Cross-linked α-amylase aggregates on Fe3O4 magnetic nanoparticles modified with polydopamine/polyethyleneimine for efficient hydrolysis of starch--颗粒学报PARTICUOLOGY

Cui, J., Tang, X., Ma, Q., Chang, Y., Zhang, Q., & Jia, S. (2024). Cross-linked α-amylase aggregates on Fe3O4 magnetic nanoparticles modified with polydopamine/polyethyleneimine for efficient hydrolysis of starch. Particuology, 90, 98-105. https://doi.org/10.1016/j.partic.2023.11.020

Cross-linked α-amylase aggregates on Fe₃O₄ magnetic nanoparticles modified with polydopamine/polyethyleneimine for efficient hydrolysis of starch

Jiandong Cui ^{a b *}, Xiuming Tang ^a, Qingqing Ma ^a, Yuyan Chang^a, Qunli Zhang ^a, Shiru Jia ^a

a State Key Laboratory of Food Nutrition and Safety, Laboratory of Industrial Fermentation Microbiology, Ministry of Education, Tianjin University of Science and Technology, Tianjin 300457, China
b Key Laboratory of Biomass Chemical Engineering of Ministry of Education, Zhejiang University, Hangzhou 310027, China

10.1016/j.partic.2023.11.020

Volume 90, July 2024, Pages 98-105

Received 17 October 2023, Revised 4 November 2023, Accepted 14 November 2023, Available online 2 December 2023, Version of Record 26 December 2023.

E-mail: cjd007cn@163.com

Highlights

• Novel magnetic cross-linked α-amylase aggregates were successfully prepared.

• Resultant PEI/PDA-M-CLEAs and N-M-CLEAs exhibited excellent thermal stability, storage stability and pH stability.

• PEI/PDA-M-CLEAs and N-M-CLEAs exhibited higher starch hydrolysis efficiency than free α-amylase.

Abstract

In this work α-amylase was immobilized on magnetic Fe₃O₄ nanoparticles with polyethylenimine (PEI)/polydopamine (PDA) coating or 3-aminopropyl triethoxysilane (APTES) for the first time via adsorption–precipitation–cross-linking. Compared with the free α-amylase, the resultant magnetic cross-linked α-amylase aggregates (PEI/PDA-M-CLEAs and N-M-CLEAs) exhibited excellent thermal and storage stability as well as pH stability. After storage at 25 °C for 60 days, free α-amylase only retained 60% of its initial activity, while PEI/PDA-M-CLEAs and N-M-CLEAs retained 80% and 78% of their initial activities, respectively. Furthermore, N-M-CLEAs and PEI/PDA-M-CLEAs showed good reusability. After 6 repeated uses, PEI/PDA-M-CLEAs and N-M-CLEAs still maintained 65% and 62% of their initial activities, respectively. Especially, PEI/PDA-M-CLEAs and N-M-CLEAs exhibited higher starch hydrolysis efficiency than free α-amylase. The maximum dextrose equivalent (DE) values of starch hydrolysis by PEI/PDA-M-CLEAs and N-M-CLEAs reached 29.24% and 28.79% within 90 min, respectively. However, the maximum DE values of starch hydrolysis by the free α-amylase was only 27.89% even in 150 min. The magnetic cross-linked α-amylase aggregates could be introduced as effective biocatalyst for industrial applications in production of maltose syrups.

Graphical abstract

Keywords

α-amylase; Magnetic nanoparticles; Functional modification; Magnetic cross-linked enzyme aggregates; Hydrolysis of starch

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