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1

Wykorzystanie metod wysokosprawnej chromatografii cieczowej, spektroskopii w nadfiolecie oraz spektroskopii mas w badaniach mechanizmu indukowanych cieplnie oddzialywan laktoglobuliny-beta, laktoglobuliny-alfa i kazeiny-kappa

100%
Minkiewicz P.
Rozprawy i Monografie. Uniwersytet Warmińsko-Mazurski w Olsztynie
|
2004
|
tom 95
1-73
2

Charakterystyka produktow proteolizy kazeiny przez chymozyne rozdzielonych za pomoca wysokosprawnej chromatografii cieczowej

100%
Minkiewicz P.
Rozprawy i Monografie. Uniwersytet Warmińsko-Mazurski w Olsztynie
|
2000
|
tom 29
1-69
3

Biokataliza za pomocą immobilizowanych (unieruchomionych) komórek

63%
Minkiewicz P., Kostyra H.
Przemysł Spożywczy
|
1988
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tom 42
|
nr 12
4

Koagulacja mleka za pomocą immobilizowanych enzymów

63%
Minkiewicz P., Kostyra H.
Przegląd Mleczarski
|
1989
|
nr 06
5

Wplyw reszt kwasu N-acetyloneuraminowego na strukture i niektore wlasciwosci kazeiny

63%
Dziuba J., Minkiewicz P.
Biotechnologia
|
1992
|
nr 3
21-29
6
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Biologically active peptides derived from proteins - a review

63%
Iwaniak A., Minkiewicz P.
Polish Journal of Food and Nutrition Sciences
|
2008
|
tom 58
|
nr 3
Proteins play an important role in body functioning. They can also be a good source of peptides with different activities. Such peptides are defined as biologically active (bioactive peptides). Bioactive peptides interact with proper body receptors and such an effect can be beneficial or not. Biopeptides as components of food with desired features have become an interesting issue for scientific research. Many of bioactive peptides are found in milk and dairy products, plant, animal and microbial proteins. They function mainly as inhibitors of the angiotensin converting enzyme but there is a plenty of peptides derived from other sources that can even prevent chronic diseases. This paper focuses on peptides derived from different sources and their physiological role in the body as well as functional aspects of their application in food production. In this article we concentrate on the peptides exerting the following activities: affecting blood pressure, prolyl endopeptidase inhibitors, coeliac toxic, immunomodulating and opioid.
7

Proteins as the source of physiologically and functionally active peptides

63%
Iwaniak A., Minkiewicz P.
Acta Scientiarum Polonorum. Technologia Alimentaria
|
2007
|
tom 06
|
nr 3
The market of functional foods and beverages develops dynamically. Biological activities of many food components which occur naturally become an issue of many scientific and industrial interests. The structural and chemical changes occurring during the proteins processing lead to the release of bioactive peptides. Their multifunctional activity is based on their structure and other factors including e.g. hydrophobicity, charge, or microelements binding properties. This article focuses on peptides with other physiological and functional activities such as antithromobotic, antioxidative, antibacterial and antifungal, sensory, and improving those nutritional value of food.
8
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Application of ultraviolet spectroscopy to discriminate wheat alpha-beta- and gamma-gliadins separated with high-performance liquid chromatography - a short report

51%
Dziuba J., Nalecz D., Minkiewicz P., Hanasiewicz A.
Polish Journal of Food and Nutrition Sciences
|
2007
|
tom 57
|
nr 2
191-193
Studies were carried out to identify and detect potentially toxic proteins of wheat. The gliadin fractions were subjected to chromatographic and spectroscopic analyses to develop the relevant discriminants. The spectral analysis showed that these proteins differ considerably in their tryptophan-to-tyrosine molar ratios. A standard curve was used. The gliadin fractions were identified by comparing the calculated values of the tryptophan-to-tyrosine molar ratio with the values obtained based on the amino acid sequence of wheat gliadins in the Swiss-Prot/TrEMBL database. Based on the retention times and second derivatives of UV spectra, the particular wheat gliadin fractions were classified as α/β or γ-gliadins.
9
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The occurrence of sequences identical with epitopes from the allergen pen a 1.0102 among food and non-food proteins

51%
Minkiewicz P., Sokolowska J., Darewicz M.
Polish Journal of Food and Nutrition Sciences
|
2015
|
tom 65
|
nr 1
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 fi rst 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 fi rst 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 fi sh, 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.
10

Metoda wykrywania zafalszowan preparatow i produktow sojowych bialkami mleka

51%
Dziuba J., Nalecz D., Minkiewicz P.
Przegląd Mleczarski
|
2001
|
nr 08
335-337
11
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Databases and associated bioinformatic tools in studies of food allergens, epitopes and haptens - a review

51%
Bucholska J., Minkiewicz P., Darewicz M., Iwaniak A.
Polish Journal of Food and Nutrition Sciences
|
2018
|
tom 68
|
nr 2
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.
12

The influence of micelle size on selected functional properties of casein

51%
Dziuba J., Zbikowska A., Minkiewicz P.
Applied Biology Communications. Lublin Scientific Center
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1991
|
tom 01
|
nr 6
13

Chromatograficzna charakterystyka frakcji peptydowych fermentowanych produktów mleczarskich

51%
Minkiewicz P., Dziuba J., Czaplinski M.
Biuletyn Naukowy. Uniwersytet Warmińsko-Mazurski w Olsztynie
|
2003
|
nr 22
14

Determination of theoretical retention times for peptides analyzed by reversed-phase high-performance liquid chromatography

51%
Dziuba J., Minkiewicz P., Mogut D.
Acta Scientiarum Polonorum. Technologia Alimentaria
|
2011
|
tom 10
|
nr 2
Background. Peptides are important components of foods mainly due to their biological activity. The basic method of their identification is reversed phase high-performance liquid chromatography coupled with electrospray-ionization mass spectrometry (RP-HPLC- -ESI-MS). Retention time (tR) prediction in silico is very helpful in analysis of multicomponent peptide mixtures. One of problems associated with RP-HPLC-ESI-MS is deterioration of mass spectra quality by trifluoroacetic acid (TFA). This problem can be avoided through the use of chromatographic columns designed for work with low TFA concentrations in mobile phase. The objective of this study was to determine the correlations between peptide retention times predicted with the use of a program available on-line and experimental retention times obtained using the column working with low TFA concentrations. Material and methods. The set of synthetic peptides and bovine α-lactalbumin fragments (18 peptides) was used in the experiment. Theoretical retention times were calculated using Sequence Specific Retention Calculator (SSRC) program. The experimental retention times were measured via RP-HPLC-ESI-MS method using column working with low TFA content. The dependence between theoretical and experimental tR was expressed via empirical equations. Results. The best correlation between theoretical and experimental retention times of peptides containing at least four amino acid residues has been obtained when third order polynomial (R2 = 0.9536). Prediction quality for diand tripeptides was significantly lower. The method described can be applied for cysteine-containing peptides although our sample preparation procedure did not include modification of this amino acid, taken into attention by SSRC program. Conclusions. The results of this study validate the usefulness of a third degree polynomial as a simple function describing the correlation between peptide retention times predicted by an on-line application and experimental retention times. The above function can effectively predict retention times in situations when experimental conditions differ from the computational environment (various columns, mobile phase composition, use or resignation from chemical modifications during sample preparation, various HPLC equipments). On-line available tR predicting application with correction based on user’s own data may be a useful tool in food peptidomics.
15

Biologicznie aktywne peptydy pochodzące z białek mleka

51%
Darewicz M., Iwaniak A., Minkiewicz P.
Medycyna Weterynaryjna
|
2014
|
tom 70
|
nr 06
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.
16

Biologically active peptides from plant and animal proteins

51%
Dziuba J., Minkiewicz P., Nalecz D.
Polish Journal of Food and Nutrition Sciences
|
1999
|
tom 08
|
nr 1
3-16
Products of proteolysis of food proteins may play a role of agents regulating different functions in the human organism. The peptides derived from plant-, meat- and egg proteins may decrease the blood pressure, act as opioid agonists and antagonists, cause contraction of smooth muscles, inhibit platelet aggregation and oxidation. The coeliac-toxic peptides are an example of peptides with a negative influence on the human organism. The activity of food-originated peptides has mainly been investigated in vitro. Information published so far refers to biologically active peptides obtained in laboratory scale. Their application as components of so called "functional foods" (specially designed foods with desired biological activity) can however be expected possible.
17
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Update of the list of allergenic proteins from milk, based on local amino acid sequence identity with known epitopes from bovine milk proteins - a short report

51%
Minkiewicz P., Dziuba J., Gladkowska-Balewicz I.
Polish Journal of Food and Nutrition Sciences
|
2011
|
tom 61
|
nr 2
The study involved the screening of protein sequence database nrdb 95 for sequences containing fragments identical with experimentally proven sequential epitopes of bovine milk proteins. Such fragments were found in proteins from milk of the buffalo (Bubalus bubalis), yak (Bos grunniens), goat (Capra hircus) and ewe (Ovis aries). Some proteins, such as α-lactalbumins (from the yak, buffalo and goat) and κ-caseins (from the goat and ewe), have not been previously considered as allergens. They were entered into a new database of allergenic proteins from foods and their epitopes, which is part of the BIOPEP database http://www.uwm.edu.pl/biochemia. The proteins containing fragments identical with linear epitopes from known allergens should also be classified as allergens, based on local sequence identity. The absence of common linear epitopes with known allergens cannot be treated as the evidence that a given protein is not allergenic.
18
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Zastosowanie drugich i czwartych pochodnych widm UV do identyfikacji niskocząsteczkowej frakcji produktów hydrolizy kazeiny-beta przez plazminę

51%
Darewicz M., Minkiewicz P., Dziuba M., Panfil T.
Żywność Nauka Technologia Jakość
|
2012
|
tom 19
|
nr 4
Celem niniejszej pracy było opracowanie metody identyfikacji frakcji niskocząsteczkowych produktów hydrolizy bydlęcej kazeiny-β przez plazminę za pomocą wysokosprawnej chromatografii cieczowej z odwróconymi fazami (RP-HPLC) w połączeniu ze spektroskopią w nadfiolecie (UV). Bydlęcą kazeinę-β 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-β 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 nie poddanego hydrolizie. Niskocząsteczkowa frakcja hydrolizatu kazeiny-β może być identyfikowana metodą spektroskopii UV.
19
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Nadwrażliwość pokarmowa białek ryb

51%
Bucholska J., Darewicz M., Minkiewicz P., Starowicz P.
Zeszyty Problemowe Postępów Nauk Rolniczych
|
2015
|
tom 583
Niepożądane reakcje organizmu człowieka związane ze spożyciem żywności to nietolerancje pokarmowe lub alergie. Immunologiczna odpowiedź organizmu na składniki żywności jest wywoływana przez wiele czynników. Alergia objawia się w postaci wielu niespecyficznych reakcji. Epitopy białek, odpowiadające za oddziaływania z przeciwciałami dzielimy na liniowe (ciągłe fragmenty łańcucha białkowego) i konformacyjne (reszty aminokwasowe sąsiadujące w wyniku tworzenia struktury drugo- i trzeciorzędowej). Białka posiadające epitopy o podobnej budowie mogą wykazywać reakcje krzyżowe. Wśród alergii pokarmowych ważne miejsce zajmuje immunologiczna nadwrażliwość pokarmowa na białka ryb. Stabilność termiczna białek ryb powoduje, że zachowują one właściwości alergenne pomimo stosowanych procesów technologicznych. Molekularne aspekty identyfikacji i charakterystyki alergenów pokarmowych, w tym alergenów ryb, są podstawą ich wykorzystania w praktyce klinicznej. W niniejszej pracy scharakteryzowano immunologiczną nadwrażliwość pokarmową na przykładzie białek ryb, molekularne aspekty alergennych białek ryb oraz wybrane metody ich identyfikacji.
20
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Plant seed storage proteins as potential precursors of bioactive peptides

51%
Dziuba J., Minkiewicz P., Puszka K., Dabrowski S.
Polish Journal of Food and Nutrition Sciences
|
1995
|
tom 04
|
nr 3
31-42
Amino acid sequences of proteins taken from the SWISS-PROT database were analysed using the computer programme PROTEIN searching for fragments identical to bioactive peptides in chains of plant seed protein and localizing bonds susceptible to enzymatic proteolysis. Sequences of proteins from barley (Hordeum vulgare), rice (Oryzae sativa), sorghum (Sorghum bicolor milo), oat (Avena sativa), soybean (Glycine max), pumpkin (Cucurbita maxima), sunflower (Helianthus annuus) and vetch (Vicia pannonica) were analysed. Fragments with potential antihypertensive activity were present in proteins of all these plants with the exception of vetch. Fragments with potential immunomodulating (pumpkin and sunflower) and antithrombotic (vetch) activity were also found. Proteolytic enzymes may liberate bioactive peptides from plant proteins. Inmost cases the action of two enzymes is necessary. The need occurs especially in the case of protein hydrolysis by prolyl endopeptidases ( EC 3.4.21.26) or alkaline proteinase from Tritirachium called proteinase K (EC 3.4.21.14) and intracellular proteinase from Streptococcus thermophilus (EC 3.4.24.4). Proteolytic enzymes of the digestive tract, such as chymotrypsin (EC 3.4.21.1), trypsin (EC 3.4.21.4), elastase (EC 3.4.21.36) or pepsin (EC 3.4.23.4) can also take part in the liberation of some active fragments.
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