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Tomczyk, Łukasz, 2024, "Results of physicochemical properties of modified lysozyme with pepsin and trypsin", https://doi.org/10.18150/BOCBUA, RepOD, V2
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The data set contains the results of studies on an attempt to obtain bioactive peptide fractions from lysozyme derived from hen egg by enzymatic hydrolysis. The data file contains the results of enzymatic modification of lysozyme carried out in two successive stages. 1. Stage one – hydrolytic modification of lysozyme using pepsin and trypsin. For modification, a 5% aqueous solution of lysozyme at pH 2 was prepared containing a mixture of trypsin and pepsin in the ratios of 1/0, 0.75/0.25, 0.5/0.5, 0.25/0.5, 0/1, respectively. The hydrolysis reactions were carried out in the ratio of lysozyme to the enzyme mixture of 500/1. The reference sample was a lysozyme solution without added enzymes. Samples containing pepsin and trypsin and the reference sample were modified in the analytical reactor BUCHI Syncore® (Switzerland) at 55 °C for 60 minutes, then the reaction was stopped by heating them for 5 minutes at 85 °C and then, after cooling, their pH value was set at 7.0. The second stage - consisted in assessing the effect of peptides and oligomers formed as a result of lysozyme modification on physicochemical properties. For this purpose, for the most advantageous in the first variant of the experiment in the formation of the peptide and oligomeric fraction of the enzyme, i.e. pepsin, subsequent modifications of lysozyme were carried out, this time in the ratio of lysozyme to pepsin: 1/2000, 1/1500, 1/750, 1/500, 1/250, 1/166, 1/125, 1/100. The obtained preparations were frozen and then lyophilized in Labconco-freezedryer (USA). The preparations prepared in this way were subjected to analytical tests, i.e. hydrolytic and antioxidant activity, hydrophobicity, percentage of oligomeric and peptide fractions, molecular weights of the obtained individual peptide fractions and the level of immunoreactivity. The obtained fractions were also visualized using densitometric analysis.
Zbiór danych zawiera wyniki badań nad próbą otrzymania bioaktywnych frakcji peptydowych z lizozymu pochodzącego z jaja kurzego w wyniku hydrolizy enzymatycznej. Pliki danych zawierają wyniki enzymatycznej modyfikacji lizozymu prowadzonej w dwóch następujących po sobie etapach. 1. Etap pierwszy - modyfikacja hydrolityczna lizozymu z zastosowaniem pepsyny i trypsyny. Do modyfikacji przygotowano 5%-owy wodny roztwór lizozymu o pH 2 zawierający mieszaninę trypsyny i pepsyny w stosunku odpowiednio 1/0, 0.75/0.25, 0.5/0.5, 0.25/0.5, 0/1. Reakcję hydrolizy prowadzono w stosunku lizozymu do mieszaniny enzymów 500/1. Próbą odniesienia był roztwór lizozymu bez dodatku enzymów. Próby zawierające pepsynę i trypsynę oraz próbę odniesienia modyfikowano w reaktorze analitycznym BUCHI Syncore® (Szwajcaria) w temperaturze 55 °C przez 60 minut, po czym reakcję zatrzymywano ogrzewając je przez 5 minut w temperaturze 85°C, a następnie, po ich ochłodzeniu, ustalono wartość ich pH na poziomie równym 7,0. Etap drugi - polegał na ocenie wpływu powstałych w wyniku modyfikacji lizozymu peptydów i oligomerów na właściwości fizykochemiczne. W tym celu dla najkorzystniejszego w pierwszym wariancie doświadczenia w tworzeniu frakcji peptydowej i oligomerycznej enzymu tj. pepsyny przeprowadzono kolejne modyfikacje lizozymu tym razem w stosunku lizozymu do pepsyny: 1/2000, 1/1500, 1/750, 1/500, 1/250, 1/166, 1/125, 1/100. Otrzymane preparaty zostały zamrożone, a następnie zliofilizowane w Labconco-freezedryer (USA). Tak przygotowane preparaty poddano badaniom analitycznym tj. aktywność hydrolityczna, przeciwutleniająca, hydrofobowość, procentowa zawartość frakcji oligomerycznej i peptydowej, masy cząsteczkowe otrzymanych poszczególnych frakcji peptydowych oraz poziom immunoreaktywności. Dokonano również zobrazowania otrzymanych frakcji za pomocą analizy densytometrycznej.
hydrolytic activity, hydrophobicity, antioxidant activity, percentage of peptide oligomers and fractions, lysozyme, hydrolysis, oligomerization
Tomczyk, Ł., Leśnierowski, G., Tomczak, A., Ajemigbitse, J.A., Szablewski, T., Cegielska-Radziejewska, R. The influence of proteolytic enzymes on the change of lysozyme properties. PLOS.One. 2025, https://doi.org/10.1371/journal.pone.0326386 https://doi.org/10.1371/journal.pone.0326386 doi: 10.1371/journal.pone.0326386
CC BY - Creative Commons Attribution 4.0
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