biochemistry
marzieh rashvand; amir arasteh; hashem nayyeri
Abstract
Introduction: Many proteins can be converted into amyloid in the laboratory. These fields are of interest from various points of view, including as a substrate for enzyme stabilization. In this research, cellulase enzyme was immobilized on amyloid nano–biofibrils obtained from bovine serum albumin ...
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Introduction: Many proteins can be converted into amyloid in the laboratory. These fields are of interest from various points of view, including as a substrate for enzyme stabilization. In this research, cellulase enzyme was immobilized on amyloid nano–biofibrils obtained from bovine serum albumin and its kinetic properties were compared with the free form. Methods: The production of amyloid fibers was optimized by Congored absorbance and ThT fluorescence assay methods and was confirmed by transmission electron microscopy. Cellulase enzyme was immobilized via glutaraldehyde cross–linking bridges on amyloid nano–biofibrils. Results: The results of Congored absorbance and ThT fluorescence emission showed that the maximum amyloid fibers at 4 mg/ml of protein concentration, 60 ºC and a pH 3. Electron microscopy images confirmed the presence of amyloid fibers. Immobilizing the enzyme decreased the activity, specific activity and Vm and increased the Km of the enzyme. The optimum temperature of the enzyme increased from 40 to 50 ºC. Discussion: Amyloid nano–biofibrils can be used as a new nano–biomaterial for cellulase immobilization which introduce a useful product in cellulase–related industries.
