Cellulose tosylate as support for α-amylase immobilization

Tremendous potential exists to use cellulose as a support for the immobilization of enzymes. In the current study, cellulose was transformed into cellulose tosylate, and alpha-Amylase was immobilized using the derivatized polymer. Techniques like Fourier transform infrared, scanning electron microscopy, thermogravimetric analysis, and X-ray diffraction methods were used to characterize the support. The support is a perfect illustration of how both covalent and hydrophobic/ionic types of immobilizations can be experimentally used on support. The support was found to show max degradation at 320.2 degrees C with 3.2 % residual substance and crystallinity of about 56.6 %. The support presented maximum enzyme loading at the support: enzyme ratio of 1:4. The immobilized enzyme displayed two ideal pH values (about 4.6 and 7) and two ideal temperatures (approximately 60 degrees C & 40 degrees C). It was discovered that the immobilized alpha-amylase could be used easily eight times with 9.9 % residual activity. The findings of this study show that the immobilized cellulose tosylate enzyme has the potential for application in both acidic and neutral pH environments with the best activity for commercial use.

Automated summary

The study demonstrates the potential of cellulose tosylate as a support for immobilizing enzymes. The immobilized alpha-amylase shows optimal activity at pH 4.6 and 7, and temperatures of approximately 60°C and 40°C. The findings suggest that cellulose tosylate enzyme has potential for commercial use in both acidic and neutral pH environments.