scholarly journals Efficient and Stable Magnetic Chitosan-Lipase B from Candida Antarctica Bioconjugates in the Enzymatic Kinetic Resolution of Racemic Heteroarylethanols

Molecules ◽  
2020 ◽  
Vol 25 (2) ◽  
pp. 350 ◽  
Author(s):  
Cristina Georgiana Spelmezan ◽  
László Csaba Bencze ◽  
Gabriel Katona ◽  
Florin Dan Irimie ◽  
Csaba Paizs ◽  
...  

Lipase B from Candida antarctica immobilized by covalent binding on sebacoyl-activated chitosan-coated magnetic nanoparticles proved to be an efficient biocatalyst (49.2–50% conversion in 3–16 h and >96% enantiomeric excess) for the enzymatic kinetic resolution of some racemic heteroarylethanols through transesterification with vinyl acetate. Under optimal conditions (vinyl acetate, n-hexane, 45 °C), the biocatalyst remains active after 10 cycles.

Molecules ◽  
2019 ◽  
Vol 24 (3) ◽  
pp. 490 ◽  
Author(s):  
Xiu Xing ◽  
Jun-Qi Jia ◽  
Jing-Fan Zhang ◽  
Zi-Wen Zhou ◽  
Jun Li ◽  
...  

In this study, an immobilization strategy for magnetic cross-linking enzyme aggregates of lipase B from Candida antarctica (CALB) was developed and investigated. Magnetic particles were prepared by conventional co-precipitation. The magnetic nanoparticles were modified with 3-aminopropyltriethoxysilane (APTES) to obtain surface amino-functionalized magnetic nanoparticles (APTES–Fe3O4) as immobilization materials. Glutaraldehyde was used as a crosslinker to covalently bind CALB to APTES–Fe3O4. The optimal conditions of immobilization of lipase and resolution of racemic 1-phenylethanol were investigated. Under optimal conditions, esters could be obtained with conversion of 50%, enantiomeric excess of product (eep) > 99%, enantiomeric excess of substrate (ees) > 99%, and enantiomeric ratio (E) > 1000. The magnetic CALB CLEAs were successfully used for enzymatic kinetic resolution of fifteen secondary alcohols. Compared with Novozym 435, the magnetic CALB CLEAs exhibited a better enantioselectivity for most substrates. The conversion was still greater than 49% after the magnetic CALB CLEAs had been reused 10 times in a 48 h reaction cycle; both ees and eep were close to 99%. Furthermore, there was little decrease in catalytic activity and enantioselectivity after being stored at −20 °C for 90 days.


2020 ◽  
Vol 43 (12) ◽  
pp. 2253-2268 ◽  
Author(s):  
Ticiane C. de Souza ◽  
Thiago de Sousa Fonseca ◽  
Jouciane de Sousa Silva ◽  
Paula J. M. Lima ◽  
Carlos A. C. G. Neto ◽  
...  

Author(s):  
Cristian Andrei Gal ◽  
Laura Edit Barabas ◽  
Judith Hajnal Bartha-Vari ◽  
Madalina Elena Moisa ◽  
Diana Balogh-Weiser ◽  
...  

An efficient nanobioconjugate of lipase B from Candida antarctica was prepared by the covalent binding on carboxy-functionalized single-walled carbon nanotubes and tested in batch and flow mode for the enzymatic...


Crystals ◽  
2020 ◽  
Vol 10 (5) ◽  
pp. 404
Author(s):  
Jarosław Błaszczyk ◽  
Piotr Kiełbasiński

Lipase B from Candida antarctica (CAL-B) belongs to the family of α/β-hydrolases, and is one from the most extensively used biocatalysts in the kinetic resolution of amines and alcohols in a racemic state, in the desymmetrization of diacetates or diols, and in the stereoselective synthesis of chiral intermediate compounds for obtaining the various pharmaceuticals and agents which protect plants. There are also many cases of promiscuous reactions catalyzed by CAL-B. The number of very important results appeared recently in the literature in the years 2015–2019, regarding the crystal structure and conformation of CAL-B molecule. Before 2015, there was a long period of a complete lack of information concerning this enzyme’s structure. The earlier reports about CAL-B structure were dated between 1994–1995, and did not provide enough conclusions about the mechanism of the enzyme. The recently solved structures give a hint of the enzyme mechanism in three dimensions.


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