Immobilization of neocallimastix patriciarum xylanase on carboxylated multy walled carbon nanotubes to produce xylooligosaccharides from xylan

Enzymes, which are biological catalysts due to their superior properties compared to chemical catalysts, have many applications in the industry. However, since the enzymes in soluble form are not suitable for continuous processes in the industry, they are used once in batch processes or consumed together with the product or separated from the product by using very expensive techniques. In this thesis, Neocallimastix patriciarum xylanase immobilization was performed by adsorption on immobilization matrix c-MWCNT. By optimizing the immobilization conditions, 100% immobilization and 160.35% activity efficiencies were obtained. The optimum pH range of the enzyme (5.5-6.0) and the optimum temperature of the enzyme (55 oC) did not change after immobilization. The kinetic constants of the free and immobilized enzymes were also determined using the Lineweaver-Burk graph. Km values of free and immobilized enzyme as substrate for Beechwood Xylan were 1019.5 and 704.2 μg / mL, respectively, while Vmax values were 0.043 μmol / mg.dk and 0.069 μmol / mg.dk respectively. The immobilized enzyme did not lose its initial activity during repeated twenty batch use and during twenty days of storage. Using the immobilized enzyme, beach wood xylan was hydrolyzed at the end of two hours at the optimum temperature in an orbital shaker and heated incubator at a shaking rate of 150 rpm. Hydrolysis of proteins has been shown to be completed in 120 minutes. In conclusion, it can be said that the immobilized Neocallimastix patriciarum xylanase obtained in this thesis study can be used for industrial production of xylooligosaccharides with prebiotic properties.