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Research Interests: Chemistry, Food Science, Antioxidant, Applied Sciences, DPPH, and 3 moreBrine, Fractionation, and ABTS
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Research Interests: Chemistry, Food Science, Antioxidant, Casein, Cheese Ripening, and 3 moreABTS, In Silico, and Ripening
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Abstract Since the definition of bioactive peptides has been firstly published, the knowledge about these molecules is still being improved. It stems from the progress in research methods development including, e.g., the achievements of... more
Abstract Since the definition of bioactive peptides has been firstly published, the knowledge about these molecules is still being improved. It stems from the progress in research methods development including, e.g., the achievements of the bio- and cheminformatics. Hence, other protocols are used to analyze biopeptides apart from the classical (experimental) approach, namely in silico (i.e., bioinformatic) and hybrid (integrated) ones. This review presents the role of in silico methodologies used in studying peptides derived from foods. The attention is paid to databases as sources of information on peptides and the contribution of in silico procedures used for peptide analyses, including their advantages and disadvantages. Although the hybrid strategy of research seems to mutually complement in silico and experimental approaches, there are some problems requiring to be resolved for better understanding the biopeptides’ nature. These problems include: the stability of peptides, safety, bioavailability, bitterness, toxicity, water solubility, and food matrix interactions.
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The temperature has a significant effect on cathepsin activity, but the effect of temperature on the ripening of marinades, and the formation of protein hydrolysis products, is less studied than other technological factors. The results of... more
The temperature has a significant effect on cathepsin activity, but the effect of temperature on the ripening of marinades, and the formation of protein hydrolysis products, is less studied than other technological factors. The results of this study showed that herring marinated at 2 °C showed a higher mass yield, but lower non-protein nitrogen (NPN), peptides, and free amino acid fraction content, than after marinating at 7 and 12 °C. The higher temperature increased the free amino acid content the most, and decreased the hardness, as measured via sensory assessment, of the marinated meat. This was confirmed by the hardness measurement in the texture profile analysis. The highest activity of cathepsins D and B in the meat was found at 7 °C, while cathepsin L was found at 2 °C. Increasing the temperature by 10 °C increased the diffusion/loss of nitrogenous substances from the meat to the brine by 36%. The meat and brine showed high antioxidant activity, which depended on the marinat...
Research Interests: Chemistry, Food Science, Antioxidant, Applied Sciences, DPPH, and 3 moreBrine, Fractionation, and ABTS
Abstract: 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... more
Abstract: 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 samp...
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For many years, proteins and peptides have been attracting scientists’ attention as two of the most important classes of food components [...]
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Abstract: 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... more
Abstract: 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 l...
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Research Interests: Materials Engineering, Biochemistry, Chemistry, Proteins, Peptide, and 3 moreCasein, Polimery, and Prolamin
At present two-dimensional polyacrylamide gel electrophoresis (2-DE) is the most widely used proteomic tool, which enables simultaneous separation of even thousands of proteins with a high degree of resolution. The quality of 2-DE... more
At present two-dimensional polyacrylamide gel electrophoresis (2-DE) is the most widely used proteomic tool, which enables simultaneous separation of even thousands of proteins with a high degree of resolution. The quality of 2-DE separation depends on the type of biological material used as a protein source. The presence of interfering compounds (e.g., phenols, as it is the fact in plant material including oat seeds) impedes 2-DE run. With the use of this technique it is possible to analyze the complex protein mixtures, characteristic protein fractions, as well as individual proteins.The purpose of this chapter is to describe the 2-DE technique (the separate stages of the first and the second dimension) for determining the oat protein composition (oat seed proteome), separation and preliminary identification of oat prolamin fractions. Electrophoretically separated proteins are identified on the basis of pI markers (identifying the location of both ends of an IPG strip) and on 2D SDS-PAGE standards. The gel images of oat proteins are analyzed with the help of ImageMaster 2D Platinum 6.0 program (Amersham Bioscience, part of GE Healthcare, Uppsala, Sweden). It allows finding unique spot identifiers for the occurrence of oat prolamin fractions in oat total proteins. The characteristic spots of similar shape and intensity (anchoring spots) and characteristic groups of spots can be searched for the purpose of identification.