Kinetic Resolution of (<i>R,S</i>)-1-chloro-3-(1-naphthyloxy) -2-Propanol in an Immobilized Lipase Bioreactor

Fang-Di Cong; Jie Kang; Wu-Dan Bi; Tao Li; Ping Li

doi:doi:10.11648/j.bmb.20160103.12

| Peer-Reviewed

Kinetic Resolution of (R,S)-1-chloro-3-(1-naphthyloxy) -2-Propanol in an Immobilized Lipase Bioreactor

Fang-Di Cong, Jie Kang, Wu-Dan Bi, Tao Li, Ping Li

Published in Biochemistry and Molecular Biology (Volume 1, Issue 3)

Received: 30 October 2016 Accepted: 15 November 2016 Published: 14 December 2016

Views: Downloads:

Download PDF

Share This Article

Twitter
Linked In
Facebook

Abstract

A bioreactor with Pseudomonas cepacia lipase (PCL) immobilized on the inner wall was conveniently prepared by adding lipase powder and the right amount of water to a conical flask and keeping it with mouth open in an incubator shaker at 37°C and 170 rpm for more than 10 h. The bioreactor was employed on resolution of (R, S)-1-chloro-3-(1-naphthyloxy)-2-propanol by catalyzing transesterification of it with vinyl acetate. It was showed that the wall-PCL behaved an excellent catalytic activity being 10 folds of native PCL in terms of conversion, and high enantioselectivity E = 110. And also the depressed activity of immobilized PCL owing to frequently use in organic phase could be reactivated easily by again shaking bioreactor under the aforesaid conditions after adding water. The enhanced activity was attributed to the simulation on interfacial activation mechanism of lipases at water/oil interface.

Published in	Biochemistry and Molecular Biology (Volume 1, Issue 3)
DOI	10.11648/j.bmb.20160103.12
Page(s)	34-38
Creative Commons	This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited.
Copyright	Copyright © The Author(s), 2024. Published by Science Publishing Group

Keywords

Lipase, Activity, Enantioselectivity, Immobilization, Pseudomonas Cepacia Lipase, Bioreactor

References

[1]	Kapoor M, Anand N, Koul S, Chimni SS, Manhas KS, Raina C, Parshad R, Taneja SC, Qazi GN. Kinetic resolution of 1-chloro-3-(1-naphthyloxy)-2-propanol, an intermediate in the synthesis of b-adrenergic receptor blockers. Bioorg Chem 2003; 31: 259-69.
[2]	Shum WP. Process for producing optically active epoxy alcohol derivatives. United States Patent 5,252,759 (1993).
[3]	Wang YF, Chen ST, Liu KKC, Wong CH. Lipase-catalyzed irreversible transesterification using enol esters: resolution of cyanohydrins and syntheses of ethyl (R)-2-hydroxy-4-phenylbutyrate and (S)-propranolol. Tetrahedron lett 1989; 30: 1917-20.
[4]	Matsuo M, Ohno N. Preparation of optically active l-acetoxy-2-aryloxypropionitriles and its application to a facile synthesis of (S)-(-)-propanolol. Tetrahedron lett 1985; 26: 5533-4.
[5]	Lagos FM, Campo CD, Llama EF, Sinisterra JV. New yeast strains for enantioselective production of halohydrin precursor of (S)-Propranolol. Enzyme Microb Tech 2002; 30: 895-901.
[6]	Lagos FM, Carballeira JD, Bermudez JL, Alvarezb E, Sinisterra JV. Highly stereoselective reduction of haloketones using three new yeasts: application to the synthesis of (S)-adrenergic β-blockers related to propranolol. Tetrahedron-Asymmetr 2004; 15: 763-70.
[7]	Klunder JM, Ko SY, Sharpless KB. Asymmetric Epoxidation of Allyl Alcohol: Efficient Routes to Homochiral b-Adrenergic Blocking Agents. J Org Chem 1986; 51: 3710-2.
[8]	Sharpless KB, Klunder JM. Optically active derivatives of glycidol. United States Patent 5,344,947 (1994).
[9]	Kirchner G, Scollar MP, Klibanov AM. Resolution of racemic mixture via Lipase catalysis in organic solvents. J Am Chem Soc 1985; 107:7072-6.
[10]	Chiou TW, Chang CC, Lai CT, Tai DF. Kinetic resolution of propranolol by a lipase-catalyzed N-acetylation. Bioorg Med Chem lett 1997; 7: 433-6.
[11]	Bevinakatti HS, Banerji AA. Practical Chemoenzymatic synthesis of both enantiomers of propranolol. J Org Chem 1991; 56: 5372-5.
[12]	Tang L, Su M, Yan J, Xie S, Zhang W. Lid hinge region of Penicillium expansum lipase affects enzyme activity and interfacial activation, Process Biochem 2015; 50: 1218-122.
[13]	R. Verger. ‘Interfacial activation’ of lipases: facts and artifacts. Trends Biotechnol 1997; 15: 32-8.
[14]	Dachuri V, Boyineni J, Choi S, Chung HS, Jang SH, Lee CW, Organic solvent-tolerant, cold-adapted lipases PML and LipS exhibit increased conformational flexibility in polarorganic solvents, J Mol Catal B-Enzym 2016;131:73-78
[15]	[15] Klibanov AM. Why are enzymes less active in organic solvents than in water. Trends Biotechnol 1997; 15: 97-101.
[16]	[16] Garcia-Viloca M, Gao J, Karplus M, Truhlar DG. How enzymes work: analysis by mordern rate theory and computer simulations. Science 2004; 303: 186-95.
[17]	Balcao VM, Paiva AL, Malcata FX. Bioreactor with immobilized lipases: state of the art. Enzyme Microb Tech 1996; 18: 392-416.
[18]	Nguyen BV. Chiral Building Blocks for Synthesis of Pine Sawfly Sex Pheromones. Doctoral Thesis 2000.
[19]	Kim KK, Song HK, Shin DH, Hwang KY, Suh SW. The crystal structure of a triacylglycerol lipase from Pseudomonas cepacia reveals a highly open conformation in the absence of a bound inhibitor. Struct 1997; 5: 173-85.
[20]	Schrag JD, Li Y, Cygler M, Lang D, Burgdorf T, Hecht HJ, Schmid R, Schomburg D, Rydel TJ, Oliver JD, Strickland LC, Dunaway CM, Larson SB, Day J, McPherson A. The open conformation of a Pseudomonas lipase. Struct 1997; 5: 187-202.
[21]	Gonzalez-Navarro H, Braco L. Improving lipase activity in solvent-free media by interfacial activation-based molecular bioimprinting. J Mol Catal B-Enzym 1997;3:111-9
[22]	Martinez F, Campo CD, Sinisterra JV, Llama EF. Preparation of halohydrin β-blocker precursors using yeast-catalysed reduction. Tetrahedron-Asymmetr 2000; 11: 4651-60.
[23]	Bermudez JL, Campo CD, SalazarL, Llama EF, Sinisterra JV. A new application of Candida Antarctica Lipase for obtaining Natural Homochiral BBAs aryloxypropanolamine. Tetrahedron-Asmmetr 1996; 7: 2485-8.
[24]	Muller PK. Process of manufacturing enzyme preparation rich in lipase. United States Patent 4,088,539 (1978).
[25]	Kokusho Y, Machida H, Iwasaki S. Microbial lipase, process for its preparation and microbiologically pure culture therefore. United States Patent 4,283,494 (1981).
[26]	Zamana MM, Hayashia Y, Talukderb MMR, Kawanishia T. Enhanced activity and stability of Chromobacterium viscosum lipase in AOT reverse micellar systems by pretreatment with acetone. J Mol Catal B-Enzym 2005; 32: 149-55.
[27]	Rotticci D. Understanding and Engineering the Enantioselectivity of Candida Antarctica Lipase B towards sec-Alcohols. ISBN: 91-7170-550-3, Stockholm; 2000.

Cite This Article

Plain Text BibTeX RIS

APA Style

Fang-Di Cong, Jie Kang, Wu-Dan Bi, Tao Li, Ping Li. (2016). Kinetic Resolution of (R,S)-1-chloro-3-(1-naphthyloxy) -2-Propanol in an Immobilized Lipase Bioreactor. Biochemistry and Molecular Biology, 1(3), 34-38. https://doi.org/10.11648/j.bmb.20160103.12

Copy | Download

ACS Style

Fang-Di Cong; Jie Kang; Wu-Dan Bi; Tao Li; Ping Li. Kinetic Resolution of (R,S)-1-chloro-3-(1-naphthyloxy) -2-Propanol in an Immobilized Lipase Bioreactor. Biochem. Mol. Biol. 2016, 1(3), 34-38. doi: 10.11648/j.bmb.20160103.12

Copy | Download

AMA Style

Fang-Di Cong, Jie Kang, Wu-Dan Bi, Tao Li, Ping Li. Kinetic Resolution of (R,S)-1-chloro-3-(1-naphthyloxy) -2-Propanol in an Immobilized Lipase Bioreactor. Biochem Mol Biol. 2016;1(3):34-38. doi: 10.11648/j.bmb.20160103.12

Copy | Download

@article{10.11648/j.bmb.20160103.12,
  author = {Fang-Di Cong and Jie Kang and Wu-Dan Bi and Tao Li and Ping Li},
  title = {Kinetic Resolution of (R,S)-1-chloro-3-(1-naphthyloxy) -2-Propanol in an Immobilized Lipase Bioreactor},
  journal = {Biochemistry and Molecular Biology},
  volume = {1},
  number = {3},
  pages = {34-38},
  doi = {10.11648/j.bmb.20160103.12},
  url = {https://doi.org/10.11648/j.bmb.20160103.12},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.bmb.20160103.12},
  abstract = {A bioreactor with Pseudomonas cepacia lipase (PCL) immobilized on the inner wall was conveniently prepared by adding lipase powder and the right amount of water to a conical flask and keeping it with mouth open in an incubator shaker at 37°C and 170 rpm for more than 10 h. The bioreactor was employed on resolution of (R, S)-1-chloro-3-(1-naphthyloxy)-2-propanol by catalyzing transesterification of it with vinyl acetate. It was showed that the wall-PCL behaved an excellent catalytic activity being 10 folds of native PCL in terms of conversion, and high enantioselectivity E = 110. And also the depressed activity of immobilized PCL owing to frequently use in organic phase could be reactivated easily by again shaking bioreactor under the aforesaid conditions after adding water. The enhanced activity was attributed to the simulation on interfacial activation mechanism of lipases at water/oil interface.},
 year = {2016}
}

Copy | Download

TY  - JOUR
T1  - Kinetic Resolution of (R,S)-1-chloro-3-(1-naphthyloxy) -2-Propanol in an Immobilized Lipase Bioreactor
AU  - Fang-Di Cong
AU  - Jie Kang
AU  - Wu-Dan Bi
AU  - Tao Li
AU  - Ping Li
Y1  - 2016/12/14
PY  - 2016
N1  - https://doi.org/10.11648/j.bmb.20160103.12
DO  - 10.11648/j.bmb.20160103.12
T2  - Biochemistry and Molecular Biology
JF  - Biochemistry and Molecular Biology
JO  - Biochemistry and Molecular Biology
SP  - 34
EP  - 38
PB  - Science Publishing Group
SN  - 2575-5048
UR  - https://doi.org/10.11648/j.bmb.20160103.12
AB  - A bioreactor with Pseudomonas cepacia lipase (PCL) immobilized on the inner wall was conveniently prepared by adding lipase powder and the right amount of water to a conical flask and keeping it with mouth open in an incubator shaker at 37°C and 170 rpm for more than 10 h. The bioreactor was employed on resolution of (R, S)-1-chloro-3-(1-naphthyloxy)-2-propanol by catalyzing transesterification of it with vinyl acetate. It was showed that the wall-PCL behaved an excellent catalytic activity being 10 folds of native PCL in terms of conversion, and high enantioselectivity E = 110. And also the depressed activity of immobilized PCL owing to frequently use in organic phase could be reactivated easily by again shaking bioreactor under the aforesaid conditions after adding water. The enhanced activity was attributed to the simulation on interfacial activation mechanism of lipases at water/oil interface.
VL  - 1
IS  - 3
ER  -

Copy | Download

Author Information

Fang-Di Cong

Department of Biopharmaceuticals, College of Basic Sciences, Tianjin Agricultural University, Tianjin, China
Jie Kang

Department of Biopharmaceuticals, College of Basic Sciences, Tianjin Agricultural University, Tianjin, China
Wu-Dan Bi

Department of Biopharmaceuticals, College of Basic Sciences, Tianjin Agricultural University, Tianjin, China
Tao Li

Department of Biopharmaceuticals, College of Basic Sciences, Tianjin Agricultural University, Tianjin, China
Ping Li

Department of Biopharmaceuticals, College of Basic Sciences, Tianjin Agricultural University, Tianjin, China

Download PDF

Sections

Plain Text BibTeX RIS

APA Style

Fang-Di Cong, Jie Kang, Wu-Dan Bi, Tao Li, Ping Li. (2016). Kinetic Resolution of (R,S)-1-chloro-3-(1-naphthyloxy) -2-Propanol in an Immobilized Lipase Bioreactor. Biochemistry and Molecular Biology, 1(3), 34-38. https://doi.org/10.11648/j.bmb.20160103.12

Copy | Download

ACS Style

Fang-Di Cong; Jie Kang; Wu-Dan Bi; Tao Li; Ping Li. Kinetic Resolution of (R,S)-1-chloro-3-(1-naphthyloxy) -2-Propanol in an Immobilized Lipase Bioreactor. Biochem. Mol. Biol. 2016, 1(3), 34-38. doi: 10.11648/j.bmb.20160103.12

Copy | Download

AMA Style

Fang-Di Cong, Jie Kang, Wu-Dan Bi, Tao Li, Ping Li. Kinetic Resolution of (R,S)-1-chloro-3-(1-naphthyloxy) -2-Propanol in an Immobilized Lipase Bioreactor. Biochem Mol Biol. 2016;1(3):34-38. doi: 10.11648/j.bmb.20160103.12

Copy | Download

@article{10.11648/j.bmb.20160103.12,
  author = {Fang-Di Cong and Jie Kang and Wu-Dan Bi and Tao Li and Ping Li},
  title = {Kinetic Resolution of (R,S)-1-chloro-3-(1-naphthyloxy) -2-Propanol in an Immobilized Lipase Bioreactor},
  journal = {Biochemistry and Molecular Biology},
  volume = {1},
  number = {3},
  pages = {34-38},
  doi = {10.11648/j.bmb.20160103.12},
  url = {https://doi.org/10.11648/j.bmb.20160103.12},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.bmb.20160103.12},
  abstract = {A bioreactor with Pseudomonas cepacia lipase (PCL) immobilized on the inner wall was conveniently prepared by adding lipase powder and the right amount of water to a conical flask and keeping it with mouth open in an incubator shaker at 37°C and 170 rpm for more than 10 h. The bioreactor was employed on resolution of (R, S)-1-chloro-3-(1-naphthyloxy)-2-propanol by catalyzing transesterification of it with vinyl acetate. It was showed that the wall-PCL behaved an excellent catalytic activity being 10 folds of native PCL in terms of conversion, and high enantioselectivity E = 110. And also the depressed activity of immobilized PCL owing to frequently use in organic phase could be reactivated easily by again shaking bioreactor under the aforesaid conditions after adding water. The enhanced activity was attributed to the simulation on interfacial activation mechanism of lipases at water/oil interface.},
 year = {2016}
}

Copy | Download

TY  - JOUR
T1  - Kinetic Resolution of (R,S)-1-chloro-3-(1-naphthyloxy) -2-Propanol in an Immobilized Lipase Bioreactor
AU  - Fang-Di Cong
AU  - Jie Kang
AU  - Wu-Dan Bi
AU  - Tao Li
AU  - Ping Li
Y1  - 2016/12/14
PY  - 2016
N1  - https://doi.org/10.11648/j.bmb.20160103.12
DO  - 10.11648/j.bmb.20160103.12
T2  - Biochemistry and Molecular Biology
JF  - Biochemistry and Molecular Biology
JO  - Biochemistry and Molecular Biology
SP  - 34
EP  - 38
PB  - Science Publishing Group
SN  - 2575-5048
UR  - https://doi.org/10.11648/j.bmb.20160103.12
AB  - A bioreactor with Pseudomonas cepacia lipase (PCL) immobilized on the inner wall was conveniently prepared by adding lipase powder and the right amount of water to a conical flask and keeping it with mouth open in an incubator shaker at 37°C and 170 rpm for more than 10 h. The bioreactor was employed on resolution of (R, S)-1-chloro-3-(1-naphthyloxy)-2-propanol by catalyzing transesterification of it with vinyl acetate. It was showed that the wall-PCL behaved an excellent catalytic activity being 10 folds of native PCL in terms of conversion, and high enantioselectivity E = 110. And also the depressed activity of immobilized PCL owing to frequently use in organic phase could be reactivated easily by again shaking bioreactor under the aforesaid conditions after adding water. The enhanced activity was attributed to the simulation on interfacial activation mechanism of lipases at water/oil interface.
VL  - 1
IS  - 3
ER  -

Copy | Download