A nanorod-like lanthanum
metal–organic
framework (LaMOF) was synthesized in aqueous solution by coordinating
La(III) to the ligand 1,3,5-benzenetricarboxylic acid. The fibrous
LaMOF was fabricated by splitting the nanorod-like LaMOF in a solution
of
d
-amino acid oxidase, and the enzyme was immobilized simultaneously.
Based on SEM and TEM images, STEM mapping, and spectra of XPS and
FTIR, the mechanism of formation of the fibrous LaMOF and the distinct
interfacial phenomena have been elucidated. The fabrication of the
fibrous LaMOF and simultaneous immobilization of the enzyme were carried
out in aqueous solutions at room temperature, without using any organic
solvent. It is a clean and time- and energy-effective process. This
work presents a distinct and clean methodology for the fabrication
of the fibrous MOF. Potentially, the environmentally benign methodology
can be extended to immobilize other enzymes.
Dehaloperoxidase (DHP) catalyzes detoxifying halophenols. It is a heme-containing enzyme using H 2 O 2 as the oxidant. Heme bleaching from the active site is of great concern. In addition, the interference of DHP by H 2 O 2 leads to the inactivation of the enzyme. To solve these two problems, DHP is coordinated to Zn (II) in PBS buffer to form a biomineralized composite (DHP&Zn-CP). DHP&Zn-CP was characterized by measuring SEM and confocal images, as well as energy dispersive X-ray spectrometry mapping. Fluorescence spectra demonstrated that DHP&Zn-CP can prevent heme bleaching. Two-dimensional FTIR spectra were measured, dynamically providing insight into the structural change of DHP along the coordination process. Raman spectra were performed to analyze the structural change. The optical spectra confirmed that the forming of DHP&Zn-CP had a little effect on the structures of DHP. For the dehalogenation of 2,4,6-trichlorophenol, DHP&Zn-CP can tolerate the presence of H 2 O 2 and is resistant to the interference by H 2 O 2. The catalytic efficiency of DHP&Zn-CP is much higher than that of free DHP.
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