Rodyti trumpą aprašą

dc.contributor.authorGruškienė, Rūta
dc.contributor.authorKavleiskaja, Tatjana
dc.contributor.authorSereikaitė, Jolanta
dc.date.accessioned2023-09-18T16:46:42Z
dc.date.available2023-09-18T16:46:42Z
dc.date.issued2017
dc.identifier.issn0023-6438
dc.identifier.urihttps://etalpykla.vilniustech.lt/handle/123456789/116522
dc.description.abstractProteolytic stability of nisin-loaded pectin and nisin-loaded pectin-inulin particles, previously developed for food preservation, was investigated and compared with free nisin. The acid protease from Aspergillus saitoi and trypsin were used. The hydrolysis of free nisin by the mentioned proteases resulted in four and three peaks of degradation products, respectively, in the analysis by capillary zone electrophoresis method. The complexation of nisin with biopolymers increased its proteolytic stability. The areas of detected peaks significantly decreased. The stability of particles was dependent on the degree of pectin esterification. The particles prepared using pectic acid or the pectin with low degree of esterification exhibited the highest proteolytic stability. Overall, nisin-loaded pectin-inulin particles were more stable than nisin-loaded pectin particles.eng
dc.formatPDF
dc.format.extentp. 283-286
dc.format.mediumtekstas / txt
dc.language.isoeng
dc.relation.isreferencedbyAcademic Search Complete
dc.relation.isreferencedbyScopus
dc.relation.isreferencedbyScience Citation Index Expanded (Web of Science)
dc.source.urihttps://doi.org/10.1016/j.lwt.2017.04.061
dc.subjectFM01 - Biokatalitinių procesų modeliavimas / Modelling of biocatalytic processes
dc.titleNisin-loaded pectin and nisin-loaded pectin-inulin particles: comparison of their proteolytic stability with free nisin
dc.typeStraipsnis Web of Science DB / Article in Web of Science DB
dcterms.references27
dc.type.pubtypeS1 - Straipsnis Web of Science DB / Web of Science DB article
dc.contributor.institutionVilniaus Gedimino technikos universitetas
dc.contributor.institutionVilniaus universitetas
dc.contributor.facultyFundamentinių mokslų fakultetas / Faculty of Fundamental Sciences
dc.contributor.departmentChemijos ir bioinžinerijos katedra / Department of Chemistry and Bioengineering
dc.subject.researchfieldT 005 - Chemijos inžinerija / Chemical engineering
dc.subject.ltspecializationsL101 - Agroinovacijos ir maisto technologijos / Agro-innovation and food technologies
dc.subject.enNisin-loaded pectin particles
dc.subject.enNisin-loaded pectin-inulin particles
dc.subject.enProteolytic stability
dc.subject.enThe acid protease
dc.subject.enTrypsin
dcterms.sourcetitleLWT-Food science and technology
dc.description.volumeVol. 82
dc.publisher.nameElsevier
dc.publisher.cityAmsterdam
dc.identifier.doi000402497000037
dc.identifier.doi10.1016/j.lwt.2017.04.061
dc.identifier.elaba23034132


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