Researchers demonstrate that encapsulation is not necessary to achieve controlled, long-term protein release.

No abstract

The stability of a paper-immobilized antibody was investigated over a range of temperatures (40-140 °C) and relative humidities (RH, 30-90%) using both unmodified filter paper and the same paper impregnated with polyamide-epichlorohydrin (PAE) as supports. Antibody stability decreased with increasing temperature, as expected, but also decreased with increasing RH. At 40 °C, the half-life was more than 10 days, with little dependence on RH. However, at 80 °C, the half-life varied from ~3 days at low RH to less than half an hour at 90% RH, demonstrating that hydration of the antibody promotes unfolding. Antibody stability was not influenced by the PAE paper surface treatment. This work shows that antibodies are good candidates for development of bioactive paper as they have sufficient stability at high temperature to withstand printing and other roll-to-roll processing steps, and sufficient low temperature stability to allow long-term storage of bioactive paper materials.

No abstract

Polyelectrolyte complexes formed between laccase and polyvinylamine with grafted TEMPO moieties, PVAm-T, adsorb onto cellulose, causing oxidation. All evidence supports the view that aldehyde groups on oxidized cellulose condense with primary amine groups, giving a grafted layer of PVAm-T complexed with laccase. The grafted PVAm-T serves as a primer layer promoting wet cellulose-to-cellulose adhesion in the presence of PVAm adhesive. The cellulose modification occurs at ambient temperatures and pH 5. The adhesion improvements with mixtures of PVAm-T and laccase are remarkable because both components are macromolecular, which should inhibit the ability of the TEMPO to act as a shuttle between the enzyme and the primary hydroxyl groups on cellulose. It is proposed that PVAm-bound oxoammonium ions exchange with neighboring TEMPO moieties, providing a mechanism for the transfer of oxidation activity from immobilized enzyme to the cellulose surfaces.