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A kind of hmfo@mofs composite material and its preparation method and application

A technology of composite materials and mixing temperature, applied in biochemical equipment and methods, fixed on/in organic carriers, fermentation, etc., can solve the problems of lack of structural properties and mechanisms, and achieve good stability and reusability performance, low energy consumption, and high enzyme loading capacity

Active Publication Date: 2022-03-11
DALIAN INST OF CHEM PHYSICS CHINESE ACAD OF SCI
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Since the choice of immobilization carrier needs to comprehensively consider the molecular size, amino acid composition, structural characteristics and physical and chemical properties of the target enzyme, so far there is no general immobilization method for a certain type of enzyme, and there is still a lack of broader structural properties and mechanism research.

Method used

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  • A kind of hmfo@mofs composite material and its preparation method and application
  • A kind of hmfo@mofs composite material and its preparation method and application
  • A kind of hmfo@mofs composite material and its preparation method and application

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0035] Preparation process of 5-hydroxymethylfurfural oxidase

[0036]1. Synthesize the 5-hydroxymethylfurfural oxidase gene (sequence list 1), and connect the 5-hydroxymethylfurfural oxidase gene to the pPICZa-A expression vector with restriction endonucleases XhoI and XbaI. Ligation was performed overnight with T4 ligase. Take 5 μL of the connection solution and transform it into Escherichia coli Top10, spread it on a resistance plate containing ampicillin and culture it overnight at 37°C for 12-15h. Pick 10 large and scattered single colonies on the ampicillin plate for colony PCR identification, analyze the products by agarose gel electrophoresis, continue to culture the colonies containing the target band, extract the plasmid, and perform sequencing analysis.

[0037] 2. Plasmid extraction: Centrifuge the bacterial solution at 5000rpm for 5min. Remove the supernatant and precipitate the plasmid with a plasmid kit.

[0038] The extracted plasmid was subjected to double ...

Embodiment 2

[0060] Preparation process of HMFO@MOFs

[0061] Take 2.0mL 2-methylimidazole (160.0mM) solution, add 0.5mL HMFO (1.0mg / mL) solution, mix evenly, add 2.0mL zinc acetate solution with a concentration of 40.0mM, stir at 25°C for 30min and let stand for 12h, the obtained The solid was washed 3 times with deionized water to obtain HMFO@MOFs.

[0062] Add an appropriate amount of glacial acetic acid to dissolve the HMFO@MOFs prepared in Example 2, add a mixed solution of ethanol and acetone with a volume ratio of 1:1 according to the volume ratio of 4:1, place it at -20°C for 2 hours, centrifuge, discard the supernatant, and use Wash the precipitate three times with absolute ethanol, add 2.0% SDS to dissolve it ultrasonically, take 40 μL of protein solution and 10.0 μL of sample buffer (5×), mix well, boil for 10 min, and take the supernatant for SDS-PAGE determination ( Figure 4 , M is the standard protein molecule, band 1 is the supernatant during preparation, and band 2 is HMF...

Embodiment 3

[0067] Preparation process of HMFO@MOFs

[0068] Take 2.0mL of 2-methylimidazole (160.0mM) solution, add 0.5mL of HMFO (2.0mg / mL) solution, mix evenly, add 2.0mL of zinc acetate solution with a concentration of 40mM, stir at 25°C for 10min, and let stand for 18h to obtain The solid was washed 3 times with deionized water to obtain HMFO@MOFs.

[0069] Add an appropriate amount of glacial acetic acid to dissolve the HMFO@MOFs prepared in Example 3, add a mixed solution of ethanol and acetone with a volume ratio of 1:1 according to the volume ratio of 4:1, place it at -20°C for 2 hours, centrifuge, discard the supernatant, and use Wash the precipitate three times with absolute ethanol, add 2.0% SDS to dissolve it ultrasonically, take 40 μL of protein solution and 10.0 μL of sample buffer (5×), mix well, boil for 10 min, and take the supernatant for SDS-PAGE determination ( Figure 6 , M is the standard protein molecule, band 1 is the supernatant during preparation, band 2 is HMF...

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Abstract

The present invention relates to inorganic organic nanometer catalyst and application field thereof, specifically 2-methylimidazole, zinc ion and 5-hydroxymethylfurfural oxidase (5-hydroxymethylfurfural oxidase, HMFO) prepare a kind of novel fan-shaped multi-layered nano flower The structure of the composite material is different from the classic rhombic dodecahedron of ZIF‑8, but the fan-shaped nanoflower structure is composed of multiple sheets, which is more conducive to the diffusion of small molecules and the transfer of substrates, and is conducive to improving the catalytic performance. efficiency. The technical scheme adopted in the invention uses aqueous solution as a solvent, does not contain organic solvents, and is environmentally friendly. The reaction only needs to be carried out at room temperature, the energy consumption is small, and it is simple and convenient. The HMFO@MOFs composite of the present invention retains the catalytic activity of HMFO, can catalyze HMF to generate a series of high value-added products, and has application value.

Description

technical field [0001] The present invention relates to inorganic-organic nanocatalysts and their application fields, in particular to a composite material of MOFs immobilized with 5-hydroxymethylfurfural oxidase and its preparation method and a method for catalyzing 5-hydroxymethylfurfural to generate a series of high value-added compounds application. [0002] technical background [0003] Free enzymes have unique characteristics of high selectivity, high catalytic activity, mild conditions, and environmental protection, and are widely used in chemical, pharmaceutical, and food fields. However, the stability of the free enzyme is not good, and recovery is difficult, which limits its industrial application. In order to solve the problems of free enzymes, the technology of immobilized enzymes emerged and developed continuously. At present, the research on immobilized enzymes on new materials mainly focuses on many model enzymes, including glucose oxidase, horseradish peroxi...

Claims

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Application Information

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Patent Type & Authority Patents(China)
IPC IPC(8): C12N11/089C12N9/04C12P17/04C08G83/00
CPCC12N11/02C12N11/08C12N9/0006C12Y101/03C12P17/04C08G83/008
Inventor 尹恒巩凤芹
Owner DALIAN INST OF CHEM PHYSICS CHINESE ACAD OF SCI
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