAPs' bioavailability and regulatory requirements in different countries were also presented. Results revealed that the human studies of BAPs are essential for approvals as healthy food and to prevent the consumers from misinformation and false promises. The BAPs that escape the gastrointestinal tract epithelium and move to the stomach are considered good peptides and get circulated into the blood using different pathways. In addition, the hydrophobicity, net charge, molecular size, length, amino acids composition/sequences, and structural characteristics of BAPs are critical for bioavailability, and appropriate food-grade carriers can enhance it. The abovementioned features are also vital to optimize the solubility, water holding capacity, emulsifying ability, and foaming property of BAPs in food products. In the case of safety, the possible allergenic and toxic peptides often exhibit physiological functions and could be produced during the hydrolysis of food proteins. It was also noted that the production of iso-peptides bonds and undesirable Maillard reaction might occur during protein extraction, sample pretreatments, and peptide synthesis.

The bioactivities of peptides encrypted in major milk proteins are latent until released and activated by enzymatic proteolysis, e.g. during gastrointestinal digestion or food processing. The proteolytic system of lactic acid bacteria can contribute to the liberation of bioactive peptides. In vitro, the purified cell wall proteinase of Lactococcus lactis was shown to liberate oligopeptides from beta- and alpha-caseins which contain amino acid sequences present in casomorphins, casokinines, and immunopeptides. The further degradation of these peptides by endopeptidases and exopeptidases of lactic acid bacteria could lead to the liberation of bioactive peptides in fermented milk products. However, the sequences of practically all known biologically active peptides can also be cleaved by peptidases from lactic acid bacteria. Activated peptides are potential modulators of various regulatory processes in the body: Opioid peptides are opioid receptor ligands which can modulate absorption processes in the intestinal tract, angiotensin-I-converting enzyme (ACE)-inhibitory peptides are hemodynamic regulators and exert an antihypertensive effect, immunomodulating casein peptides stimulate the activities of cells of the immune system, antimicrobial peptides kill sensitive microorganisms, antithrombotic peptides inhibit aggregation of platelets and caseinophosphopeptides may function as carriers for different minerals, especially calcium. Bioactive peptides can interact with target sites at the luminal side of the intestinal tract. Furthermore, they can be absorbed and then reach peripheral organs. Food-derived bioactive peptides are claimed to be health enhancing components which can be used for functional food and pharmaceutical preparations.

The possible roles of food-derived bioactive peptides in reducing the risk of cardiovascular disease

Functional peptides constitute a class of small molecular peptide chains with specific functions in biology and are typically composed of various amino acids. The chemical‐synthesis methods for preparation of functional peptides can bring high toxicity to the human body. Therefore, there is a growing need to explore alternative, safter sources to obtain bioactive peptides. Food‐derived bioactive peptides (FBPs) stand out as an ideal substitution offering safety and accessibility that can be used in health products and pharmaceuticals to elicit their effects. Presently, the extraction, purification, functional properties, and bioavailability of FBPs have been poorly summarized. This review aims to address this gap by summarizing key aspects of FBPs, covering their source, methods of preparation, extraction, isolation, purification, and identification. Additionally, the review explores the functional characteristics and mechanism underlying FBPs. Emphasis is placed on strategies to enhance the stability and bioaccessibility of FBPs, crucial for their successful application in the food and medical industries. Existing research findings suggest that adopting appropriate methods can extract FBPs with high yield and purity. FBPs exhibit both in vitro and in vivo biological activities regulating relevant pathways, showcasing their potential in the medical field. In the quest for improved stability, the application of nanomaterials emerges as a promising strategy. These advancements collectively hint at a bright future for FBPs in both food and medical matrices. As the field progresses, further exploration and refinement of extraction techniques, functional properties, and bioavailability will contribute to unlocking the full potential of FBPs in various applications.

Interest in food-derived bioactive peptides is on the rise. In 2023, the 3rd International Symposium on Bioactive Peptides (ISBP) was held in Niagara Falls, Canada, to provide a platform for knowledge exchange, networking, and collaboration among researchers in this field. This article aims to provide a high-level overview of the key progress and emerging trends in bioactive peptides based on the 3rd ISBP. This review highlights the production of bioactive peptides from sustainable sources through the integration of artificial intelligence and wet-lab research, the emerging roles of bioactive peptides in cognitive function, and the ability of peptides to act as taste modifiers. The emerging research trend in bioactive peptides focuses on utilizing novel processing technologies, understanding peptide-receptor interactions, applying omics in mechanistic studies, conducting clinical trials, and facilitating product development and commercialization.

Bioactive peptides (BP) are specific protein fragments that can affect biological processes or substrates that have a positive impact on functions and conditions on body health. Plant and animal sources that contain physiologically active food proteins, native or processed, are rich sources of bioactive peptides. Bioactive peptides derived from food proteins have been demostrated to have variety of beneficial effects, such as anti-inflammatory and antioxidant properties. BP are accepted the new generation of biologically active regulators; they can prevent oxidation and microbial degradation in foods and furthermore improve quality of life by treating various diseases and disorders. The present review highlights the recent findings on the roles of various food-derived bioactive peptides in inflammation and oxidative stress and discuss the potential benefits and limitations of using these compounds against the burden of chronic diseases.

Bioactive peptides (BP) are specific protein fragments that can affect biological processes or substrates that have a positive impact on functions and conditions on body health. Plant and animal sources that contain physiologically active food proteins, native or processed, are rich sources of bioactive peptides. Bioactive peptides derived from food proteins have been demostrated to have variety of beneficial effects, such as anti-inflammatory and antioxidant properties. BP are accepted the new generation of biologically active regulators; they can prevent oxidation and microbial degradation in foods and furthermore improve quality of life by treating various diseases and disorders. The present review highlights the recent findings on the roles of various food-derived bioactive peptides in inflammation and oxidative stress and discuss the potential benefits and limitations of using these compounds against the burden of chronic diseases.

Streamlining Bioactive Peptide Discovery With In Silico Prospecting: An investigation on Seaweed Pacific Dulse