Assembly of peptide linker to amino acid dehydrogenase and immobilized with metal–organic framework. Issue 3 (1st November 2021)

• Record Type: Journal Article
• Authors: Wang, Shiyan; Duan, Lingxuan; Jiang, Liang; Liu, Kailong; Wang, Shizhen
• Is Part Of: Journal of chemical technology & biotechnology. Volume 97:Issue 3(2022)
• Page Start: 741
• Page End: 748
• Publication Date: 2021-11-01
• Subjects: immobilization -- enzymes -- kinetics -- chiral -- biocatalysis; Biotechnology -- Periodicals; Chemistry, Technical -- Periodicals; Chemical engineering -- Periodicals; Industries -- Environmental aspects -- Periodicals; 660
• DOI: 10.1002/jctb.6959
• Languages: English
• ISSNs: 0268-2575

Abstract

Abstract: BACKGROUND: The metal–organic framework (MOF) ZIF‐8 has the advantages of a large specific surface area and high stability. A new strategy for the assembly of amino acid dehydrogenase with peptide linker and for improving enzyme immobilization is proposed. RESULTS: Peptide linker enhanced enzyme activity after immobilization by 138.7%, and maintained 81.2% of its initial activity after seven recycles. The stability of PheDH_1D02/ZIF‐8 was greatly enhanced at 70–80 °C and pH 10–11. The catalytic efficiency of PheDH_1D02/ZIF‐8 was also enhanced compared with PheDH_1C1D/ZIF‐8 and two free enzymes. CONCLUSIONS: Metal ions coordinated with the peptide linker and reoriented immobilization of enzyme onto the MOF with high enzyme loading capacity were achieved. The mesoporous structure of PheDH_1D02/ZIF‐8 facilitates substrate diffusion. Combining the assembly of peptide linker and MOF immobilization is a simple, economical and efficient method for improving dehydrogenase stability. © 2021 Society of Chemical Industry (SCI).