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

Autor:	Salem K; Centre de Biotechnologie de Sfax (CBS), Université de Sfax, Route de Sidi Mansour Km 6, BP '1177', 3018 Sfax, Tunisie., Jabalera Y; Departamento de Microbiologia, Universidad de Granada, Campus de Fuentenueva s/n, 18071 Granada, Spain., Puentes-Pardo JD; Departamento de Microbiologia, Universidad de Granada, Campus de Fuentenueva s/n, 18071 Granada, Spain., Vilchez-Garcia J; Departamento de Microbiologia, Universidad de Granada, Campus de Fuentenueva s/n, 18071 Granada, Spain., Sayari A; ENIS, Université de Sfax, BP '1173', 3038 Sfax, Tunisie., Hmida-Sayari A; Centre de Biotechnologie de Sfax (CBS), Université de Sfax, Route de Sidi Mansour Km 6, BP '1177', 3018 Sfax, Tunisie., Jimenez-Lopez C; Departamento de Microbiologia, Universidad de Granada, Campus de Fuentenueva s/n, 18071 Granada, Spain., Perduca M; Department of Biotechnology, University of Verona, Strada Le Grazie 15, 37134 Verona, Italy.
Jazyk:	angličtina
Zdroj:	ACS sustainable chemistry & engineering [ACS Sustain Chem Eng] 2021 Mar 22; Vol. 9 (11), pp. 4054-4063. Date of Electronic Publication: 2021 Mar 09.
DOI:	10.1021/acssuschemeng.0c08300
Abstrakt:	Immobilization of enzymes has been extensively required in a wide variety of industrial applications as a way to ensure functionality and the potential of enzyme recycling after use. In particular, enzyme immobilization on magnetic nanoparticles (MNPs) could offer reusability by means of magnetic recovery and concentration, along with increased stability and robust activity of the enzyme under different physicochemical conditions. In the present work, microbial α-amylase (AmyKS) and xylanase (XAn11) were both immobilized on different types of MNPs [MamC-mediated biomimetic MNPs (BMNPs) and inorganic MNPs] by using two different strategies (electrostatic interaction and covalent bond). AmyKS immobilization was successful using electrostatic interaction with BMNPs. Instead, the best strategy to immobilize XAn11 was using MNPs through the hetero-crosslinker 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC) and N -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. Competing Interests: The authors declare no competing financial interest. (© 2021 American Chemical Society.)
Databáze:	MEDLINE
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