Assembly of peptide linker to amino acid dehydrogenase and immobilized with metal-organic framework

被引:4
|
作者
Wang, Shiyan [1 ]
Duan, Lingxuan [1 ]
Jiang, Liang [1 ]
Liu, Kailong [1 ]
Wang, Shizhen [1 ,2 ]
机构
[1] Xiamen Univ, Dept Chem & Biochem Engn, Xiamen, Peoples R China
[2] Xiamen Univ, Key Lab Synthet Biotechnol Xiamen City, Xiamen, Peoples R China
基金
中国国家自然科学基金;
关键词
immobilization; enzymes; kinetics; chiral; biocatalysis; L-PHENYLALANINE DEHYDROGENASE; DRIVEN; ENZYME;
D O I
10.1002/jctb.6959
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
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 degrees 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. (c) 2021 Society of Chemical Industry (SCI).
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页码:741 / 748
页数:8
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