+ Site Statistics
References:
54,258,434
Abstracts:
29,560,870
PMIDs:
28,072,757
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

CALB Immobilized onto Magnetic Nanoparticles for Efficient Kinetic Resolution of Racemic Secondary Alcohols: Long-Term Stability and Reusability



CALB Immobilized onto Magnetic Nanoparticles for Efficient Kinetic Resolution of Racemic Secondary Alcohols: Long-Term Stability and Reusability



Molecules 24(3)



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.

Please choose payment method:






(PDF emailed within 0-6 h: $19.90)

Accession: 066446178

Download citation: RISBibTeXText

PMID: 30704049

DOI: 10.3390/molecules24030490


Related references

Lipase immobilized in ordered mesoporous silica: A powerful biocatalyst for ultrafast kinetic resolution of racemic secondary alcohols. Process Biochemistry 53: 102-108, 2017

Improved activity of lipase immobilized in microemulsion-based organogels for ( R , S )-ketoprofen ester resolution: Long-term stability and reusability. Biotechnology Reports 7: 1-8, 2015

Efficient dynamic kinetic resolution of racemic secondary alcohols by a chemoenzymatic system using bifunctional iridium complexes with C-N chelate amido ligands. Chemical Communications 48(30): 3635-3637, 2012

Magnetic Attachment of Lipase Immobilized on Bacteriogenic Iron Oxide Inside a Microtube Reactor for the Kinetic Resolution of Secondary Alcohols. Synlett 28(07): 805-810, 2017

Improvement of stability and reusability of α-amylase immobilized on naringin functionalized magnetic nanoparticles: A robust nanobiocatalyst. International Journal of Biological Macromolecules 113: 354-360, 2018

Stability, Scalability, and Reusability of a Volume Efficient Biocatalytic System Constructed on Magnetic Nanoparticles. Catalysis Science and Technology 6(7): 2361-2369, 2016

A mesoporous-silica-immobilized oxovanadium cocatalyst for the lipase-catalyzed dynamic kinetic resolution of racemic alcohols. Angewandte Chemie 52(13): 3654-3658, 2013

An efficient resolution of racemic secondary alcohols on magnetically separable biocatalyst. Biochemical and Biophysical Research Communications 365(4): 609-613, 2007

Kinetic resolution of racemic secondary alcohols catalyzed by chiral diaminodiphosphine-Ir(I) complexes. Organic Letters 8(24): 5565-5567, 2006

Oxidative kinetic resolution of racemic secondary alcohols in water with chiral PNNP/Ir catalyst. Green Chemistry 14(5): 1289-0, 2012

Remote ester group leads to efficient kinetic resolution of racemic aliphatic alcohols via asymmetric hydrogenation. Journal of the American Chemical Society 136(50): 17426-9, 2015

Highly stereoselective synthesis of Z-homoallylic alcohols by kinetic resolution of racemic secondary allyl boronates. Angewandte Chemie 52(20): 5338-5341, 2013

A polymer-supported proline-based diamine catalyst for the kinetic resolution of racemic secondary alcohols. Journal of Organic Chemistry 66(3): 868-873, 2001

Aerobic oxidative kinetic resolution of racemic secondary alcohols with chiral bifunctional amido complexes. Angewandte Chemie 47(13): 2447-2449, 2008

Oxidative kinetic resolution of racemic secondary alcohols catalyzed by recyclable chiral dimeric Mn(III) salen catalysts. Journal of Molecular Catalysis A: Chemical 274(1-2): 120-126, 2007