Publications

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    ABSTRACT: In the digestive tract in humans, bioactive peptides, i.e. protein fragments impacting the physiological activity of the body, may be released during the digestion of food proteins, including those of fish. The aim of the study was to establish the method of human ex vivo digestion of carp muscle tissue and evaluate the angiotensin I-converting enzyme inhibitory and antioxidant activities of hydrolysates obtained after digestion. It was found that the hydrolysates of carp muscle tissue obtained with the three-stage method of simulated ex vivo digestion showed ACE inhibitory as well as antioxidative activities. It was demonstrated that the degree of hydrolysis depended on the duration of individual stages and the degree of comminution of the examined material. Although the applied gastric juices initiated the process of hydrolysis of carp muscle tissue, the duodenal juices caused a rapid increase in the amount of hydrolysed polypeptide bonds. The antihypertensive and antioxidative activities of the hydrolysates of carp muscle tissue increased together with progressive protein degradation. However, the high degree of protein hydrolysis does not favour an increase in the activity of free radical scavenging. The presented results are an example of the first preliminary screening of the potential health-promoting biological activity of carp muscle tissue in an ex vivo study.
    Food & Function 01/2015; 6(1):211-218. DOI:10.1039/C4FO00621F · 2.91 Impact Factor
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    ABSTRACT: The presence of common epitopes among tropomyosins of invertebrates, including arthropods e.g. edible ones, may help to explain the molecular basis of cross-reactivity between allergens. The work presented is the first survey concerning global distribution of epitopes from Pen a 1.0102 in universal proteome. In the group of known tropomyosin epitopes, the fragment with the sequence ESKIVELEEEL was found in the sequence of channel catfish (Ictalurus punctatus) tropomyosin. To date, this is the first result suggesting the presence of a complete sequential epitope interacting with IgE in vertebrate tropomyosin. Another fragment with the sequence VAALNRRIQL, a major part of the epitope, was found in 11 fish, 8 amphibians, 3 birds, 19 mammalians and 4 human tropomyosin sequences. Identical epitopes are common in sequences of invertebrate tropomyosins, including food and non-food allergens annotated in the Allergome database. The rare pentapeptide with the DEERM sequence occurs in proteins not sharing homology with tropomyosins. Pathogenic microorganisms are the most abundant category of organisms synthesizing such proteins.
    Polish Journal of Food and Nutrition Sciences 01/2015; 65(1):21-29. DOI:10.1515/pjfns-2015-0002
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    ABSTRACT: Supplement to the publication: The occurrence of sequences identical with epitopes from the allergen Pen a 1.0102 among food and non-food proteins. Piotr Minkiewicz, Jolanta Sokołowska, Małgorzata Darewicz Polish Journal of Food and Nutrition Sciences, 2015, vol. 65, issue 1 DOI: 10.1515/pjfns-2015-0002 List of proteins containing fragments identical with linear epitopes of tropomyosin from Shrimp Farfantepenaeus aztecus (allergen Pen a 1.0102). Journal website: http://journal.pan.olsztyn.pl Article address: http://journal.pan.olsztyn.pl/show.php?id=1410
  • Piotr Minkiewicz, Anna Iwaniak, Małgorzata Darewicz
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    ABSTRACT: Internet databases serve as an important source of information on chemical compounds that students can readily investigate, including those studying food science and food technology. This Activity provides a brief introduction to the application of chemical information resources with a focus on conducting structure-based searches.
    Journal of chemical education 01/2015; DOI:10.1021/ed5006739 · 1.00 Impact Factor
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    ABSTRACT: http://www.mdpi.com/1422-0067/15/8/14077 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.
    International Journal of Molecular Sciences 08/2014; 15(8-8):14077-14101. DOI:10.3390/ijms150814077 · 2.34 Impact Factor
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    ABSTRACT: Białka żywności są źródłem peptydów o różnych aktywnościach biologicznych. Mogą m. in. oddziaływać na funkcjonowanie układu krążenia. Do tej grupy biopeptydów można zaliczyć peptydy obniżające ciśnienie krwi (inhibitory enzymu konwertującego angiotensynę - ACE), przeciwkrzepliwe oraz redukujące poziom cholesterolu. Spośród peptydów o wymienionych aktywnościach biologicznych najwięcej z nich pełni funkcję inhibitorów ACE. Niektóre peptydy redukujące ciśnienie krwi stanowią składniki żywności funkcjonalnej oraz nutraceutyków i uzyskały status żywności specjalnego przeznaczenia. Źródłem peptydów przeciwkrzepliwych są głównie białka mleka natomiast obniżających poziom cholesterolu białka soi, ale naukowcy podejmują prace nad poszukiwaniem nowych alternatywnych źródeł peptydów o wymienionych aktywnościach. Należy pamiętać, że chociaż peptydy bioaktywne pochodzące z białek żywności są uznawane za bezpieczne składniki żywności i mogą wspomagać terapię chorób układu krążenia, niemniej nie mogą być traktowane jako zamienniki leków. Niniejszy przegląd przedstawia charakterystykę wybranych peptydów obniżających ciśnienie krwi, poziom cholesterolu oraz peptydów przeciwkrzepliwych, zidentyfikowanych w białkach żywności i badanych z udziałem ludzi lub zwierząt.
    Polski merkuriusz lekarski: organ Polskiego Towarzystwa Lekarskiego 06/2014; 216:403-406.
  • Anna Iwaniak, Małgorzata Darewicz, Piotr Minkiewicz
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    ABSTRACT: Nadciśnienie tętnicze jest chorobą cywilizacyjną występującą u pacjentów na całym świecie, szczególnie w krajach o wysokim poziomie rozwoju gospodarczego. Wpływ na występowanie tej choroby ma wiele czynników, takich jak m. in.: wiek pacjenta, predyspozycje genetyczne, styl życia, masa ciała. Dwa ostatnie związane są dietą. Składnikami żywności, które wykazują zdolność obniżania ciśnienia krwi są znajdujące się w sekwencjach białek inhibitory enzymu konwertującego angiotensynę (inhibitory ACE). Niektóre z nich są dostępne na rynku w formie produktów żywnościowych, składników żywności lub suplementów. W pracy scharakteryzowano wybrane inhibitory ACE pochodzące z żywności, których efekt przeciwnadciśnieniowy potwierdzono w badaniach na zwierzętach i/lub ludziach oraz porównano takie peptydy z lekami pełniącymi funkcję inhibitora ACE.
    Lekarz wojskowy 06/2014; 92(1):89-95.
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    Małgorzata Darewicz, Anna Iwaniak, Piotr Minkiewicz
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    ABSTRACT: Milk proteins possess a wide range of nutritional and biological properties. They are used as a source of energy, amino acids, vitamins, and minerals which are needed for the growth and development of organisms. Milk proteins contain physiologically active peptides encrypted in the protein sequences. Peptides with biological activity are produced during gastrointestinal digestion or food processing and could play an important role in metabolic regulation and modulation. This suggests the potential use of biopeptides as nutraceuticals and ingredients of functional foods to promote health and reduce the risk of diseases. Milk-derived bioactive peptides were shown to have antihypertensive, antihrombotic, antimicrobial, antioxidative, opioid, mineral-binding properties and anticancer activities. In vitro and in vivo studies are currently being carried out to identify milk bioactive peptides as well as to study their bioavailability and molecular mechanisms of action. Milk as a traditional food product can serve as the example of a functional food and be relevant for health-promoting as well as health-preventing factors. Entire text is in Polish.
    Medycyna weterynaryjna 06/2014; 70(6):348-352. · 0.20 Impact Factor
  • Anna Iwaniak, Piotr Minkiewicz, Małgorzata Darewicz
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    ABSTRACT: 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.
    Comprehensive Reviews in Food Science and Food Safety 02/2014; 13(2):114-134. DOI:10.1111/1541-4337.12051 · 3.54 Impact Factor
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    ABSTRACT: Według aktualnych poglądów każde białko, oprócz swej podstawowej funkcji, może pełnić rolę prekursora biologicznie aktywnych peptydów. Bioaktywne motywy w łańcuchach białek są definiowane jako te fragmenty, które pozostają nieaktywne w sekwencjach swoich prekursorów, natomiast po uwolnieniu przez enzymy proteolityczne mogą oddziaływać z odpowiednimi receptorami oraz regulować funkcje fizjologiczne organizmu. Peptydy pochodzące z białek żywności mogą wpływać na obniżenie ciśnienia krwi, stymulować działanie układu odpornościowego, hamować proces agregacji płytek krwi oraz procesy utleniania, wykazywać aktywność opioidową, wykazywać aktywność opioidową, antybakteryjną, powierzchniową, wiązać jony metali, kształtować właściwości sensoryczne. Bioaktywne peptydy polecane są jako składniki tzw. żywności funkcjonalnej. Na świecie obserwuje się wzrost zainteresowania tego typu żywnością. W artykule przedstawione przykłady dostępnych komercyjnie produktów zawierających bioaktywne peptydy.
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    ABSTRACT: Bioinformatics and cheminformatics tools such as databases play an increasingly important role in modern science. They are commonly used in biological and medical sciences and they have many applications in food science. Databases listing biologically-active compounds contribute to the design of functional foods and nutraceuticals. Databases of toxic or allergenic compounds are useful for food safety evaluations. This review presents examples of freely available databases (without obligatory registration) listing major groups of bioactive components. The main categories of compounds annotated in online databases include: nucleic acids, proteins, peptides, carbohydrates, lipids, and low-molecular weight compounds. Other categories of database entries are also discussed, including enzymes, allergens and their epitopes, flavor-enhancing compounds as well as toxic substances. The last section of the review focuses on metabases, which are websites that create access to multiple databases.
    Food Reviews International 10/2013; 29(4):321-351. DOI:10.1080/87559129.2013.818011 · 2.54 Impact Factor
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    Małgorzata Darewicz, Anna Iwaniak, Piotr Minkiewicz
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    ABSTRACT: MetaComBio (Meta Compound Bioactivity) is a website containing links to chemical databases describing carbohydrates, flavor and aroma enhancing compounds, haptens, lipids, toxic compounds and other substances important for food quality and safety. MetaComBio provides links to freely available resources.
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    Marta Dziuba, Piotr Minkiewicz, Marianna Dąbek
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    ABSTRACT: The objective of this study was to analyse allergenic proteins by identifying their molecular biomarkers for detection in food using bioinformatics tools. The protein and epitope sequences were from BIOPEP database, proteolysis was simulated using BIOPEP program and UniProt database screening via BLAST and FASTA programs. The biomarkers of food proteins were proposed: for example for whey proteins - TPEVDDEALEKFDKALKALPMHIR (β-Lg: fragment 141-164), chicken egg - AAVSVDCSEYPKPDCTAEDRPL (ovomucoid: 156-177), wheat - KCNGTVEQVESIVNTLNAGQIASTDVVEVVVSPPY (triose phosphate isomerase: 12-46) and peanuts - QARQLKNNNPFKFFVPPFQQSPRAVA (arachin: 505-530). The results are annotated in the BIOPEP database of allergenic proteins and epitopes, available at http://www.uwm.edu.pl/biochemia. The epitope-receptor interactions are attributed to the epitope's sequence and suggest that in silico proteolysis products showing the highest degree of sequence identity with an epitope or its part are characteristic of a given protein or a group of cross-reactive homologs. The protein markers from basic food groups were proposed based on the above assumption.
    01/2013; 12(1):101-11.
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    ABSTRACT: The aim of this study was to analyze the distribution of hexapeptide fragments considered as epitopes of Baltic cod parvalbumin beta (allergen Gad c 1) in the universal proteome. Cod (Gadus morhua subsp. callarias) parvalbumin hexapeptides cataloged in the Immune Epitope Database were used as query sequences. The UniProt database was screened using the WU-BLAST 2 program. The distribution of hexapeptide fragments was investigated in various protein families, classified according to the presence of the appropriate domains, and in proteins of plant, animal and microbial species. Hexapeptides from cod parvalbumin were found in the proteins of plants and animals which are food sources, microorganisms with various applications in food technology and biotechnology, microorganisms which are human symbionts and commensals as well as human pathogens. In the last case possible coverage between epitopes from pathogens and allergens should be avoided during vaccine design.
    Peptides 08/2012; 38(1):105-109. DOI:10.1016/j.peptides.2012.08.011 · 2.61 Impact Factor
  • Food proteins and peptides: chemistry, functionality, and commercialization, 1st edited by Navam Hettiarachchy, 01/2012: chapter 13: pages 317-359; CRC Press, Taylor and Francis Group., ISBN: 978-1-4200-9341-4
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    ABSTRACT: The aim of the study was to evaluate the possibility of predicting potential epitope sequences and location in allergenic proteins from food using EVALLER program by comparison with experimental epitopes summarised in the BIOPEP database of allergenic proteins. Sequences of experimental epitopes from food allergens, present in the BIOPEP database of allergenic proteins were used in the study. Sequences of potential epitopes were found using EVALLER program. The Positive Predictive Value (PPV) has been used as a measure of prediction quality. The potential epitopes fully or partially overlapping with the experimental ones were considered as true positive results whereas these unrelated to the experimental ones as false positive results. The PPV for entire dataset containing 310 potential epitopes was 80.6%. The PPV varied signifi cantly among particular allergen families defined according to the AllFam database. Caseins revealed PPV=100% (with one exception), proteins from tropomyosin family and proteins from papain-like cystein protease family – exceeding 50%. The last two families possess also relatively low frequency of epitope occurrence. The predictive potential was poor (less than 50%) for plant allergens from cupin superfamily. Families such as lipocalins from milk and EF-hand family (parvalbumins) revealed high variability within family. The EVALLER program may be used as a tool for the prediction of epitope location although its potential varies considerably among allergen families. High PPV is associated with a high number of known experimental epitopes (such as in caseins) and/or a high degree of sequence conservation within family (caseins, tropomyosins).
    Polish Journal of Food and Nutrition Sciences 01/2012; 62(3):151-157. DOI:10.2478/v10222-011-0036-2
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    ABSTRACT: Celem niniejszej pracy było opracowanie metody identyfikacji frakcji niskocząsteczkowych produktów hydrolizy bydlęcej kazeiny-beta przez plazminę za pomocą wysokosprawnej chromatografii cieczowej z odwróconymi fazami (RP-HPLC) w połączeniu ze spektroskopią w nadfiolecie (UV). Bydlęcą kazeinę-beta poddano hydrolizie przez plazminę. Supernatant pozostały po wytrąceniu nierozpuszczalnej frakcji hydrolizatu rozdzielono za pomocą ultrafiltracji na retentat zawierający polipeptydy i permeat zawierający peptydy o małej masie cząsteczkowej. Do identyfikacji frakcji permeatu wykorzystano parametry charakteryzujące ilościowo drugie i czwarte pochodne widm UV. Kształt pochodnych widm permeatu wskazywał na obecność niewielkich ilości tryptofanu, który nie został wykryty metodą spektrometrii mas. Wartości parametrów charakteryzujących pochodne widm UV niskocząsteczkowej frakcji hydrolizatu kazeiny-beta różnią się w sposób istotny statystycznie (w granicach od p < 0,05 do p < 0,001) od analogicznych parametrów dla pochodnych widm pozostałych frakcji tego hydrolizatu oraz od pochodnych widm białka niepoddanego hydrolizie. Niskocząsteczkowa frakcja hydrolizatu kazeiny-beta może być identyfikowana metodą spektroskopii UV.
    Zywnosc: Nauka, Technologia, Jakosc 01/2012; · 0.31 Impact Factor
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    ABSTRACT: This study presents and analyzes the results of in silico, in vitro, and in vivo tests investigating the potential preventive properties of a group of biologically active milk and colostrum proteins and peptides; that is, casein, α-lactalbumin, β-lactoglobulin, lysozyme, lactoferrin, glycomacropeptide, proline-rich peptides, and lactoperoxidase. Casein or its peptides lowers blood pressure, reduces tumor growth, and shows anticoagulant, antimicrobial, and antioxidant activity. Casein hydrolysates decrease the probability of diabetes. α-Lactalbumin and β-lactoglobulin manifest antiviral activity directed against HIV and antibacterial and hypotensive activities. A diet rich in α-lactalbumin has antistress, antidepressive, and anticarcinogenic properties. Lysozyme is used as a supplement in infant formulas and an anti-inflammatory and analgesic agent in neoplastic diseases. Lactoferrin demonstrates an antibacterial, antiviral, fungistatic, antiparasitic, and antithrombotic effect. Glycomacropeptide is characterized by antibacterial, antiviral, and antithrombotic properties. Colostrinin, a proline-rich peptide, is applied in the treatment of neurodegenerative diseases of the brain and autoimmune diseases. Lactoperoxidase is an antimicrobial agent. Studies indicate that milk and colostrum proteins and peptides have many applications in the prevention and treatment of various diseases in patients from all age groups.
    Food Reviews International 10/2011; 27(4):357-388. DOI:10.1080/87559129.2011.563396 · 2.54 Impact Factor
  • P Minkiewicz, J Dziuba, J Michalska
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    ABSTRACT: The aim of the present study was to perform an in silico evaluation of bovine meat proteins as potential precursors of biologically active peptides, as well as to determine whether such peptides can be released by selected proteolytic enzymes. The sequences of 19 bovine meat proteins were processed using the BIOPEP database and program. The profiles of potential biological activity of protein fragments were determined and the following parameters were calculated: the frequency of occurrence of fragments with given activity (A), the frequency of release of fragments with given activity by selected enzymes (A(E)), and the relative frequency of release of fragments with given activity by selected enzymes (W). Among the examined proteins, collagen and elastin appear to be the richest potential source of bioactive peptides, in particular of angiotensin-converting enzyme inhibitors, antithrombotic fragments, inhibitors of dipeptidyl peptidase IV and peptides regulating gastric mucosal activity. The high number of bioactive fragments in collagen and elastin is associated with a high content of glycine and proline, amino acids that are most abundant in biologically active fragments. Of the two investigated proteolytic enzymes, Proteinase K - an enzyme with broad specificity (e.g., against peptide bonds formed by the carboxyl groups of proline) can release considerably more biologically active fragments than Proteinase P1 - an enzyme with narrow specificity, not including proline residues.
    Food Science and Technology International 02/2011; 17(1):39-45. DOI:10.1177/1082013210368461 · 0.98 Impact Factor

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