Acet, Ömürİnanan, TüldenKoç, Eda ÖndülSert, BuseAcet, Burcu ÖnalOdabaşı, Mehmet2024-06-062024-06-062023Acet, Ö., İnanan, T., Koc, E. O., Sert, B., Önal Acet, B., Odabaşı, M., ... & Dizge, N. (2023). Immobilization of Alpha‐Amylase onto Ni2+ Attached Carbon Felt: Investigation of Kinetic Parameters from Potato Wastewater. Starch‐Stärke, 75(11-12), 2300033.0038-90561521-379Xhttp://dx.doi.org/10.1002/star.202300033https://hdl.handle.net/20.500.12491/12207Alpha-amylase is an important enzyme for textile, food, paper, and the pharmaceutical industrial areas. In this study, Ni2+ attached carbon felt structures with nitrogen active site (Ni2+-N-ACF) are produced. The surface morphologies of the N-ACF and Ni2+-N-ACF are investigated by means of scanning electron microscopy (SEM) analysis. Ni2+ ions binding on the N-ACFs are determined by energy dispersive X-ray (EDX) analysis and a graphite furnace atomic absorption spectrometer (AAS). The effect of pH, ionic strength, initial alpha-amylase concentration, and temperature parameters is investigated for alpha-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 are made. Lastly, starch degradation in potato waste water is tested on Ni2+-N-ACF. The obtained results show that alpha-amylase immobilized Ni2+-N-ACF can be used for starch degradation on an industrial scale.eninfo:eu-repo/semantics/closedAccessActivated Carbon FeltActivationAlpha-AmylaseImmobilizationStarch DegradationMetalArticle10.1002/star.2023000337511-12182-s2.0-85168586502Q2WOS:001115819400016Q2