Division of Pharmaceutical Technology, Faculty of Pharmacy, University of Helsinki, Helsinki, P.O. Box 56, 00014, Finland.
AAPS PharmSciTech. 2010 Jun;11(2):959-65. doi: 10.1208/s12249-010-9462-4. Epub 2010 May 29.
We nano-coated powdered lactose particles with the enzyme beta-galactosidase using an ultrasound-assisted technique. Atomization of the enzyme solution did not change its activity. The amount of surface-attached beta-galactosidase was measured through its enzymatic reaction product D-galactose using a standardized method. A near-linear increase was obtained in the thickness of the enzyme coat as the treatment proceeded. Interestingly, lactose, which is a substrate for beta-galactosidase, did not undergo enzymatic degradation during processing and remained unchanged for at least 1 month. Stability of protein-coated lactose was due to the absence of water within the powder, as it was dry after the treatment procedure. In conclusion, we were able to attach the polypeptide to the core particles and determine precisely the coating efficiency of the surface-treated powder using a simple approach.
我们使用超声辅助技术将β-半乳糖苷酶纳米涂层涂覆在粉状乳糖颗粒上。酶溶液的雾化并没有改变其活性。通过使用标准化方法测量其酶反应产物 D-半乳糖来测量附着在表面的β-半乳糖苷酶的量。随着处理的进行，酶涂层的厚度几乎呈线性增加。有趣的是，乳糖是β-半乳糖苷酶的底物，在处理过程中没有发生酶降解，至少在 1 个月内保持不变。蛋白质涂层乳糖的稳定性是由于粉末中没有水分，因为处理后它是干燥的。总之，我们能够将多肽附着在核心颗粒上，并使用简单的方法精确确定表面处理粉末的涂层效率。
