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^*

^*此作品的通讯作者

Beijing Institute of Technology

科研成果: 期刊稿件 › 文章 › 同行评审

17 引用（Scopus）

摘要

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.

源语言	英语
页（从-至）	987-991
页数	5
期刊	Catalysis Communications
卷	11
期	11
DOI	https://doi.org/10.1016/j.catcom.2010.04.015
出版状态	已出版 - 11 6月 2010

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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",

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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

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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

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