Immobilization of [alpha]-amylase in polyelectrolyte complexes

• Published in: Journal of applied polymer science Vol. 134; no. 27
• Main Authors: Kubelbeck, Sonja, Mikhael, Jules, Schoof, Sebastian, Andrieu-Brunsen, Annette, Baier, Grit
• Format: Journal Article
• Language: English
• Published: Hoboken Wiley Subscription Services, Inc 15.07.2017
• Subjects: Materials science; Polymers
• ISSN: 0021-8995; 1097-4628
• DOI: 10.1002/app.45036

Herein, we report the formation of [alpha]-amylase containing polyelectrolyte complexes (PECs). The method for the encapsulation of [alpha]-amylase is based on interactions between two oppositely charged polyelectrolytes, poly(acrylic acid) (PAA) and polyethylenimine (PEI). We could show that electrostatic interactions ensure the incorporation of the enzyme into the formed polyelectrolyte complexes. The encapsulation has no negative effect on enzyme activity and protects against denaturation of the enzyme initiated by low pH values. The resulting PECs are 150-250 nm in size with narrow size distribution, appear in a spherical shape and are colloidally stable. The complexation of both polyelectrolytes and the immobilization of [alpha]-amylase are investigated using fractionating techniques mainly the analytical ultracentrifugation and asymmetrical-flow field-flow fractionation. The formation of PECs represents a simple method for the encapsulation of [alpha]-amylase without the use of organic solvents and requires no additional purifications steps. This one-step approach, yielding high encapsulation efficiencies, shows the potential as a drug delivery system for sensitive hydrophilic actives in future. [alpha]-amylase is immobilized in polyelectrolyte complexes made of polyethylenimine and poly(acrylic acid). Optimized encapsulation conditions and the resulting polyelectrolyte complexes are investigated via determination of IEP, [alpha]-amylase activity assays, nanoDSC measurements, zeta potential values, dynamic light scattering, microscopy, and fractionating techniques. The encapsulated enzyme is protected against denaturation initiated by low pH values. © 2017 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2017, 134, 45036.