Thermal stability of bioactive enzymatic papers

Mohammad Khan, Xu Li, Wei Shen, Gil Garnier

Research output: Contribution to journalArticleResearchpeer-review

46 Citations (Scopus)

Abstract

The thermal stability of two enzymes adsorbed on paper, alkaline phosphatase (ALP) and horseradish peroxidase (HRP), was measured using a colorimetric technique quantifying the intensity of the product complex. The enzymes adsorbed on paper retained their functionality and selectivity. Adsorption on paper increased the enzyme thermal stability by 2a??3 orders of magnitude compared to the same enzyme in solution. ALP and HRP enzymatic papers had half-lives of 533 h and 239 h at 23 A?C, respectively. The thermal degradation of adsorbed enzyme was found to follow two sequential first-order reactions, indication of a reaction system. A complex pattern of enzyme was printed on paper using a thermal inkjet printer. Paper and inkjet printing are ideal material and process to manufacture low-costa??high volume bioactive surfaces.
Original languageEnglish
Pages (from-to)239 - 246
Number of pages8
JournalColloids and Surfaces B: Biointerfaces
Volume75
Issue number1
DOIs
Publication statusPublished - 2010

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