Enzyme Storage and Recycling: Nanoassemblies of α-Amylase and Xylanase Immobilized on Biomimetic Magnetic Nanoparticles

Karima Salem(University of Sfax), Ylenia Jabalera(Universidad de Granada), Jose D. Puentes-Pardo(Universidad de Granada), Jesus Vilchez-Garcia(Universidad de Granada), Adel Sayari(University of Sfax), Aïda Hmida‐Sayari(University of Sfax), Concepción Jiménez-López(Universidad de Granada), Massimiliano Perduca(University of Verona)
ACS Sustainable Chemistry & Engineering
March 9, 2021
Cited by 47Open Access
Full Text

Abstract

-hydroxysuccinimide (NHS). The immobilization protocols were optimized by varying glutaraldehyde (GA) concentration, enzyme quantity, and reaction time. Under optimal conditions, 92% of AmyKS and 87% of XAn11 were immobilized on BMNPs and MNPs-E/N, respectively (here referred as AmyKS-BMNPs and XAn11-MNPs nanoassemblies). The results show that the immobilization of the enzymes did not extensively alter their functionality and increased enzyme stability compared to that of the free enzyme upon storage at 4 and 20 °C. Interestingly, the immobilized amylase and xylanase were reused for 15 and 8 cycles, respectively, without significant loss of activity upon magnetic recovery of the nanoassemblies. The results suggest the great potential of these nanoassemblies in bioindustry applications.


Related Papers

No related papers found

Powered by citation graph analysis