Looking for breakthrough ideas for innovation challenges? Try Patsnap Eureka!

A kind of cross-linked biological enzyme catalyst and its application

A catalyst and bio-enzyme technology, applied in the direction of biochemical equipment and methods, enzymes, hydrolytic enzymes, etc., can solve the problems of affecting enzyme activity and mass transfer limitations, and achieve the effects of low price, easy availability of raw materials, and no environmental pollution

Active Publication Date: 2022-01-14
SHANGHAI NORMAL UNIVERSITY
View PDF4 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, most of the active sites of the prepared enzyme polymers are internal, which leads to severe mass transfer restrictions when they catalyze the reaction of macromolecular substrates, which affects the enzyme activity.

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • A kind of cross-linked biological enzyme catalyst and its application
  • A kind of cross-linked biological enzyme catalyst and its application
  • A kind of cross-linked biological enzyme catalyst and its application

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0029] Dissolve 50 mg of bovine serum albumin in 2 mL of phosphate buffer, add 1 mL of Candida antarctica lipase solution, stir well, add 1.083 g of ammonium sulfate and 30 μL of glutaraldehyde (50 wt %), and stir for 2 Centrifuge after 1 hour, collect the solid body, and wash repeatedly with phosphate buffer saline to obtain cross-linked enzyme aggregates. Then add 3 mL of phosphate buffer to disperse the cross-linked enzyme polymer, stir well, add 50 μL of glutaraldehyde (50 wt %), continue stirring for 30 minutes under ice-water bath conditions, add 1 mL of Candida antarctica lipase solution, and place on ice Stir in a water bath for 1 hour for the second cross-linking, wash after centrifugation, and freeze-dry in a freeze dryer. The sample is marked as Com-CLEAs-1, figure 1 It is the SEM picture of the prepared cross-linked biological enzyme catalyst.

Embodiment 2

[0031] Dissolve 100 mg of bovine serum albumin in 2 mL of phosphate buffer, add 1 mL of Candida antarctica lipase solution, stir well, add 1.083 g of ammonium sulfate and 30 μL of glutaraldehyde (50 wt %), and stir for 2 Centrifuge after 1 hour, collect the solid body, and wash repeatedly with phosphate buffer saline to obtain cross-linked enzyme aggregates. Then add 3 mL of phosphate buffer to disperse the cross-linked enzyme polymer, stir well, add 50 μL of glutaraldehyde (50 wt %), continue stirring for 30 minutes under ice-water bath conditions, add 1 mL of Candida antarctica lipase solution, and place on ice Stir in a water bath for 1 hour to carry out the second cross-linking, wash after centrifugation, and freeze-dry in a freeze dryer. The sample is marked as Com-CLEAs-2.

Embodiment 3

[0033] Dissolve 150 mg of bovine serum albumin in 2 mL of phosphate buffer, add 1 mL of Candida antarctica lipase solution, stir well, add 1.083 g of ammonium sulfate and 30 μL of glutaraldehyde (50 wt %), and stir for 2 Centrifuge after 1 hour, collect the solid body, and wash repeatedly with phosphate buffer saline to obtain cross-linked enzyme aggregates. Then add 3 mL of phosphate buffer to disperse the cross-linked enzyme polymer, stir well, add 50 μL of glutaraldehyde (50 wt %), continue stirring for 30 minutes under ice-water bath conditions, add 1 mL of Candida antarctica lipase solution, and place on ice Stir in a water bath for 1 hour to carry out the second cross-linking, wash after centrifugation, and freeze-dry in a freeze dryer. The sample is marked as Com-CLEAs-3.

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

PUM

PropertyMeasurementUnit
concentrationaaaaaaaaaa
Login to View More

Abstract

The invention relates to a cross-linked biological enzyme catalyst and its application. It is prepared by the following method: dissolving bovine serum albumin in a phosphate buffer to obtain a bovine serum albumin solution, and then adding candida antarctica lipase B solution and stirring , to obtain an enzyme-protein mixture, add a precipitant and a cross-linking agent, stir in an ice-water bath, collect the solid, wash the solid with a phosphate buffer to obtain a cross-linked enzyme polymer, add a phosphate buffer to disperse , then add a cross-linking agent, stir in an ice-water bath to obtain an aldehyde-modified cross-linked enzyme polymer, add Candida antarctica lipase B solution, stir in an ice-water bath, collect the product by centrifugation, wash, and freeze-dry After that, the product is obtained. The prepared cross-linked biological enzyme catalyst exhibits excellent catalytic activity in kinetic resolution and dynamic kinetic resolution of α-phenylethylamine, showing high stability, separable recovery, reusability, simple process and low price And so on a series of advantages.

Description

technical field [0001] The invention belongs to the technical field of catalysts, and in particular relates to a cross-linked biological enzyme catalyst and its application. Background technique [0002] α-Phenylethylamine is a very important chemical intermediate raw material, its optical single enantiomer (R)-α-Phenylethylamine and (S)-α-Phenylethylamine can not only be used as many racemic It is a chiral resolution reagent for organic acids, alcohols, esters or phenolic compounds. It can also be used as a chiral auxiliary agent and a chiral raw material for asymmetric synthesis. It has a wide range of uses. Derivatives of optically pure α-phenylethylamine are also widely used in the fields of medicine, spices, dyes and emulsifiers, and have very good application prospects. [0003] At present, optically pure α-phenylethylamine is mainly prepared by asymmetric synthesis and resolution. Asymmetric synthesis mainly introduces one or more molecules with chiral centers into ...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

Application Information

Patent Timeline
no application Login to View More
Patent Type & Authority Patents(China)
IPC IPC(8): C12N9/20C12P41/00C12P13/00
CPCC12N9/20C12P13/001C12P41/00C12Y301/01003
Inventor 李辉王萌封波李远华韩昕宸蓝梓桀顾华军
Owner SHANGHAI NORMAL UNIVERSITY
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Patsnap Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Patsnap Eureka Blog
Learn More
PatSnap group products

Browse by: Latest US Patents, China's latest patents, Technical Efficacy Thesaurus, Application Domain, Technology Topic, Popular Technical Reports.

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap|About US| Contact US: help@patsnap.com