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The influence of proteolytic enzymes on the change of lysozyme properties

cris.virtual.author-orcid0000-0002-4644-0111
cris.virtual.author-orcid0000-0002-9674-9803
cris.virtual.author-orcid0000-0003-2530-6535
cris.virtual.author-orcid0000-0001-6076-8095
cris.virtual.author-orcid0000-0002-3554-5276
cris.virtual.author-orcid#PLACEHOLDER_PARENT_METADATA_VALUE#
cris.virtualsource.author-orcidd3aa317f-f6c6-43ef-a508-ee305375c7c4
cris.virtualsource.author-orcid157f10c9-f5b6-45a8-a8e3-aff60e541c67
cris.virtualsource.author-orcid9af677aa-a894-4dc6-8898-f77473ec4e6d
cris.virtualsource.author-orcidf3725b78-a868-4158-aaed-7f4692cfd53b
cris.virtualsource.author-orcidbc235846-e970-4e78-8686-9de6ac41765e
cris.virtualsource.author-orcid#PLACEHOLDER_PARENT_METADATA_VALUE#
dc.abstract.enThis research examines the enzymatic modification of lysozyme, a glycosidic hydrolase that has restricted effectiveness against Gram-negative bacteria, in order to produce bioactive peptide fractions with improved antibacterial and physicochemical characteristics. Utilizing chicken egg lysozyme, modifications were performed in controlled settings with proteolytic enzymes, mainly pepsin, and experiments with a pepsin-trypsin ratio. The modification methods sought to improve the hydrophobic nature of lysozyme’s surface, create oligomeric and peptide forms, and decrease immunogenicity. Findings showed that raising pepsin concentration enhanced the creation of peptide fractions, increasing surface hydrophobicity while reducing hydrolytic and antioxidant activities. Increased hydrophobicity and reduced enzyme activity were linked to enhanced antibacterial effectiveness, particularly against Gram-negative bacteria, a characteristic absent in natural lysozyme. Additionally, the research noted a decrease in immunoreactivity as pepsin concentrations increased, achieving the lowest antibody response in optimized formulations. This enzymatic method offers an economical way to create lysozyme derivatives that hold considerable promise for wider applications, particularly in scenarios where lower immunoreactivity and a prolonged antibacterial spectrum are needed.
dc.affiliationWydział Nauk o Żywności i Żywieniu
dc.affiliation.instituteKatedra Zarządzania Jakością i Bezpieczeństwem Żywności
dc.affiliation.instituteKatedra Biochemii i Analizy Żywności
dc.contributor.authorTomczyk, Łukasz
dc.contributor.authorLeśnierowski, Grzegorz
dc.contributor.authorTomczak, Aneta
dc.contributor.authorAjemigbitse, Jubilee Amajuoritse
dc.contributor.authorSzablewski, Tomasz
dc.contributor.authorCegielska-Radziejewska, Renata
dc.date.access2025-08-07
dc.date.accessioned2025-08-11T06:05:07Z
dc.date.available2025-08-11T06:05:07Z
dc.date.copyright2025-06-26
dc.date.issued2025
dc.description.abstract<jats:p>This research examines the enzymatic modification of lysozyme, a glycosidic hydrolase that has restricted effectiveness against Gram-negative bacteria, in order to produce bioactive peptide fractions with improved antibacterial and physicochemical characteristics. Utilizing chicken egg lysozyme, modifications were performed in controlled settings with proteolytic enzymes, mainly pepsin, and experiments with a pepsin-trypsin ratio. The modification methods sought to improve the hydrophobic nature of lysozyme’s surface, create oligomeric and peptide forms, and decrease immunogenicity. Findings showed that raising pepsin concentration enhanced the creation of peptide fractions, increasing surface hydrophobicity while reducing hydrolytic and antioxidant activities. Increased hydrophobicity and reduced enzyme activity were linked to enhanced antibacterial effectiveness, particularly against Gram-negative bacteria, a characteristic absent in natural lysozyme. Additionally, the research noted a decrease in immunoreactivity as pepsin concentrations increased, achieving the lowest antibody response in optimized formulations. This enzymatic method offers an economical way to create lysozyme derivatives that hold considerable promise for wider applications, particularly in scenarios where lower immunoreactivity and a prolonged antibacterial spectrum are needed.</jats:p>
dc.description.accesstimeat_publication
dc.description.bibliographyil., bibliogr.
dc.description.financepublication_nocost
dc.description.financecost0,00
dc.description.if2,6
dc.description.number6
dc.description.points100
dc.description.versionfinal_published
dc.description.volume20
dc.identifier.doi10.1371/journal.pone.0326386
dc.identifier.issn1932-6203
dc.identifier.urihttps://sciencerep.up.poznan.pl/handle/item/4122
dc.identifier.weblinkhttps://journals.plos.org/plosone/article?id=10.1371/journal.pone.0326386
dc.languageen
dc.relation.ispartofPLoS ONE
dc.relation.pagese0326386
dc.rightsCC-BY
dc.sciencecloudsend
dc.share.typeOPEN_JOURNAL
dc.titleThe influence of proteolytic enzymes on the change of lysozyme properties
dc.typeJournalArticle
dspace.entity.typePublication
oaire.citation.issue6
oaire.citation.volume20