Taher, Alan YaseenAlizadeh, MohammadAslan, Yakup2024-12-242024-12-2420242008-8787https://doi.org10.22034/FSCT.20.145.208https://hdl.handle.net/20.500.12604/3961This study was carried out with the aim of covalent immobilization of Aspergillus oryzae beta-galactosidase and Bacillus licheniformis protease on multi-walled amino-carbon nanotubes. In this method, fractional 2k design was used to study the effect of seven continuous factors (activation pH, glutaraldehyde molarity, activation time, buffer solution pH, buffer solution molarity, MWCNT-NH3-glutaraldehyde amount and stabilization time) on the stabilization efficiency and enzyme activity. . Design-expert software was used to analyze data and draw graphs. The results showed that the aforementioned factors predict the level of enzyme activity of Bacillus licheniformis protease and Aspergillus oryzae beta-galactosidase with correlation coefficients of 0.80 and 0.92 at the rate of 77 and 88%, respectively. Also, the correlation coefficient of the covalent fixation efficiency model of Aspergillus oryzae beta-galactosidase and Bacillus licheniformis protease on multi-walled carbon nanotubes was 0.89 and 0.82, respectively, and the studied factors were able to determine the covalent fixation beta efficiency, respectively. Aspergillus oryzae galactosidase and Bacillus licheniformis protease on multi-walled amino-carbon nanotubes predict 83 and 77%, respectively. © 2024 Tarbiat Modares University. All rights reserved.eninfo:eu-repo/semantics/closedAccessAlkaline proteasecarbon nanotubescovalent immobilization?-galactosidaseArticle20145208224Q42-s2.0-8518489300210.22034/FSCT.20.145.208