Immobilization of Alpha‐Amylase onto Ni²⁺ Attached Carbon Felt: Investigation of Kinetic Parameters from Potato Wastewater

Abstract

Abstractα‐amylase is an important enzyme for textile, food, paper, and pharmaceutics industrial areas. In this study, Ni+2 attached carbon felt structures with nitrogen active site (Ni+2‐N‐ACF) were produced. The surface morphologies of the N‐ACF and Ni2+‐N‐ACF were investigated by means of SEM analysis. Ni2+ ions binding on the N‐ACFs were determined by energy dispersive X‐ray (EDX) analysis and a graphite furnace atomic absorption spectrometer (AAS). The effect of pH, ionic strength, initial α‐amylase concentration and temperature parameters were investigated for α‐amylase immobilization on Ni2+‐N‐ACF structures. In addition, pH and temperature effect on the activities of the free and the immobilized amylase, kinetic parameters, storage and operational stabilities were made decision. Lastly, starch degradation in potato waste water was tested on Ni2+‐N‐ACF. The obtained results showed that α‐amylase immobilized Ni2+‐N‐ACF can be used for starch degradation in industrial scale.This article is protected by copyright. All rights reserved