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1 Figura, Olea europaea L. is the source of virgin olive oil (VOO). During its extraction, a high amount of by-products (pomace, mill wastewaters, leaves, stones, and seeds) is originated, which possess an environmental problem. If the generation of waste cannot be prevented, its economic value must be recovered and its effects on the environment and climate change must be avoided or minimized. The bioactive compounds (e.g., phenols, pectins, peptides) of these by-product fractions are being investigated as nutraceutical due to the beneficial properties it might have. In this review, the aim is to summarize the in vivo studies carried out in animals and humans with bioactive compounds exclusively obtained from olive by-products, aiming to demonstrate the potential health benefits these products can exert, as well as to describe its use in the food industry as bioactive ingredient. Several food matrices have been fortified with olive by-products fractions, leading to an improvement of properties. Animal and human studies suggest the benefits of ingesting olive-derived products to promote health. However, the investigation until now is scarce and consequently, well-designed human studies are required in order to fully address and confirm the safety and health-promoting properties of olive oil by-products., Maria C. Millan-Linares acknowledges the financial grant US-1381492 supported by Andalusian Plan for Research, Development, and Innovation 2020 from the European Regional Development Fund (ERDF). Africa Fernandez-Prior has the benefit of a Juan de la Cierva postdoctoral fellowship (FJC2021-047485-I) from the Spanish Ministry of Science and Innovation. Fernando Rivero-Pino acknowledges his postdoctoral contract supported by TED2021-130521A-I00.

11 Páginas.-- 1 Figura.-- 5 Tablas.-- Material suplementario, Hemp is the term commonly used to refer to the variety of Cannabis sativa L. cultivated for industrial purposes. The seeds have gained interest in recent years as functional foods due to their nutritional composition and high content of protein and bioactive compounds. In this study, ten hemp protein hydrolysates (HPHs) were obtained by enzymatic hydrolysis with Alcalase and Flavourzyme from hemp protein isolate (HPI) and their antioxidant properties (DPPH radical scavenging activity, beta-carotene activity and ferric ion reducing antioxidant power (FRAP)) were evaluated. Shorter peptide sequences, mainly obtained with Flavourzyme, were found to react with free radicals more easily. The peptidome of all the hydrolysates was characterized, identifying, and quantifying the peptides. Furthermore, 19 unique peptides were assessed by in silico tools to hypothesize those that could be responsible of the bioactivity reported for the hydrolysates. From the identified peptides, based on the molecular features and the predictions, the peptides KNAIYTPH, EERPGHF, and KNGMMAPH, among others, are proposed to be highly contributing to the antioxidant activity of the hydrolysates., This research was funded by grant P20_00661 from the Andalusian Plan for Research, Development and Innovation (PAIDI) 2020 and by grant US-1381492 from the European Regional Development Fund (ERDF).

4 Figuras.-- 2 Tablas, The increase in the world population along with new policies aimed at a more sustainable world has led to the need of searching for new food sources, which are environmentally friendly, implying healthy and nutritious diets. This study explored the biological activity of two kiwicha (Amaranthus caudatus L.) protein hydrolysates obtained with the aid of Bioprotease LA-660 regarding their anti-inflammatory response at the intestinal level, employing the CACO-2 cell line. The results obtained showed that the in vitro administration of these hydrolysates decreased the expression of proinflammatory cytokines, increased the expression of anti-inflammatory cytokines, and decreased the gene expression of the major components of inflammasomes in the intestinal CACO-2 cell model. To the best of our knowledge, this is the first study involving the evaluation of the anti-inflammatory activity of kiwicha hydrolysates at the intestinal level, employing the CACO-2 cell model and its ultrastructural characterization using scanning electron microscopy. We conclude that the Amaranthus caudatus hydrolysates are a valuable source of active peptides that take part as functional ingredients in food and nutraceutical preparations., This study was supported by a grant from the Andalusian Government (2021/CTS-1074). Rocio Toscano has the benefit of a “Margarita Salas” postdoctoral grant from the Recovery, Transformation and Resilience Plan (Next Generation EU). Elena Grao-Cruces has the benefit of a doctoral fellowship (BES-2012-056104) from the Andalusian Government. Maria C. Millan-Linares acknowledges the financial grant US-1381492 supported by Andalusian Plan for Research, Development, and Innovation 2020 from the European Regional Development Fund (ERDF).

The increase in the world population along with new policies aimed at a more sustainable world has led to the need of searching for new food sources, which are environmentally friendly, implying healthy and nutritious diets. This study explored the biological activity of two kiwicha (

Diabetes prevalence has been rapidly increasing worldwide, and there is a need for searching natural compounds to prevent and treat it. Bioactive peptides derived from insect protein would be an interesting sustainable option. However, the potential of insects such as mealworms (Tenebrio molitor) as source for antidiabetic peptides has not been widely studied. In this work, the influence of ultrasound and the sequential hydrolysis with subtilisin and trypsin hydrolysis were analysed for the release α-glucosidase inhibitory peptides. Short time of ultrasound improved the following releasing of bioactive peptides but longer ultrasound treatment time limited their production. Subtilisin hydrolysis did not allow the release of α-glucosidase inhibitory peptides, but it is needed to cleave the protein before trypsin releases these peptides. These high-bioactive hydrolysates could be used as ingredient regulating the glycaemic index in food formulation.

New challenges in food production and processing are appearing due to increasing global population and the purpose of achieving a sustainable food system. Bioactive peptides obtained from food proteins can be employed to prevent or pre-treat several diseases such as diabetes, cardiovascular diseases, inflammation, thrombosis, cancer, etc. Research on the bioactivity of protein hydrolysates is very extensive, especially in vitro tests, although there are also tests in animal models and in humans studies designed to verify their efficacy. However, there is very little published literature on the functionality of these protein hydrolysates as an ingredient in food matrices, as well as the effect that thermal or non-thermal processing, and storage may have on the bioactivity of these bioactive peptides. This review aims to summarize the published literature on protein hydrolysates as a functional ingredient including processing, storage and simulated gastrointestinal digestion regarding the bioactivity of these peptides inside food matrices.

The book was inadvertently published with an incorrect affiliation. Ermolaos Ververis is affiliated to National and Kapodistrian University of Athens (NKUA), Department of Hygiene, Epidemiology and Medical Statistics, School of Medicine, Athens, Greece and EFSA, Nutrition and Food Innovation Unit, Novel Foods Team, Parma, Italy.

In the European Union, insects and products thereof fall under Regulation (EU) 2283/2015 on Novel Foods, as they were not consumed to a significant degree within the EU before 15 May 1997. This chapter elucidates the risk assessment process performed by EFSA, highlighting the various elements considered when assessing the safety of insect-derived foodstuffs. The information discussed stems from EFSA outputs on the safety evaluation of such products, which have confirmed the safety of their consumption under the proposed conditions of use.

This work was supported by the Spanish Ministry of Economy, Industry and Competitiveness and by FEDER (project CTQ2017-87076-R). The authors would like to thank MealFoodEurope (Salamanca, Spain) for kindly providing Tenebrio molitor meal., The increasing world population has led to the need to search for new protein sources, such as insects, the harvesting of which can be economical and environmentally sustainable. This study explores the biological activities (angiotensin-converting enzyme (ACE) inhibition, antioxidant capacity, and dipeptidyl peptidase IV (DPP-IV) inhibition) of Tenebrio molitor hydrolysates produced by a set of food-grade proteases, namely subtilisin, trypsin, ficin and flavourzyme, and the degree of hydrolysis (DH), ranging from 5% to 20%. Trypsin hydrolysates exhibited the highest ACE inhibitory activity at a DH of 10% (IC50 0.27 mg mL(-1)) in the experimental series, which was attributed to the release of short peptides containing Arg or Lys residues in the C terminus, and described as the ACE-inhibition feature. The levels of in vitro antioxidant activities were comparable to those reported for insect species. Subtilisin and trypsin hydrolysates at a DH of 10% displayed optimal DPPH scavenging and ferric reducing activities, which was attributed to the presence of 5-10-residue active peptides, as reported in the literature. Iron chelating activity was significantly favoured by increasing the DH, attaining a minimal IC50 of 0.8 mg mL(-1) at a DH of 20% regardless of the enzymatic treatment. Similarly, in vitro antidiabetic activity was significantly improved by extensive hydrolysis, and, more specifically, the presence of di- and tripeptides. In this regard, the combined treatment of subtilisin-flavourzyme at a DH of 20% showed maximal DPP-IV inhibition (IC50 2.62 mg mL(-1)). To our knowledge, this is the first study evaluating the DPP-IV activity of Tenebrio molitor hydrolysates obtained from these commercial proteases. We conclude that Tenebrio molitor hydrolysates produced with food-grade proteases are a valuable source of active peptides that can be used as functional ingredients in food and nutraceutical preparations., Spanish Ministry of Economy, Industry and Competitiveness, European Commission CTQ2017-87076-R

The exponential increase in world population is leading to a need for new sustainable protein sources that could supply the high demands without resulting in an enormous environmental impact. Bioactive peptides from food proteins are currently seen as capable of modulating physiological processes, such as diabetes. The potential of insects as a cheap source of antidiabetic peptides is a recent research topic. In this work, fractionation and identification of dipeptidyl peptidase IV (DPP-IV) and α-glucosidase inhibitory peptides from mealworm (Tenebrio molitor) was carried out. Peptides from 500 to 1600 Da showed the highest level of DPP-IV inhibition (IC50 value of 0.91 mg ml-1) and peptides below 500 Da showed the highest level of α-glucosidase inhibition (IC50 value of 2.58 mg ml-1). Numerous novel peptides were identified from the most bioactive fractions, and based on the molecular features usually described for these peptides, some of them are suggested to be the bioactive peptides responsible for the inhibition observed (e.g. APVAH for DPP-IV inhibition and CSR for α-glucosidase inhibition). Hence, these insect protein hydrolysates or their purified fractions could be used as ingredients for regulation of the glycaemic index.

Vegetable proteins are appearing as a sustainable source for human consumption. Food-derived peptides are an important field of research in terms of bioactive molecules. In this study, seven vegetable proteins were enzymatically hydrolysed following an optimised treatment (sequential hydrolysis with subtilisin-trypsin-flavourzyme) to obtain dipeptidyl peptidase IV (DPP-IV) inhibitory peptides. Hydrolysates were fractionated by size exclusion chromatography and, from the most bioactive fractions (corresponding to Glycine max, Chenopodium quinoa and Lupinus albus proteins); peptides responsible for this bioactivity were identified by mass spectrometry. Peptides with adequate molecular features and based on in silico analysis were proposed as DPP-IV inhibitors from soy (EPAAV) lupine (NPLL), and quinoa (APFTVV). These vegetable protein sources are adequate to obtain protein hydrolysates for functional food.

Vegetables consumption in human diets is rapidly increasing due to their proven health benefits and their environmentally friendly character. Chickpea (Cicer arietinum) is an important pulse crop grown consumed worldwide. In this work, different enzymatic treatments were employed to obtain chickpea protein hydrolysates with increased solubility and α-glucosidase inhibitory activity. A sequential hydrolysis with subtilisin and trypsin up to a degree of hydrolysis of 20% showed the highest inhibition (IC50 value of 1.43 ± 0.08 mg/mL) compared to the hydrolysis with single enzymes, or used simultaneously. This hydrolysate was fractionated by size exclusion chromatography. Peptides from 500 to 1100 Da were responsible of the highest level of inhibition, showing an IC50 value of 0.52 ± 0.03 mg/mL. An in silico hydrolysis of the sequences of the major proteins allowed to identify the potential peptides contained in the most active fractions based on their molecular features. The identified peptides were characterized employing different bioinformatics tools to determine which peptides would be most inhibitory ones. These peptides could be potentially employed as ingredient regulating the glycaemic index in food formulation.

Production of bioactive peptides via enzymatic hydrolysis is a sustainable way to take advantage of proteinaceous by-products from food industry, such as fish discards. Sardine pilchardus protein was subjected to different enzymatic treatments using two endopeptidases of different selectivity and one exopeptidase in order to produce hydrolysates with antidiabetic activity. The highest dipeptidyl peptidase IV inhibitory activity was obtained by the combination of three enzymes (subtilisin, trypsin and flavourzyme) employed sequentially. This hydrolysate was subsequently purified by size exclusion chromatography to obtain fractions sorted by size (hydrodynamic volume). Peptides below 1400 Dalton had the highest activity, and these pools were analysed by mass spectrometry in order to identify the peptides responsible for that activity. Numerous peptides with adequate molecular features, it is, owning an alanine (A) as their penultimate N-terminal residue (e.g. NAPNPR, YACSVR) were identified and are proposed to be antidiabetic peptides from Sardine pilchardus muscle.

Protein hydrolysates bioactivity makes them suitable for functional food ingredients. However, their chemical reactivity with different molecules, mainly reducing sugars, might lead to a modification of their structure, and thus function, after their inclusion into food matrices. The effect of food matrix and the storage time on the antihypertensive and antioxidant capacity of sardine hydrolysates was evaluated. Furthermore, bioactivity remaining after simulated gastrointestinal digested samples was also analyzed to verify its potential to be administrated orally. Sugar containing matrix improved the ACE inhibitory and DPPH radical scavenging activity of hydrolysates after thermal treatment and storage up to 80%. Maillard reaction products were responsible for the changes observed in the bioactivity of enriched food. Digested samples showed different but still adequate bioactivity depending on the matrix containing the hydrolysate. These results support the potential of fish protein hydrolysates to be used as ingredient in food formulation.

Numerous peptides derived from food proteins have been identified as bioactive compounds in literature. The final objective of these peptides would be its incorporation to food formulas. However, food processing can modify the bioactive potential of peptides employed in the formulation of functional foods. This study focus on evaluating the changes originated in the antihypertensive and antioxidant capacity of sardine hydrolysates obtained by enzymatic hydrolysis, after heat treatments, high pressure homogenization, ultrasound treatment and spray drying. Both the angiotensin-converting enzyme inhibitory activity and antioxidant activity of sardine hydrolysate did not change or was improved after heat treatments and drying. Similarly, non-thermal treatments led to a slight increase of antihypertensive potential. The resistance of the hydrolysate after different treatments commonly used in food industry suggests its potential use as ingredient in food formulation.