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We live in the Big Data Era which affects many aspects of science, including research on bioactive peptides derived from foods, which during the last few decades have been a focus of interest for scientists. These two issues, i.e., the development of computer technologies and progress in the discovery of novel peptides with health-beneficial properties, are closely interrelated. This Chapter presents the example applications of bioinformatics for studying biopeptides, focusing on main aspects of peptide analysis as the starting point, including: (i) the role of peptide databases; (ii) aspects of bioactivity prediction; (iii) simulation of peptide release from proteins. Bioinformatics can also be used for predicting other features of peptides, including ADMET, QSAR, structure, and taste. To answer the question asked "bioinformatics and bioactive peptides from foods: do they work together?", currently it is almost impossible to find examples of peptide research with no bioinformatics involved. However, theoretical predictions are not equivalent to experimental work and always require critical scrutiny. The aspects of compatibility of in silico and in vitro results are also summarized herein.
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Alimentos , Péptidos , Péptidos/química , Simulación por Computador , Biología Computacional/métodosRESUMEN
This study aimed to evaluate the association of diet quality and perception of consumption benefits with intake of fermented dairy products in a representative sample of the Polish population. The study was carried out in February 2020 and involved 2009 men and women randomly sampled from the representative Polish population stratified into two age groups (19-30 and 66-75 years). Dairy product intake was evaluated using a qualitative food frequency questionnaire. Diet quality was assessed by calculating the Mediterranean Diet Adherence Screener (MEDAS) score. The perceived health benefit of dairy product consumption was assessed by a literature-based questionnaire. The Health Concern Scale was used to measure participants' attitudes toward health. The median intake of fermented dairy products was 0.8 portion/day (IQR: 0.4-1.6). Intake of fermented dairy products was associated with a higher MEDAS score. We observed that people with the highest intake of fermented dairy products consumed more oils, vegetables, wine, legumes, fish and seafood, sweets and pastries, nuts, had a higher preference for white meat and were more likely to report their perceived benefits to maintain body weight, reduce cardiovascular risk, and improve immune and dental health. Moreover, a high intake of fermented dairy products was positively related to paying more attention to health. Our study identified patterns of health behaviors associated with the frequent consumption of fermented dairy products. We observed that the intake of fermented dairy products is associated with better diet quality, consumer self-consciousness, and a greater attitude toward personal health.
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Productos Lácteos Cultivados , Dieta Mediterránea , Animales , Dieta , Productos Lácteos , Verduras , Peso CorporalRESUMEN
The aim of this study was to characterize the digests and peptides derived from oat kernel proteins in terms of their major enzyme inhibitory activities related to the prevention of cardiometabolic syndrome. It also entailed the characteristics of antioxidant bioactivity of the analyzed material. The study was carried out using coupled in silico and in vitro methods. The additional goal was to investigate whether identified peptides can pervade Caco-2 cells. Based on the results of bioinformatic analysis, it was found that the selected oat proteins may be a potential source of 107 peptides with DPP-IV and/or ACE inhibitory and/or antioxidant activity. The duodenal digest of oat kernels revealed multiple activities. It inhibited the activities of the following enzymes: DPP-IV (IC50 = 0.51 vs. 10.82 mg/mL of the intact protein), α-glucosidase (IC50 = 1.55 vs. 25.20 mg/mL), and ACE (IC50 = 0.82 vs. 34.52 mg/mL). The DPPH⢠scavenging activity was 35.7% vs. 7.93% that of the intact protein. After in silico digestion of oat proteins, 24 peptides were selected for identification using LC-Q-TOF-MS/MS. Among them, 13 sequences were successfully identified. One of them, i.e., VW peptide, exhibited triple activities, i.e., DPP-IV and ACE inhibitory and DPPH⢠scavenging activity. The multifunctional peptides: PW, TF, VF, and VW, were identified in the basolateral samples after transport experiments. Both in silico and in vitro analyses demonstrated that oat kernel proteins were the abundant sources of bioactive digests and peptides to be used in a diet for patients suffering from cardiometabolic syndrome.
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Inhibidores de la Dipeptidil-Peptidasa IV , Síndrome Metabólico , Humanos , Avena/química , Síndrome Metabólico/prevención & control , Células CACO-2 , Inhibidores de la Dipeptidil-Peptidasa IV/química , Espectrometría de Masas en Tándem , Péptidos/químicaRESUMEN
This study is the first to present an integrated approach involving in silico and in vitro protocols that was pursued to analyse an antioxidative potency of Gouda cheese with modified content of ß-casein. Firstly, the predictions of the presence of antioxidant peptides in the casein sequences were computed using the BIOPEP-UWM database. Then, the antioxidative bioactivity of six variants of Gouda cheese (with reduced, normative, and increased content of ß-casein at the initial and final stage of ripening) was assessed. Finally, the RP-HPLC-MS/MS was applied to identify antioxidative peptides in Gouda-derived water-soluble extracts (WSEs). Analyses were supported with the heatmaps and the computation of parameters describing the efficiency of proteolysis of caseins in the modified Gouda cheeses, i.e., the frequency and the relative frequency of the release of antioxidative fragments during cheese ripening (AEexp and Wexp., respectively). All Gouda cheese variants exhibited the antioxidative potential which differed depending on the assay employed. The highest antioxidative activity (ABTS·+ radical scavenging effect, FRAP, and Fe-chelating) was observed for WSEs derived from Gouda cheese with increased content of ß-casein after the 60th day of ripening. The results obtained suggest the potential of Gouda cheese as the antioxidant-promoting food.
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Queso , Antioxidantes , Caseínas/química , Queso/análisis , Péptidos , Espectrometría de Masas en TándemRESUMEN
The aim of the study presented here was to determine if there is a correlation between the presence of specific protein domains within tree nut allergens or tree nut allergen epitopes and the frequency of bioactive fragments and the predicted susceptibility to enzymatic digestion in allergenic proteins from tree nuts of cashew (Anacardium occidentale), pecan (Carya illinoinensis), English walnut (Juglans regia) and pistachio (Pistacia vera) plants. These bioactive peptides are distributed along the length of the protein and are not enriched in IgE epitope sequences. Classification of proteins as bioactive peptide precursors based on the presence of specific protein domains may be a promising approach. Proteins possessing a vicilin, N-terminal family domain, or napin domain contain a relatively low occurrence of bioactive fragments. In contrast, proteins possessing the cupin 1 domain without the vicilin N-terminal family domain contain a relatively high total frequency of bioactive fragments and predicted release of bioactive fragments by the joint action of pepsin, trypsin, and chymotrypsin. This approach could be utilized in food science to simplify the selection of protein domains enriched for bioactive peptides.
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Apart from the classical (experimental) methods, biologically active peptides can be studied via bioinformatics approach, also known as in silico analysis. This study aimed to verify the following research hypothesis: ACE inhibitors and antioxidant peptides can be released from salmon and carp proteins during simulated in silico human-like gastrointestinal digestion. The potential to release biopeptides was evaluated using the BIOPEP-UWM quantitative criteria including the profile of biological activity, frequency of the occurrence (A)/release (AE) of fragments with an ACE inhibitory or antioxidant activity by selected enzymes, and relative frequency of release of bioactive fragments with a given activity by selected enzymes (W). Salmon collagen and myofibrillar proteins of carp turned out to be the best potential source of the searched peptides-ACE inhibitors and antioxidant peptides. Nonetheless, after digestion, the highest numbers of ACE inhibitors and antioxidant peptides were potentially released from the myofibrillar proteins of salmon and carp. Peptide Ranker Score, Pepsite2, and ADMETlab platform were applied to evaluate peptides' bioactivity potential, their safety and drug-like properties. Among the 63 sequences obtained after the simulated digestion of salmon and carp proteins, 30 were considered potential biopeptides. The amino acid sequences of ACE-inhibiting and antioxidant peptides were predominated by P, G, F, W, R, and L. The predicted high probability of absorption of most analyzed peptides and their low toxicity should be considered as their advantage.
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Inhibidores de la Enzima Convertidora de Angiotensina/metabolismo , Antioxidantes/metabolismo , Colágeno/metabolismo , Biología Computacional/métodos , Digestión , Proteínas de Peces/metabolismo , Fragmentos de Péptidos/metabolismo , Animales , Carpas , Tracto Gastrointestinal , Humanos , SalmónRESUMEN
In silico and in vitro methods were used to analyze ACE- and DPP-IV-inhibiting potential of Gouda cheese with a modified content of ß-casein. Firstly, the BIOPEP-UWM database was used to predict the presence of ACE and DPP-IV inhibitors in casein sequences. Then, the following Gouda cheeses were produced: with decreased, increased, and normative content of ß-casein after 1 and 60 days of ripening each (six variants in total). Finally, determination of the ACE/DPP-IV-inhibitory activity and the identification of peptides in respective Gouda-derived water-soluble extracts were carried out. The identification analyses were supported with in silico calculations, i.e., heatmaps and quantitative parameters. All Gouda variants exhibited comparable ACE inhibition, whereas DPP-IV inhibition was more diversified among the samples. The samples derived from Gouda with the increased content of ß-casein (both stages of ripening) had the highest DPP-IV-inhibiting potency compared to the same samples measured for ACE inhibition. Regardless of the results concerning ACE and DPP-IV inhibition among the cheese samples, the heatmap showed that the latter bioactivity was predominant in all Gouda variants, presumably because it was based on the qualitative approach (i.e., peptide presence in the sample). Our heatmap did not include the bioactivity of a single peptide as well as its quantity in the sample. In turn, the quantitative parameters showed that the best sources of ACE/DPP-IV inhibitors were all Gouda-derived extracts obtained after 60 days of the ripening. Although our protocol was efficient in showing some regularities among Gouda cheese variants, in vivo studies are recommended for more extensive investigations of this subject.
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Inhibidores de la Enzima Convertidora de Angiotensina/aislamiento & purificación , Caseínas/química , Queso/análisis , Inhibidores de la Dipeptidil-Peptidasa IV/aislamiento & purificación , Inhibidores de la Enzima Convertidora de Angiotensina/química , Biología Computacional , Dipeptidil Peptidasa 4/química , Inhibidores de la Dipeptidil-Peptidasa IV/química , Humanos , Péptidos/química , Péptidos/aislamiento & purificación , Péptidos/farmacología , Peptidil-Dipeptidasa A/química , Peptidil-Dipeptidasa A/genéticaRESUMEN
Phosphorylation represents one of the most important modifications of amino acids, peptides, and proteins. By modifying the latter, it is useful in improving the functional properties of foods. Although all these substances are broadly annotated in internet databases, there is no unified code for their annotation. The present publication aims to describe a simple code for the annotation of phosphopeptide sequences. The proposed code describes the location of phosphate residues in amino acid side chains (including new rules of atom numbering in amino acids) and the diversity of phosphate residues (e.g., di- and triphosphate residues and phosphate amidation). This article also includes translating the proposed biological code into SMILES, being the most commonly used chemical code. Finally, it discusses possible errors associated with applying the proposed code and in the resulting SMILES representations of phosphopeptides. The proposed code can be extended to describe other modifications in the future.
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Secuencia de Aminoácidos/genética , Aminoácidos/genética , Anotación de Secuencia Molecular , Proteínas/genética , Aminoácidos/clasificación , Código Genético/genética , Humanos , Fosfopéptidos/clasificación , Fosfopéptidos/genética , Fosforilación/genética , Proteínas/clasificaciónRESUMEN
The potential of collagens to release biopeptides was evaluated using the BIOPEP-UWM-implemented quantitative criteria including the frequency of the release of fragments with a given activity by selected enzyme(s) (AE), relative frequency of release of fragments with a given activity by selected enzyme(s) (W), and the theoretical degree of hydrolysis (DHt). Cow, pig, sheep, chicken, duck, horse, salmon, rainbow trout, goat, rabbit, and turkey collagens were theoretically hydrolyzed using: stem bromelain, ficin, papain, pepsin, trypsin, chymotrypsin, pepsin+trypsin, and pepsin+trypsin+chymotrypsin. Peptides released from the collagens having comparable AE and W were estimated for their likelihood to be bioactive using PeptideRanker Score. The collagens tested were the best sources of angiotensin I-converting enzyme (ACE) and dipeptidyl peptidase IV (DPP-IV) inhibitors. AE and W values revealed that pepsin and/or trypsin were effective producers of such peptides from the majority of the collagens examined. Then, the SwissTargetPrediction program was used to estimate the possible interactions of such peptides with enzymes and proteins, whereas ADMETlab was applied to evaluate their safety and drug-likeness properties. Target prediction revealed that the collagen-derived peptides might interact with several human proteins, especially proteinases, but with relatively low probability. In turn, their bioactivity may be limited by their short half-life in the body.
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The BIOPEP-UWM™ database of bioactive peptides (formerly BIOPEP) has recently become a popular tool in the research on bioactive peptides, especially on these derived from foods and being constituents of diets that prevent development of chronic diseases. The database is continuously updated and modified. The addition of new peptides and the introduction of new information about the existing ones (e.g., chemical codes and references to other databases) is in progress. New opportunities include the possibility of annotating peptides containing D-enantiomers of amino acids, batch processing option, converting amino acid sequences into SMILES code, new quantitative parameters characterizing the presence of bioactive fragments in protein sequences, and finding proteinases that release particular peptides.
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Péptidos/química , Secuencia de Aminoácidos , Aminoácidos/química , Animales , Bases de Datos Factuales , Humanos , Péptido Hidrolasas/químicaRESUMEN
Multiple linear regression (MLR) models were constructed to explain the bitter taste of di- and tripeptides based on their chemical nature (structure). Sequences (51 di- and 51 tripeptides) were derived from the BIOPEP-UWM database of sensory peptides and amino acids. The measure of their bitterness was Rcaf. , that is, bitterness relative to that of 1 mM caffeine solution (Rcaf. = 1.0). The variables were the indices describing properties of a single residue forming a peptide structure taken from ProtScale and Biological Magnetic Resonance Data Bank. MLR was made for two separate data sets by use of Statistica 13.1. We found that the presence of branched side residues or ring in a di- or tripeptide sequence (as in L, I, V, Y, F) affected its bitterness. Another variable affecting the bitter taste of di- and tripeptides was the hydrophobicity of amino acids. Using the commonly available statistical tools as well as chemical information reflecting the nature of peptides may be helpful in understanding the structure-taste relationship in food peptides. PRACTICAL APPLICATIONS: Our approach takes account of bioinformatic and cheminformatic techniques of data mining to analyze structure-bitterness of di- and tripeptides derived from food protein sources. Data on bitter peptides available in databases of biological and chemical information can be useful in creating models which help understanding the relationship between the role of structural properties of a molecule (e.g., peptide) and its function (e.g., taste). The bitterness of a peptide resulting from the presence of specific residues in its sequence, which represent different physicochemical properties may contribute to extending the knowledge about their taste-forming role in food systems. Such knowledge may be useful in designing food products with improved properties like taste which can be either enhanced or masked (considered as unwanted when thinking about the sensory value of foods). Our research strategy is universal and can also be applied to study structure-function relationships of peptides with other activities.
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Proteínas en la Dieta/química , Dipéptidos/farmacología , Oligopéptidos/farmacología , Gusto/efectos de los fármacos , Dipéptidos/química , Humanos , Oligopéptidos/química , Relación Estructura-ActividadRESUMEN
Forward and backward stepwise regression (FR and BR, respectively) was applied for the structureâ»bioactivity prediction of angiotensin converting enzyme (ACE)-inhibitory/bitter-tasting dipeptides. The datasets used in this study consisted of 28 sequences and numerical variables reflecting dipeptides' physicochemical nature. The data were acquired from the BIOPEP-UWM, Biological Magnetic Resonance Databank, ProtScale, and AAindex databases. The calculations were computed using STATISTICA®13.1. FR/BR models differed in R² (0.91/0.76, respectively). The impact of C-atC(-) and N-Molw(+) on the dual function of dipeptides was observed. Positive (+) and negative (-) correlations with log IC50 are presented in parens. Moreover, C-Bur(+), N-atH(+), and N-Pol(-) were also found to be important in the FR model. The additional statistical significance of N-bul(-), N-Bur(-), and N-Hdr(+) was reported in the BR model. These attributes reflected the composition of the dipeptides. We report that the "ideal" bitter ACE inhibitor should be composed of P, Y, F (C-end) and G, V, I, L (N-end). Functions: log Rcaf. = f (observed log IC50) and log Rcaf. = f (predicted log IC50) revealed no direct relationships between ACE inhibition and the bitterness of the dipeptides. It probably resulted from some structural discrepancies between the ACE inhibitory/bitter peptides and/or the measure of activity describing one of the two bioactivities. Our protocol can be applicable for the structureâ»bioactivity prediction of other bioactivities peptides.
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Inhibidores de la Enzima Convertidora de Angiotensina/química , Dipéptidos/química , Bases de Datos Factuales , Relación Estructura-Actividad CuantitativaRESUMEN
Diet is considered to be a significant factor in cancer prevention and therapy. Many food components reveal anticancer activity. The increasing number of experiments concerning the anticancer potential of chemical compounds, including food components, is a challenge for data searching. Specialized databases provide an opportunity to overcome this problem. Data concerning the anticancer activity of chemical compounds may be found in general databases of chemical compounds and databases of drugs, including specialized resources concerning anticancer compounds, databases of food components, and databases of individual groups of compounds, such as polyphenols or peptides. This brief review summarizes the state of knowledge of chemical databases containing information concerning natural anticancer compounds (e.g., from food). Additionally, the information about text- and structure-based search options and links between particular internet resources is provided in this paper. Examples of the application of databases in food and nutrition sciences are also presented with special attention to compounds that are interesting from the point of view of dietary cancer prevention. Simple examples of potential database search possibilities are also discussed.
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Productos Biológicos/química , Neoplasias/tratamiento farmacológico , Acceso a la Información , Productos Biológicos/uso terapéutico , Bases de Datos de Compuestos Químicos , Dieta , Humanos , Navegador WebRESUMEN
Metabolic syndrome (MSyn) includes physiological, biochemical, clinical, and metabolic abnormalities, leading to an increase in health problems like obesity, dyslipidemia, cardiovascular diseases, and diabetes, which contribute to an increase in mortality rate. One of the main factors having a key impact on our health is the food we consume. Thus, scientists work towards the discovery of novel bioactive compounds with therapeutic potential to address MSyn. According to scientific reports, peptides derived from food proteins exhibit bioactivities important for the prevention of MSyn diseases; that is, they regulate blood pressure and glycemia; reduce cholesterol level and body mass; and scavenge free radicals. The aim of this review is to study the potential role of peptides in the prevention of MSyn. Particularly peptides which exhibit the following activities: antihypertensive [angiotensin-converting enzyme (ACE) inhibition (EC 3.4.15.1)], antidiabetic [dipeptidyl peptidase IV (DPP-IV) (EC 3.4.14.5)/α-glucosidase (EC 3.2.1.20)/α-amylase (EC 3.2.1.1) inhibition)], cholesterol level reduction, antioxidative, and obesity prevention, were studied. If possible, special attention is paid in the review to the bioactivities of peptides that were measured in vivo. Some examples of peptides showing dual or multiple action against MSyn targets are presented. Moreover, using the database of bioactive peptide sequences (BIOPEP) we made a list of peptides serving simultaneous functions in counteracting MSyn dysfunctions. Such an approach may simplify the discovery of MSyn preventive peptides, as well as highlight some of them as potent bioactive ingredients that may be incorporated into foods. Moreover, the research strategy involving the in silico and in vitro/in vivo methodologies may be useful in the production of food protein hydrolysates supporting the treatment of MSyn dysfunctions.
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Contemporary peptide science exploits methods and tools of bioinformatics, and cheminformatics. These approaches use different languages to describe peptide structures-amino acid sequences and chemical codes (especially SMILES), respectively. The latter may be applied, e.g., in comparative studies involving structures and properties of peptides and peptidomimetics. Progress in peptide science "in silico" may be achieved via better communication between biologists and chemists, involving the translation of peptide representation from amino acid sequence into SMILES code. Recent recommendations concerning good practice in chemical information include careful verification of data and their annotation. This publication discusses the generation of SMILES representations of peptides using existing software. Construction of peptide structures containing unnatural and modified amino acids (with special attention paid on glycosylated peptides) is also included. Special attention is paid to the detection and correction of typical errors occurring in SMILES representations of peptides and their correction using molecular editors. Brief recommendations for training of staff working on peptide annotations, are discussed as well.
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Aminoácidos/química , Biología Computacional/métodos , Péptidos/química , Peptidomiméticos/química , Secuencia de Aminoácidos , Glicosilación , Estructura Molecular , Programas Informáticos , Relación Estructura-ActividadRESUMEN
Carp muscle tissue is a valuable source of biologically active constituents known to positively influence human health. In this study, carp protein digests/hydrolysates generated by human/ porcine digestive enzymes were analysed for their angiotensin I-converting enzyme inhibitory (ACEi) activity. The ex vivo digests and in vitro hydrolysates were used in a screening for ACEi peptides as well. Carp proteins were hydrolysed more rapidly by human gastrointestinal juices than by porcine enzymes. Sarcoplasmic protein fractions were digested/hydrolysed more easily than the myofibrillar ones. The inhibitory concentrations at 50% (IC50) for ex vivo digested sarcoplasmic and myofibrillar protein fractions were established at 1.50 and 1.04 mg/mL, respectively. While, for in vitro hydrolysed sarcoplasmic and myofibrillar protein fractions, the IC50 values were calculated as 2.57 and 1.12 mg/mL, respectively. The digested/hydrolysed samples of carp sarcoplasmic and myofibrillar protein fractions were separated by RP-HPLC-MS. Amino acid sequences were identified with the use of the LC-MS/MS method coupled with in silico systematic screening for ACEi peptides. ACEi peptides with IVY, IY, VY, ALPHA and VKAGF sequences were found in the carp digests/hydrolysates. In the ex vivo carp digest, an ACEi peptide TVY was also detected, while the ACEi peptide IW was identified in in vitro hydrolysate. Our study showed that different ACEi effects of carp digests and hydrolysates were generated with the use of human gastrointestinal and porcine enzymes.
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Inhibidores de la Enzima Convertidora de Angiotensina/farmacología , Carpas/metabolismo , Proteínas de Peces/análisis , Tracto Gastrointestinal/enzimología , Péptidos/aislamiento & purificación , Inhibidores de la Enzima Convertidora de Angiotensina/química , Inhibidores de la Enzima Convertidora de Angiotensina/aislamiento & purificación , Animales , Proteínas de Peces/química , Proteínas de Peces/farmacología , Humanos , Hidrólisis , Miofibrillas/metabolismo , Péptidos/química , Péptidos/farmacología , Hidrolisados de Proteína , PorcinosRESUMEN
Internet databases of small molecules, their enzymatic reactions, and metabolism have emerged as useful tools in food science. Database searching is also introduced as part of chemistry or enzymology courses for food technology students. Such resources support the search for information about single compounds and facilitate the introduction of secondary analyses of large datasets. Information can be retrieved from databases by searching for the compound name or structure, annotating with the help of chemical codes or drawn using molecule editing software. Data mining options may be enhanced by navigating through a network of links and cross-links between databases. Exemplary databases reviewed in this article belong to two classes: tools concerning small molecules (including general and specialized databases annotating food components) and tools annotating enzymes and metabolism. Some problems associated with database application are also discussed. Data summarized in computer databases may be used for calculation of daily intake of bioactive compounds, prediction of metabolism of food components, and their biological activity as well as for prediction of interactions between food component and drugs.
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Bases de Datos Factuales , Biología Computacional , Minería de Datos , Tecnología de Alimentos , InternetRESUMEN
Taste is one of the factors based on which the organism makes the selection of what to ingest. It also protects humans from ingesting toxic compounds and is one of the main attributes when thinking about food quality. Five basic taste sensations are recognized by humans: bitter, salty, sour, sweet, and umami. The taste of foods is affected by some molecules of some specific chemical nature. One of them are peptides derived from food proteins. Although they are not the major natural compounds originating from food sources that are responsible for the taste, they are in the area of scientific research due to the specific composition of amino acids which are well-known for their sensory properties. Literature data implicate that sweet, bitter, and umami are the tastes attributable to peptides. Moreover, the bitter peptide tastants are the dominant among the other tastes. Additionally, other biological activities like, e.g., inhibiting enzymes that regulate the body functions and acting as preventive food agents of civilization diseases, are also associated with the taste of peptides. The advance in information technologies has contributed to the elaboration of internet archives (databases) as well as in silico tools for the analysis of biological compounds. It also concerns peptides - namely taste carriers originating from foods. Thus, our paper provides a summary of knowledge about peptides as tastants with special attention paid to the following aspects: a) basis of taste perception, b) taste peptides detected in food protein sequences with special emphasis put on the role of bitter peptides, c) peptides that may enhance/suppress the taste of foods, d) databases as well as bioinformatic approaches suitable to study the taste of peptides, e) taste-taste interactions, f) basis of sensory analysis in the evaluation of the taste of molecules, including peptides, and g) the methodology applied to reduce/eliminate the undesired taste of peptides. The list of taste peptides serving some biological functions is presented in the Supplement file. The information provided includes database resources, whereas peptide sequences are given with InChiKeys, which is aimed at facilitating the Google® search. Our collection of data regarding taste peptides may be supportive for the scientists working with the set of peptide data in the context of structure-function activity of peptides.
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BACKGROUND: Salmon (Salmo salar L.) myofibryllar protein (MP) and sarcoplasmic protein (SP) were digested with human gastric and duodenal juices and hydrolysed in vitro with commercial pepsin and Corolase PP. RESULTS: The digestion after duodenal juice/Corolase PP caused almost complete breakdown of peptide bonds in MP and SP. The DPPH(â¢) scavenging activity of proteins decreased during both ex vivo digestion and in vitro hydrolysis. The highest value of DPPH(â¢) scavenging activity was shown for the gastric digest of SP (8.88 ± 0.87%). The ABTS(+â¢) scavenging activity of MP and SP increased during digestion/hydrolysis. The duodenal digest of SP was characterised by the highest value of ABTS(+â¢) scavenging activity (72.7 ± 1.2%). In turn, the highest value of ferric-reducing power was determined for the gastric digest of SP (84.8 ± 0.2%). Salmon antioxidant peptides Phe-Ile-Lys-Lys, His-Leu, Ile-Tyr, Pro-His-Leu, Pro-Trp, Val-Pro-Trp were identified in both ex vivo digested and in vitro hydrolysed MP and SP. An antioxidant peptide, Val-Tyr, was additionally detected in the in vitro hydrolysate of SP. CONCLUSION: The results indicate the salmon myofibrillar and sarcoplasmic protein fractions as potential sources of antioxidant peptides that could be released in the gastrointestinal tract but their amino acid sequence and quantification vary. © 2015 Society of Chemical Industry.
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Antioxidantes/química , Proteínas de Peces/química , Salmo salar , Animales , Simulación por Computador , Humanos , Hidrólisis , Modelos QuímicosRESUMEN
The presence of specific peptides with antioxidant properties released during carp protein ex vivo and in vitro hydrolysis by human/porcine digestive enzymes, respectively, was examined. Based on the results of the in silico data analysis, antioxidant peptides were selected for subsequent identification in the digests/hydrolysates. Carp proteins were more resistant to hydrolysis by porcine enzymes than by human digestive juices. The sarcoplasmic proteins were hydrolyzed faster than the myofibrillar ones by both human/porcine enzymes. The in vitro myofibrillar protein hydrolysate showed the highest ABTS(+) scavenging activity (â¼232.3 TEAC, µM Trolox/g), whereas the ex vivo hydrolysate of sarcoplasmic proteins showed the highest DPPH scavenging activity (â¼88µM/g) and reducing power. Five antioxidant peptides were identified in carp protein ex vivo and in vitro hydrolysates: FIKK, HL, IY, PW, VY. The peptide HL from myofibrillar proteins was identified only in the ex vivo hydrolysate, whereas the peptide PW from sarcoplasmic proteins was identified only in the in vitro hydrolysate.