Efficient enzymatic kinetic resolution of 2-heptylamine with a highly active acyl donor

Jian Hua Sun; Rong Ji Dai; Wei Wei Meng; Yu Lin Deng

doi:10.1016/j.catcom.2010.04.015

Efficient enzymatic kinetic resolution of 2-heptylamine with a highly active acyl donor

Jian Hua Sun, Rong Ji Dai, Wei Wei Meng, Yu Lin Deng^*

^*Corresponding author for this work

Beijing Institute of Technology

Research output: Contribution to journal › Article › peer-review

17 Citations (Scopus)

Abstract

Novozyme435 facilitated kinetic resolution of 2-heptylamine was here presented. Methyl methoxyacetate was used as acyl donor. A survey of influencing factors including hydrogen bonding effect, solvent effect, steric effect, temperature and the amount of acyl donor were investigated in detail. At the optimum conditions, the enantiomeric separation was successfully obtained within 8 h at 20 °C, and gave high conversion and optical purity of (R)-2-heptylamine, 48.9% and over 99% respectively. The immobilized lipase B was found to be suitable for the enantiomeric separation of aliphatic amines with good recyclability.

Original language	English
Pages (from-to)	987-991
Number of pages	5
Journal	Catalysis Communications
Volume	11
Issue number	11
DOIs	https://doi.org/10.1016/j.catcom.2010.04.015
Publication status	Published - 11 Jun 2010

Keywords

2-Heptylamine
Enzymatic kinetic resolution
Methyl methoxyacetate
Novozyme435

Access to Document

10.1016/j.catcom.2010.04.015

Cite this

Sun, J. H., Dai, R. J., Meng, W. W., & Deng, Y. L. (2010). Efficient enzymatic kinetic resolution of 2-heptylamine with a highly active acyl donor. Catalysis Communications, 11(11), 987-991. https://doi.org/10.1016/j.catcom.2010.04.015

@article{d10a284d5322495b9d3c02ee07dcafc1,

title = "Efficient enzymatic kinetic resolution of 2-heptylamine with a highly active acyl donor",

abstract = "Novozyme435 facilitated kinetic resolution of 2-heptylamine was here presented. Methyl methoxyacetate was used as acyl donor. A survey of influencing factors including hydrogen bonding effect, solvent effect, steric effect, temperature and the amount of acyl donor were investigated in detail. At the optimum conditions, the enantiomeric separation was successfully obtained within 8 h at 20 °C, and gave high conversion and optical purity of (R)-2-heptylamine, 48.9% and over 99% respectively. The immobilized lipase B was found to be suitable for the enantiomeric separation of aliphatic amines with good recyclability.",

keywords = "2-Heptylamine, Enzymatic kinetic resolution, Methyl methoxyacetate, Novozyme435",

author = "Sun, {Jian Hua} and Dai, {Rong Ji} and Meng, {Wei Wei} and Deng, {Yu Lin}",

year = "2010",

month = jun,

day = "11",

doi = "10.1016/j.catcom.2010.04.015",

language = "English",

volume = "11",

pages = "987--991",

journal = "Catalysis Communications",

issn = "1566-7367",

publisher = "Elsevier B.V.",

number = "11",

}

TY - JOUR

T1 - Efficient enzymatic kinetic resolution of 2-heptylamine with a highly active acyl donor

AU - Sun, Jian Hua

AU - Dai, Rong Ji

AU - Meng, Wei Wei

AU - Deng, Yu Lin

PY - 2010/6/11

Y1 - 2010/6/11

N2 - Novozyme435 facilitated kinetic resolution of 2-heptylamine was here presented. Methyl methoxyacetate was used as acyl donor. A survey of influencing factors including hydrogen bonding effect, solvent effect, steric effect, temperature and the amount of acyl donor were investigated in detail. At the optimum conditions, the enantiomeric separation was successfully obtained within 8 h at 20 °C, and gave high conversion and optical purity of (R)-2-heptylamine, 48.9% and over 99% respectively. The immobilized lipase B was found to be suitable for the enantiomeric separation of aliphatic amines with good recyclability.

AB - Novozyme435 facilitated kinetic resolution of 2-heptylamine was here presented. Methyl methoxyacetate was used as acyl donor. A survey of influencing factors including hydrogen bonding effect, solvent effect, steric effect, temperature and the amount of acyl donor were investigated in detail. At the optimum conditions, the enantiomeric separation was successfully obtained within 8 h at 20 °C, and gave high conversion and optical purity of (R)-2-heptylamine, 48.9% and over 99% respectively. The immobilized lipase B was found to be suitable for the enantiomeric separation of aliphatic amines with good recyclability.

KW - 2-Heptylamine

KW - Enzymatic kinetic resolution

KW - Methyl methoxyacetate

KW - Novozyme435

UR - http://www.scopus.com/inward/record.url?scp=77954212637&partnerID=8YFLogxK

U2 - 10.1016/j.catcom.2010.04.015

DO - 10.1016/j.catcom.2010.04.015

M3 - Article

AN - SCOPUS:77954212637

SN - 1566-7367

VL - 11

SP - 987

EP - 991

JO - Catalysis Communications

JF - Catalysis Communications

IS - 11

ER -

Efficient enzymatic kinetic resolution of 2-heptylamine with a highly active acyl donor

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this