Exceptional thermal stability of industrially-important enzymes by entrapment within nano-boehmite derived alumina

Vladimir V. Vinogradov*, David Avnir

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

24 Scopus citations

Abstract

We developed an alumina sol-gel matrix based on boehmite nanorods as a superior carrier for enzyme immobilization. Proteinase and xylanase were chosen for this study, as important representatives of industrially applied enzymes. For these two enzymes we observed exceptional thermal stability by entrapment within the alumina (enzyme@alumina). We show - using kinetics, DSC and CD analyses - that alumina holds strongly and thus keeps the native structures of the proteins, preventing unfolding at high temperatures. For instance, the activity of xylanase entrapped within alumina increases with temperature up to 80°C (!), whereas being in solution or entrapped in silica drops the activities to zero at that temperature; whereas CD clearly shows that proteinase undergoes conformational changes above 30°C, in the case of the entrapped enzyme, the ellipticity remains constant up to 90°C. The importance of the nanoporosity of the nanorods derived alumina is shown for this superior stability. The findings open the door to potential new applications of these enzymes for high temperature organic syntheses.

Original languageEnglish
Pages (from-to)10862-10868
Number of pages7
JournalRSC Advances
Volume5
Issue number15
DOIs
StatePublished - 2015

Bibliographical note

Publisher Copyright:
© The Royal Society of Chemistry 2015.

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