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

A kind of immobilization method of Candida antarctica lipase b

A technology of Candida Antarctica and lipase, applied in the field of enzyme engineering, can solve problems such as loss, and achieve the effects of convenient operation, good temperature stability and solvent tolerance, and simple preparation conditions

Active Publication Date: 2021-08-24
ZHEJIANG UNIV OF TECH
View PDF5 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Although MOFs can improve many properties of enzymes, MOFs itself is a powdery substance, which is easily absorbed by materials during the experimental operation and causes loss.

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 immobilization method of Candida antarctica lipase b
  • A kind of immobilization method of Candida antarctica lipase b
  • A kind of immobilization method of Candida antarctica lipase b

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0023] Example 1 Immobilization conditions and lipase activity assay method of Candida antarctica lipase B

[0024] Add dimethylimidazole and zinc nitrate to deionized water respectively, and sonicate at 40 Hz for 20 minutes to prepare 0.3125 mol / L dimethylimidazole aqueous solution and 0.3125 mol / L zinc nitrate aqueous solution respectively. Take 60mL0.3125mol / L dimethylimidazole aqueous solution, 1.5mL0.3125mol / L zinc nitrate aqueous solution and 3mL Candida antarctica lipase B enzyme solution (Novozymes, Denmark) CALB, enzyme amount 72mg / ml, 4166.67U / ml) were mixed to obtain a mixed enzyme liquid, and reacted with magnetic stirring at 25°C and 200rpm for 30min to obtain a reaction liquid containing MOFs (CALB-ZIF-8) complex. Add 0.5g of macroporous resin D101-1 and 2.5mL of 25% polyvinylimide (PEI) aqueous solution to the reaction solution, conduct crosslinking reaction at 30°C and 200rpm in a water bath for 5 hours, and vacuum After suction filtration, the filter cake wa...

Embodiment 2

[0031] The ratio and the concentration of the solution used in the preparation process of the immobilized enzyme of embodiment 2 have an impact on the enzyme activity

[0032] Zinc nitrate aqueous solution volume is set as 1.0mL-2.4mL among the embodiment 1, other operation and condition are identical with embodiment 1, and the result is as shown in table 1, and the optimum volume ratio of dimethylimidazole aqueous solution and zinc nitrate aqueous solution is 40: 1.

[0033] Table 1: Specific enzyme activity results of different volumes of zinc nitrate aqueous solution

[0034]

Embodiment 3

[0035] The impact of the amount of enzyme liquid used in the preparation process of embodiment 3 immobilized enzyme on enzyme activity

[0036] The volume of Candida antarctica lipase B enzyme liquid in Example 1 is set to 1-6ml, other operations and conditions are the same as in Example 1, the results are as shown in Table 2, the optimal value of adding enzyme liquid is 3mL (72mg / ml).

[0037] Table 2 The specific enzyme activity results of different volumes of enzyme solution

[0038]

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

No PUM Login to View More

Abstract

The invention discloses a method for immobilizing Candida antarctica lipase B. In the method, dimethylimidazole aqueous solution, zinc nitrate aqueous solution and Candida antarctica lipase B are mixed under the conditions of 25° C. and 200 rpm magnetic stirring React for 30 minutes, then add non-polar macroporous adsorption resin and cross-linking agent, conduct cross-linking reaction at 15-45°C and 200 rpm water bath for 5 hours, filter with vacuum filter, and dry the filter cake to obtain immobilized Candida antarctica Lipase B: Compared with the existing commodity immobilized lipase on the market, the immobilized lipase prepared by the present invention has higher enzyme activity, so the enzyme immobilization method has a good industrial application prospect.

Description

[0001] (1) Technical field [0002] The invention belongs to the field of enzyme engineering and relates to an immobilization method of Candida antarctica lipase B. [0003] (2) Background technology [0004] Lipase (Lipase, EC3.1.1.3, glyceryl ester hydrolase) belongs to carboxyl ester hydrolase, which can gradually hydrolyze triglyceride into glycerol and fatty acid, and also decompose, esterify, and esterify ester compounds. Exchange, lactone synthesis, peptide synthesis, ester polymerization and acylation reactions. Lipase exists in fat-containing animal, plant and microbial (such as mold, bacteria, etc.) tissues. Candida antarctica lipase B (CALB) is an important lipase. Candida antarctica lipase B is widely used in optically active drugs, structural lipids with special physiological functions, fine chemicals, chiral compounds and biodiesel, and has great application value. [0005] The lipase-catalyzed reaction has the characteristics of mild reaction conditions, high ...

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): C12N11/14C12N11/089
CPCC12N9/20C12N11/08C12N11/14C12Y301/01003
Inventor 郑建永蔡鑫勇章银军汪钊
Owner ZHEJIANG UNIV OF TECH
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