Recombinant INANE1 (rINANE1), a recombinant intracellular GDSL-type esterase from Aspergillus niger GZUF36, has high acetate substrate specificity. Here, rINANE1 was successfully immobilized on polydopamine (PDA)-modified magnetic ferric oxide nanoparticles (FeONPs) by adsorption-precipitation-cross-linking to obtain cross-linked enzyme aggregate (CLEA)-rINANE1-FeO@PDA. FeO, FeO@PDA, and CLEA-rINANE1-FeO@PDA were characterized by scanning electron microscopy, X-ray diffraction, vibrating-sample magnetometry, Fourier transform infrared (FTIR) spectroscopy, and zeta potential analysis. Upon immobilization, CLEA-rINANE1-FeO@PDA, with a protein loading of 72.72 ± 1.01 mg/g, reached optimal activity recovery of 104.40 % ± 1.14 %. FTIR analysis showed that immobilization increased the relative content of β-folding in rINANE1 by 12.25 % and reduced irregular curl by 4.16 %, rendering the structure more orderly. Specifically, under an alkaline condition (pH 10), CLEA-rINANE1-FeO@PDA performed over 100 % of initial activity. The optimum temperature increased by 5 °C, and over 55 % of the initial activity was observed after 12 h at 55 °C. CLEA-rINANE1-FeO@PDA showed over 40 % of its relative activity, whereas free rINANE1 showed <10 % in acetonitrile. In addition, the relative activity of CLEA-rINANE1-FeO@PDA was retained at about 80 % after eight cycles and maintained at 109 % after 45 days. The PDA-modified magnetic ferrite nanoparticles exhibited excellent stability and recyclability, providing a new avenue for developing industrial biocatalysts.
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The synthesis of cinnamyl acetate and deacetyl-7-aminocephalosporanic acid by a GDSL-type esterase and its substrate specificity analysis.
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