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Motifs with potential physiological activity in food proteins - BIOPEP database

100%

Iwaniak A., Dziuba B.

Acta Scientiarum Polonorum. Technologia Alimentaria

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2009

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tom 08

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nr 3

59-85

Proteins are the multifunctional food components affecting the living organ-isms. One of the proteins function is the impact on the body due to the presence of motifs that show specific physiological and biological activities. Due to the worldwide growth of demand for the food containing bioactive components, increasing attention has been paid recently to the use of bioactive peptides as physiologically active food ingredients. They are important elements of the prevention and treatment of various lifestyle diseases. In addition to its primary function and according to current knowledge, each protein may be a reserve source of peptides controlling the life processes of organisms. For this reason, in this work, application of a new, additional criterion for evaluating proteins as a potential source of biologically active peptides, contributes to a more comprehensive and objective definition of their biological value. A complementary part of such research is the strategy for evaluation of the food proteins as precursors of biologically active peptides which involves the database of proteins and bioactive peptides - BIOPEP (available on-line at: http://www.uwm.edu.pl/biochemia). The database contains information on 2123 peptides representing 48 types of bioactivities, their EC50 values and source of origin. Proteins (706 sequences) are considered as bioactive peptide precursors based on newly introduced criteria: the profile of potential biological activity, the frequency of bioactive fragments occurrence and potential biological protein activity. This original and unprecedented so far approach, started to be successfully and more widely applied by other authors. BIOPEP can be interfaced with global databases such as e.g. TrEMBL, SWISS-PROT, EROP and PepBank. Recently the BIOPEP database was enlarged with the data about allergenic proteins, including information about structure of their epitopes and molecular markers

2

Physico-chemical characteristics of different genetic variants of bovine beta-casein, modified covalently by glucose, galactose and lactose

100%

Dziuba J., Darewicz M., Mioduszewska H.

Polish Journal of Food and Nutrition Sciences

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1998

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tom 07

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nr 2 Suppl.

3

Effect of non-enzymatic glycation on biological properties of morphiceptin

100%

Krawczuk S., Kostyra E., Kostyra H., Fraczek J.

Polish Journal of Food and Nutrition Sciences

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2000

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tom 09/50

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nr 1

In the course of food proteins digestion, mid-molecular weight opioid peptides are generated. Their amine groups might undergo non-enzymatic glycation with glucose which is promoted by pH and temperature. The glycation conditions of morphiceptin (pH 7.8 and temp. 37°C) used in this experiment proved that non-enzymatic glycation of the peptides could take place in the digestive tract. The results obtained herein suggest that glycation decreases the contraction amplitude of isolated rabbit duodenum by 14.1% and changes the immunogenicity of morphiceptin (Tyr-Pro- Phe-Pro-NH2), probably due to a new epitope produced.

4

Food allergy and the oral immunotherapy approach

84%

Cabrera C. M., Urra J. M.

Archivum Immunologiae et Therapiae Experimentalis

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2015

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tom 63

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nr 1

5

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The occurrence of sequences identical with epitopes from the allergen pen a 1.0102 among food and non-food proteins

84%

Minkiewicz P., Sokolowska J., Darewicz M.

Polish Journal of Food and Nutrition Sciences

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2015

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tom 65

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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.

6

Challenges and solutions in reference material development for quantification of food allergens

84%

Torok K., Bugyi Z., Hajas L., Adonyi Z., Tomoskozi S.

Polish Journal of Food and Nutrition Sciences

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2011

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tom 61

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nr Suppl.1

7

Biologically active peptides derived from food proteins

84%

Kostyra H., Kostyra E.

Polish Journal of Food and Nutrition Sciences

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1992

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tom 01

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nr 4

8

Application of the conductometric method for differentiation of proteins and peptides

84%

Mierzejewska D., Marciniak-Darmochwal K., Kostyra H., Rudnicka B.

Polish Journal of Food and Nutrition Sciences

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2007

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tom 57

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nr 1

The aim of this work was to use the conductometry method for the differentiation of the chemically- and enzymatically-modified food proteins. The protein extracts of soybean, bean pea, maize and rice seeds, 3 varieties “Tonacja”, “Nawra” and “Sukces” of wheat, as well bovine serum albumin, pepsin trypsin and acid protein hydrolyzates were investigated. Additionally, proteins were glycated by glucose. It was found that differences of the electrolytic conductivity between native proteins and their hydrolyzates were statistically significant; the electrolytic conductivity of the water protein solutions was directly proportional to the concentration of protein. It was also proved that the concentration of glucose in the protein solution modified its electrolytic conductivity. Moreover, statistically significant differences were observed between native and glycated proteins. Finally, it was stated that the electrolytic conductivity can be a tool for the differentiation of the native and modified proteins.

9

Opioid peptides derived from milk proteins

84%

Kostyra E., Sienkiewicz-Szlapka E., Jarmolowska B., Krawczuk S., Kostyra H.

Polish Journal of Food and Nutrition Sciences

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2004

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tom 13/54

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nr Spec.Issue 1

Ograniczanie wyników

Motifs with potential physiological activity in food proteins - BIOPEP database

Physico-chemical characteristics of different genetic variants of bovine beta-casein, modified covalently by glucose, galactose and lactose

Effect of non-enzymatic glycation on biological properties of morphiceptin

Food allergy and the oral immunotherapy approach

The occurrence of sequences identical with epitopes from the allergen pen a 1.0102 among food and non-food proteins

Challenges and solutions in reference material development for quantification of food allergens

Biologically active peptides derived from food proteins

Application of the conductometric method for differentiation of proteins and peptides

Opioid peptides derived from milk proteins