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dc.contributor.authorGlomm, Wilhelm
dc.contributor.authorWubshet, Sileshi Gizachew
dc.contributor.authorLindberg, Diana
dc.contributor.authorDankel, Katinka R.
dc.contributor.authorAfseth, Nils Kristian
dc.contributor.authorStenstad, Per Martin
dc.contributor.authorJohnsen, Heidi
dc.date.accessioned2021-09-27T07:59:24Z
dc.date.available2021-09-27T07:59:24Z
dc.date.created2021-09-16T12:08:34Z
dc.date.issued2021
dc.identifier.citationLebensmittel-Wissenschaft + Technologie. 2021, 152 1-11.
dc.identifier.issn0023-6438
dc.identifier.urihttps://hdl.handle.net/11250/2783613
dc.description.abstractImmobilization of enzymes onto magnetic particles can potentially allow for enzyme reuse, which can significantly reduce the cost associated with e.g. enzymatic protein hydrolysis (EPH) of fish and meat by-products. Here, we report glutaraldehyde-mediated immobilization of a food-grade protease (Subtilisin A) onto magnetic silica particles using three different amine ligands; a short, brush-like linker (aminopropyl trimethoxysilane), a long, flexible linker (Jeffamine), and a gel-like coating (chitosan). The three coupling strategies were evaluated and compared with respect to the amount of immobilized protease, enzyme activity and catalytic performance in the hydrolysis of chicken meat and turkey tendons, respectively. The particle systems showed high reusability (≤85% activity remaining after six consecutive cycles) and storage stability (≤93% activity remaining after 25 months storage). Particle-immobilized enzyme systems were able to catalyze degradation and extraction of protein from chicken meat and turkey tendons.
dc.language.isoeng
dc.subjectEnzymatic activity
dc.subjectEnzymatic activity
dc.subjectEnzymatic protein hydrolysis
dc.subjectEnzymatic protein hydrolysis
dc.subjectMagnetic silica particles
dc.subjectMagnetic silica particles
dc.subjectEnzyme immobilization
dc.subjectEnzyme immobilization
dc.titleImmobilized protease on magnetic particles for enzymatic protein hydrolysis of poultry by-products
dc.typePeer reviewed
dc.typeJournal article
dc.description.versionpublishedVersion
dc.source.pagenumber1-11
dc.source.volume152
dc.source.journalLebensmittel-Wissenschaft + Technologie
dc.identifier.doi10.1016/j.lwt.2021.112327
dc.identifier.cristin1934867
dc.relation.projectNorges forskningsråd: 314111
dc.relation.projectNofima AS: 12336
dc.relation.projectNofima AS: 202102
dc.relation.projectNorges forskningsråd: 280709
cristin.ispublishedtrue
cristin.fulltextoriginal
cristin.qualitycode1


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