Anna Iwaniak

Food‐Originating ACE Inhibitors, Including Antihypertensive Peptides, as Preventive Food Components in Blood Pressure Reduction

This work is a literature overview on angiotensin-converting enzyme (ACE) inhibitory/antihypertensive peptides in food protein sources. The following aspects related to peptides with the above-mentioned bioactivity are discussed: (i) mechanism of action of ACE, (ii) the structural character of ACE inhibitors/antihypertensive peptide sequences determined by different methods, including quantitative structure-activity relationship studies, (iii) their food sources, (iv) absorption of peptides, (v) in vitro and in vivo approaches involved in the production and potential release of peptide ACE inhibitors as well as in silico methods applied in research concerning peptides.

Database of biologically active peptide sequences.

Proteins are sources of many peptides with diverse biological activity. Such peptides are considered as valuable components of foods with desired and designed biological activity. Two strategies are currently recommended for research in the area of biological activity of food protein fragments. The first strategy covers investigations on products of enzymic hydrolysis of proteins. The second one is synthesis of peptides identical with protein fragments and investigations using these peptides. It is possible to predict biological activity of protein fragments using sequence alignments between proteins and biologically active peptides from database. Our database contains currently 527 sequences of bioactive peptides with antihypertensive, opioid, immunomodulating and other activities. The sequence alignments can give information about localization of biologically active fragments in protein chain, but not about possibilities of enzymic release of such fragments. The information is thus equivalent with this obtained using synthetic peptides identical with protein fragments. Possibilities offered by the database are discussed using wheat alpha/beta-gliadin, bovine beta-lactoglobulin and bovine beta-casein (including influence of genetic polymorphism and genetic engineering on amino acid sequences) as examples.

Angiotensin I-Converting Enzyme (ACE) Inhibitory Activity and ACE Inhibitory Peptides of Salmon (Salmo salar) Protein Hydrolysates Obtained by Human and Porcine Gastrointestinal Enzymes

The objectives of the present study were two-fold: first, to detect whether salmon protein fractions possess angiotensin I-converting enzyme (ACE) inhibitory properties and whether salmon proteins can release ACE inhibitory peptides during a sequential in vitro hydrolysis (with commercial porcine enzymes) and ex vivo digestion (with human gastrointestinal enzymes). Secondly, to evaluate the ACE inhibitory activity of generated hydrolysates. A two-step ex vivo and in vitro model digestion was performed to simulate the human digestion process. Salmon proteins were degraded more efficiently by porcine enzymes than by human gastrointestinal juices and sarcoplasmic proteins were digested/hydrolyzed more easily than myofibrillar proteins. The ex vivo digested myofibrillar and sarcoplasmic duodenal samples showed IC50 values (concentration required to decrease the ACE activity by 50%) of 1.06 and 2.16 mg/mL, respectively. The in vitro hydrolyzed myofibrillar and sarcoplasmic samples showed IC50 values of 0.91 and 1.04 mg/mL, respectively. Based on the results of in silico studies, it was possible to identify 9 peptides of the ex vivo hydrolysates and 7 peptides of the in vitro hydrolysates of salmon proteins of 11 selected peptides. In both types of salmon hydrolysates, ACE-inhibitory peptides IW, IY, TVY and VW were identified. In the in vitro salmon protein hydrolysates an ACE-inhibitory peptides VPW and VY were also detected, while ACE-inhibitory peptides ALPHA, IVY and IWHHT were identified in the hydrolysates generated with ex vivo digestion. In our studies, we documented ACE inhibitory in vitro effects of salmon protein hydrolysates obtained by human and as well as porcine gastrointestinal enzymes.

BIOPEP database of sensory peptides and amino acids

Peptides and amino acids belong to compounds that influence the taste of foods. The aim of this study was to develop a database of sensory peptides and amino acids. Information about the taste of the analyzed compounds was obtained from sensory studies described in the literature. The database of sensory peptides and amino acids has identical structure to the BIOPEP database of biologically active peptides. The information about sensory peptides and amino acids was inserted into the database using standard BIOPEP layouts for bioactive peptides. Information about the biological activity of sensory peptides was obtained from BIOPEP and other databases. The information annotated in the BIOPEP database of sensory peptides and amino acids includes: sequence written in a one-letter code, information about taste, reference, structure written with the use of chemical codes (SMILES, InChI and InChIKey), bioactivity data (mainly inhibition of proteolytic enzymes), if applicable, and ID numbers from other biological and chemical databases. The database contains tools for determining the location of peptides in protein sequences (profiles of potential sensory activity), comparing protein sequences as precursors of sensory peptides based on the frequency of sensory fragments as a quantitative descriptor, simulating proteolysis and calculating novel parameters for quantitative description of simulated proteolysis. The BIOPEP database of sensory peptides and amino acids is available at http://www.uwm.edu.pl/biochemia/index.php/pl/biopep. It is an open access resource that does not require user registration.

Food protein-originating peptides as tastants - Physiological, technological, sensory, and bioinformatic approaches

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.

Common Amino Acid Subsequences in a Universal Proteome--Relevance for Food Science.

A common subsequence is a fragment of the amino acid chain that occurs in more than one protein. Common subsequences may be an object of interest for food scientists as biologically active peptides, epitopes, and/or protein markers that are used in comparative proteomics. An individual bioactive fragment, in particular the shortest fragment containing two or three amino acid residues, may occur in many protein sequences. An individual linear epitope may also be present in multiple sequences of precursor proteins. Although recent recommendations for prediction of allergenicity and cross-reactivity include not only sequence identity, but also similarities in secondary and tertiary structures surrounding the common fragment, local sequence identity may be used to screen protein sequence databases for potential allergens in silico. The main weakness of the screening process is that it overlooks allergens and cross-reactivity cases without identical fragments corresponding to linear epitopes. A single peptide may also serve as a marker of a group of allergens that belong to the same family and, possibly, reveal cross-reactivity. This review article discusses the benefits for food scientists that follow from the common subsequences concept.

Internet Databases of the Properties, Enzymatic Reactions, and Metabolism of Small Molecules—Search Options and Applications in Food Science

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.

Peptides Derived from Foods as Supportive Diet Components in the Prevention of Metabolic Syndrome: Peptides compared with metabolic syndrome diseases…

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.

Databases and Associated Bioinformatic Tools in Studies of Food Allergens, Epitopes and Haptens – a Review

Abstract Allergies and/or food intolerances are a growing problem of the modern world. Diffi culties associated with the correct diagnosis of food allergies result in the need to classify the factors causing allergies and allergens themselves. Therefore, internet databases and other bioinformatic tools play a special role in deepening knowledge of biologically-important compounds. Internet repositories, as a source of information on different chemical compounds, including those related to allergy and intolerance, are increasingly being used by scientists. Bioinformatic methods play a signifi cant role in biological and medical sciences, and their importance in food science is increasing. This study aimed at presenting selected databases and tools of bioinformatic analysis useful in research on food allergies, allergens (11 databases), epitopes (7 databases), and haptens (2 databases). It also presents examples of the application of computer methods in studies related to allergies.

Structural characteristics of food protein-originating di- and tripeptides using principal component analysis

This paper presents the use of principal component analysis (PCA) to study the effect of specific physicochemical attributes on bitterness of di- and tripeptides originating from food proteins. Peptide sequences were derived from the BIOPEP-UWM database of sensory peptides and amino acids. Descriptors defining the physicochemical properties of amino acids forming the analyzed peptides were study variables. They were derived from ProtScale program and Biological Magnetic Resonance Data Bank. Finally, PCA was carried out for 51 dipeptides/12 variables, and 51 tripeptides/18 variables using STATISTICA®13.1 software. PCA allowed reducing the input datasets to 4 principal components (PCs) for dipeptides and to 5 PCs for tripeptides. The impact of the following properties on the bitterness of peptides was observed: relatively high molecular weight, bulkiness, increasing number of carbon and hydrogen atoms of amino acids forming the sequences. These properties characterized the N- (negative correlations) and C-terminal residue (positive correlations) of both di- and tripeptides. An additional property affecting peptide bitterness was amino acids’ hydrophobicity. Our results were consistent with scientific reports on structure–bitterness of peptides. Thus, we find PCA a chemometric approach helpful in broadening the knowledge about the function of peptides resulting from their chemical nature.