Enhanced starch hydrolysis using α-amylase immobilized on cellulose ultrafiltration affinity membrane

• Preparation of UF cellulose membrane with biocatalytic flexible layer was elaborated.
• Membranes with immobilized α-amylase showed enhanced starch hydrolysis properties.
• Concentration polarization was reduced due to the presence of the enzyme.
• Enzymatic layer of α-amylase can be regenerated.

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.

Figure optionsDownload as PowerPoint slide