α-Glucosidase enzyme entrapped superporous poly(amphoteric) cryogel reactor with improved enzymatic activity and stability over wide pH ranges

Abstract

Cryogels are one of the most unique materials for enzyme immobilization due to their super-porous elastic structures, and fast response times. Not only can cryogels act as flexible compartmentalization supports for enzymes, but they can also serve as solid protective matrices capable of preserving enzymatic activity over extreme conditions. The contributions of individual anionic and cationic cryogels to improve enzymatic activity can be combined into one as a cyrogels of poly(ampholyte). The present study targets the development of p(Amphoteric) cryogel as support for immobilization of enzymes and modeled in-depth characterizations and applications of α-Glucosidase (α-Glu) enzyme by entrapment ((α-Glu@p(Amphoteric)) during cryogelation. The α-Glu@p(Amphoteric) cryogels had 91.3 ± 1.7% activity at pH 6.8 and 37 °C the optimum conditions for free enzyme. They exhibited excellent pH tolerability with more than 70% activity between pH 5–8 at 37 °C, and more than 50% activity between 20–50 °C at pH 6.8. They showed improved storage stability even at 25 °C with almost 50% activity on the 10th days of storage and extraordinary reusability performances with more than 50% activity after 10th consecutive usages, respectively.