Resolution of 1-Methyl-3-Amphetamine by Magnetic Fe3O4-APTES-CS2- Lipase in a Non-Aqueous Solvent

Hong Qian Dai; Yuan Lu; Zhi Hin Ou; Min Xu

doi:10.4028/www.scientific.net/MSF.1003.128

Paper Titles

Preparation and Characterization of a Low Density and Low Pressure Sheet Molding Compound
p.98

Application of Polyaluminum Chloride-Polyacrylamide as New Water Treatment Material for the Removal of Natural Organic Matter
p.109

Self-Assembly Synthesis of ZIF-8/Polyvinylidene Fluoride(PVDF) Hybrid Membrane and its Pd (II)-Ion Extraction Behavior
p.115

Preparation and Characteristic of Ultrafine Copper-Based Powders Reduced by a Two-Step Reduction Method
p.122

Resolution of 1-Methyl-3-Amphetamine by Magnetic Fe₃O₄-APTES-CS₂- Lipase in a Non-Aqueous Solvent
p.128

A Novel Method for Analyzing Pore Size Distribution of Complex Geometry Shaped Porous Shale
p.134

Polylactide-b-Poly(Ethylene Glycol)-b-Polylactide Triblock Copolymer Films for Using as Drug Delivery Carriers
p.144

Preparation and Application of Immobilized Cells on Amino Acid-Modified Magnetic Nanoparticles
p.150

Absorption Behavior of Methanol Vapor on the Silica Gels
p.156

HomeMaterials Science ForumMaterials Science Forum Vol. 1003Resolution of 1-Methyl-3-Amphetamine by Magnetic...

Resolution of 1-Methyl-3-Amphetamine by Magnetic Fe₃O₄-APTES-CS₂- Lipase in a Non-Aqueous Solvent

Abstract:

Fe₃O₄-APTES-CS₂ was prepared by modification of Fe₃O₄ with 3-aminopropyltriethoxysilane (APTES) and carbon disulfide (CS₂). Lipase was covalently bonded to Fe₃O₄-APTES-CS₂to obtain the immobilized lipase Fe₃O₄-APTES-CS₂-lipase. The textural characteristic of Fe₃O₄-APTES-CS₂-lipase was assessed by scanning electron microscopy. The optimal immobilization conditions were 2.5 mg/mL lipase, pH 7.0, 35 °C, 3 h. The loading amount of lipase was 119.0 mg/g carrier. The immobilization efficiency reached 57%. (R)-(+)-N-acetyl-1-methyl-3-amphetamine was synthesized by Fe₃O₄-APTES-CS₂-Li- pase. The conversion, enantiomeric excess of (R)-(+)-N-acetyl-1-methyl-3-amphet-a- mine and E value reached 36.8%, 98.5% and 132, respectivel.

You might also be interested in these eBooks

View Preview

Info:

Periodical:

Materials Science Forum (Volume 1003)

Pages:

128-133

DOI:

https://doi.org/10.4028/www.scientific.net/MSF.1003.128

Citation:

Cite this paper

Online since:

July 2020

Authors:

Hong Qian Dai, Yuan Lu, Zhi Hin Ou*, Min Xu

Keywords:

(R)-(+)-N-Acetyl-1-Methyl-3-Amphetamine, Enantioselective Acetylation, Magnetic Immobilized Lipase, Non-Aqueous Organic Solvent System

Export:

RIS, BibTeX

Price:

Permissions CCC:

Request Permissions

Permissions PLS:

Request Permissions

Сopyright:

Citation:

* - Corresponding Author

References

[1] P. Csuka, Z. Boros, L. Őrfi, J. Dobosd, L. Poppe, and G. Hornyánszky, Chemoenzymatic route to Tyrphostins involving lipase-catalyzed kinetic resolution of 1-phenylethanamine with alkyl cyanoacetates as novel acylating agents, Tetrahedron:Asymmetr, 2015, 26:644-649.

DOI: 10.1016/j.tetasy.2015.04.013

Google Scholar

[2] M.Oláh, Z. Boros, G. Hornyánszky, and L. Poppe, Isopropyl 2-ethoxyacetate-an efficient acylating agent for lipase-catalyzed kinetic resolution of amines in batch and continuous-flow modes, Tetrahedron, 2015, 72:7249-7255.

DOI: 10.1016/j.tet.2015.12.046

Google Scholar

[3] Zaki S S , M. S M , Saleh A A , Lipases in asymmetric transformations: Recent advances in classical kinetic resolution and lipase–metal combinations for dynamic processes, Coordination Chemistry Reviews, 2017, 348:54-70.

DOI: 10.1016/j.ccr.2017.08.008

Google Scholar

[4] Sanfilippo C , Paternò, Alfio Adriano, Patti A, Resolution of racemic amines via lipase-catalyzed benzoylation: Chemoenzymatic synthesis of the pharmacologically active isomers of labetalol, Molecular Catalysis, 2018, 449:79-84.

DOI: 10.1016/j.mcat.2018.02.017

Google Scholar

[5] Boros, Zoltán, Falus, Péter, Márkus, How the mode of Candida antarctica lipase B immobilization affects the continuous-flow kinetic resolution of racemic amines at various temperatures, Journal of Molecular Catalysis B: Enzymatic, 2013, 85-86:119-125.

DOI: 10.1016/j.molcatb.2012.09.004

Google Scholar

[6] S.L Gilani, G.D Najafpour , A. Moghadamnia, and A.H. Kamaruddinc, Stability of immobilized porcine pancreas lipase on mesoporous chitosan beads: A comparative study. J Mol Catal B Enzym, 2016, 133:144-153.

DOI: 10.1016/j.molcatb.2016.08.005

Google Scholar

[7] B.B. Romdhane, Z.B. Romdhane, A. Gargouri, and H. Belghith, Esterification activity and stability of Talaromyces thermophilus lipase immobilized onto chitosan, Mol Catal B Enzym, 2011, 68:230-239.

DOI: 10.1016/j.molcatb.2010.11.010

Google Scholar

[8] Mohamad Hajar, Farzaneh Vahabzadeh, Biolubricant production from castor oil in a magnetically stabilized fluidized bed reactor using lipase immobilized on Fe3O4 nanoparticles, Industrial Crops & Products, 2016, 94:544-556.

DOI: 10.1016/j.indcrop.2016.09.030

Google Scholar