Australian Pulp and Paper Institute, Department of Chemical Engineering, Monash University, Clayton, VIC 3800, Australia.
Colloids Surf B Biointerfaces. 2010 Jan 1;75(1):239-46. doi: 10.1016/j.colsurfb.2009.08.042. Epub 2009 Sep 3.
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 2-3 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 degrees 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-cost-high volume bioactive surfaces.
使用一种比色技术测量产物复合物的强度来测定吸附在纸上的两种酶（碱性磷酸酶（ALP）和辣根过氧化物酶（HRP））的热稳定性。吸附在纸上的酶保留了其功能和选择性。与相同的溶液中的酶相比，吸附在纸上将酶的热稳定性提高了 2-3 个数量级。ALP 和 HRP 酶纸在 23°C 时的半衰期分别为 533 小时和 239 小时。吸附酶的热降解被发现遵循两个连续的一级反应，表明是一个反应体系。使用热喷墨打印机在纸上打印出复杂的酶图案。纸和喷墨打印是制造低成本、高容量生物活性表面的理想材料和工艺。
