ATR-FTIR and UV/Vis spectrophotometric analyses of alpha-amylase bioactive paper

Abstract

Alpha-amylase enzyme is a desirable biocatalyst in starch hydrolysis process. It can perform its catalytic activity in either soluble or immobilized form. Immobilization of this enzyme is a chief strategy to make starch hydrolysis process more robust and cost effective. In this study alpha-amylase bioactive paper (AABP) was produced using a desktop inkjet printer, commercial alpha-amylase enzyme and selected commercial cellulosic papers. Attenuated Total Reflectance Fourier Transform Infrared (ATR-FTIR) analysis showed that the inkjet printing strategy was successful in immobilizing alpha-amylase enzyme on paper surface. Functionality and recyclability of AABPs were successfully evaluated using starch-iodine assay and UV/Vis spectrophotometry. It was found that AABP2 exhibited the highest relative activity (80-90%) and was able to be recycled up to three times without notable activity loss and structural defect. Therefore, we have highlighted the durability, functionality and recyclability of AABPs which potentially contribute to low cost sugar industries.