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Nanobiocatalyst consisting of immobilized α-amylase on montmorillonite exhibiting enhanced enzymatic performance based on the allosteric effect.
- Source :
-
Colloids & Surfaces B: Biointerfaces . Mar2022, Vol. 211, pN.PAG-N.PAG. 1p. - Publication Year :
- 2022
-
Abstract
- Enzyme immobilization on nanostructured substrates is an emerging method for the efficient development of nanobiocatalysts to enhance enzymatic performance. In this study, a novel α-amylase nanobiocatalytic system was constructed based on the allosteric activation of the enzyme and its immobilization on a natural nanostructured mineral montmorillonite. The strategy of allosteric modulation and immobilization, equipped the immobilized α-amylase with higher catalytic activity and greater stability (compared to those of free α-amylase) over a broad range of pH values (4.5–9.0) and temperatures (30–80 °C). Kinetic experiments revealed that although the immobilized α-amylase possessed a considerably lower affinity for its substrate, its catalytic activity was higher than that of free α-amylase, likely owing to allosteric modulation. Thus, this study demonstrates a convenient and environmentally benign immobilization strategy to construct a nanobiocatalytic α-amylase system that exploits the phenomenon of allosteric activation of the enzyme and lays the foundation for further industrial applications. [Display omitted] • The design of α-amylase/Mt nanobiocatalytic system based on allosteric effect. • The catalytic activities of α-amylase/Ca-Mt-NaCl were hiked compared to free form. • Immobilized α-amylase have better operation and storage stability. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 09277765
- Volume :
- 211
- Database :
- Academic Search Index
- Journal :
- Colloids & Surfaces B: Biointerfaces
- Publication Type :
- Academic Journal
- Accession number :
- 155257654
- Full Text :
- https://doi.org/10.1016/j.colsurfb.2021.112290