| Literature DB >> 27516322 |
Viktoriia Konovalova1, Kateryna Guzikevich1, Anatoliy Burban1, Wojciech Kujawski2, Karolina Jarzynka3, Joanna Kujawa4.
Abstract
In order to prepare ultrafiltration membranes possessing biocatalytic properties, α-amylase has been immobilized on cellulose membranes. Enzyme immobilization was based on a covalent bonding between chitosan and a surface of cellulose membrane, followed by an attachment of Cibacron Blue F3G-A dye as affinity ligand. Various factors affecting the immobilization process, such as enzyme concentration, pH of modifying solution, zeta-potential of membrane surface, and stability of immobilized enzyme were studied. The applicability of immobilized α-amylase has been investigated in ultrafiltration processes. The immobilization of α-amylase on membrane surface allows to increase the value of mass transfer coefficient and to decrease the concentration polarization effect during ultrafiltration of starch solutions. The enzyme layer on the membrane surface prevents a rapid increase of starch concentration due to the amylase hydrolysis of starch in the boundary layer. The presented affinity immobilization technique allows also for the regeneration of membranes from inactivated enzyme.Entities:
Keywords: Cellulose affinity membranes; Concentration polarization; Membrane surface modification; Starch hydrolysis; Ultrafiltration; α-Amylase immobilization
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Year: 2016 PMID: 27516322 DOI: 10.1016/j.carbpol.2016.07.065
Source DB: PubMed Journal: Carbohydr Polym ISSN: 0144-8617 Impact factor: 9.381