Efficient preparation of enantiopure l-tert-leucine through immobilized penicillin G acylase catalyzed kinetic resolution in aqueous medium

Weiming Liu; Jixing Luo; Xiaojian Zhuang; Wenhe Shen; Yang Zhang; Shuang Li; Yi Hu; He Huang

doi:10.1016/j.bej.2013.12.016

Efficient preparation of enantiopure l-tert-leucine through immobilized penicillin G acylase catalyzed kinetic resolution in aqueous medium

Weiming Liu, Jixing Luo, Xiaojian Zhuang, Wenhe Shen, Yang Zhang, Shuang Li, Yi Hu, He Huang

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

17 Scopus citations

Abstract

Racemic _DL-tert-leucine (_DL-Tle) was resolved to obtain enantiopure _L-Tle through enantioselective hydrolysis of its N-phenylacetyl derivative with immobilized penicillin G acylase (PGA). The effects of pH, reaction temperature, substrate concentration and reaction time on the reaction were investigated. The reaction was conveniently carried out at 0.4M substrate concentration in water at pH 8.0 and 30°C. Under the optimized reaction conditions, _L-Tle was obtained in an enantiopure form (>99% ee) with 45.8% substrate conversion after 4h. The thermal stability and operational stability of immobilized PGA were examined. Furthermore, the preparation of _L-Tle was successfully performed in a recirculating packed bed reactor (RPBR) system and immobilized PGA exhibited a long-term stability for 51 days with a slight decrease of activity. The isolated _D-enantiomer was racemized at 160°C for 15min and reused as substrate. The results obtained clearly demonstrated a potential for industrial application of immobilized PGA in the preparation of _L-Tle through enantioselective hydrolysis of its N-phenylacetyl derivative.

Original language	English
Pages (from-to)	116-120
Number of pages	5
Journal	Biochemical Engineering Journal
Volume	83
DOIs	https://doi.org/10.1016/j.bej.2013.12.016
State	Published - 15 Feb 2014

Keywords

-tert-leucine
Biocatalysis
Bioprocess design
Immobilized penicillin G acylase
Optimization
Packed bed bioreactors

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10.1016/j.bej.2013.12.016

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title = "Efficient preparation of enantiopure l-tert-leucine through immobilized penicillin G acylase catalyzed kinetic resolution in aqueous medium",

abstract = "Racemic DL-tert-leucine (DL-Tle) was resolved to obtain enantiopure L-Tle through enantioselective hydrolysis of its N-phenylacetyl derivative with immobilized penicillin G acylase (PGA). The effects of pH, reaction temperature, substrate concentration and reaction time on the reaction were investigated. The reaction was conveniently carried out at 0.4M substrate concentration in water at pH 8.0 and 30°C. Under the optimized reaction conditions, L-Tle was obtained in an enantiopure form (>99% ee) with 45.8% substrate conversion after 4h. The thermal stability and operational stability of immobilized PGA were examined. Furthermore, the preparation of L-Tle was successfully performed in a recirculating packed bed reactor (RPBR) system and immobilized PGA exhibited a long-term stability for 51 days with a slight decrease of activity. The isolated D-enantiomer was racemized at 160°C for 15min and reused as substrate. The results obtained clearly demonstrated a potential for industrial application of immobilized PGA in the preparation of L-Tle through enantioselective hydrolysis of its N-phenylacetyl derivative.",

keywords = "-tert-leucine, Biocatalysis, Bioprocess design, Immobilized penicillin G acylase, Optimization, Packed bed bioreactors",

author = "Weiming Liu and Jixing Luo and Xiaojian Zhuang and Wenhe Shen and Yang Zhang and Shuang Li and Yi Hu and He Huang",

year = "2014",

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doi = "10.1016/j.bej.2013.12.016",

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T1 - Efficient preparation of enantiopure l-tert-leucine through immobilized penicillin G acylase catalyzed kinetic resolution in aqueous medium

AU - Liu, Weiming

AU - Luo, Jixing

AU - Zhuang, Xiaojian

AU - Shen, Wenhe

AU - Zhang, Yang

AU - Li, Shuang

AU - Hu, Yi

AU - Huang, He

PY - 2014/2/15

Y1 - 2014/2/15

N2 - Racemic DL-tert-leucine (DL-Tle) was resolved to obtain enantiopure L-Tle through enantioselective hydrolysis of its N-phenylacetyl derivative with immobilized penicillin G acylase (PGA). The effects of pH, reaction temperature, substrate concentration and reaction time on the reaction were investigated. The reaction was conveniently carried out at 0.4M substrate concentration in water at pH 8.0 and 30°C. Under the optimized reaction conditions, L-Tle was obtained in an enantiopure form (>99% ee) with 45.8% substrate conversion after 4h. The thermal stability and operational stability of immobilized PGA were examined. Furthermore, the preparation of L-Tle was successfully performed in a recirculating packed bed reactor (RPBR) system and immobilized PGA exhibited a long-term stability for 51 days with a slight decrease of activity. The isolated D-enantiomer was racemized at 160°C for 15min and reused as substrate. The results obtained clearly demonstrated a potential for industrial application of immobilized PGA in the preparation of L-Tle through enantioselective hydrolysis of its N-phenylacetyl derivative.

AB - Racemic DL-tert-leucine (DL-Tle) was resolved to obtain enantiopure L-Tle through enantioselective hydrolysis of its N-phenylacetyl derivative with immobilized penicillin G acylase (PGA). The effects of pH, reaction temperature, substrate concentration and reaction time on the reaction were investigated. The reaction was conveniently carried out at 0.4M substrate concentration in water at pH 8.0 and 30°C. Under the optimized reaction conditions, L-Tle was obtained in an enantiopure form (>99% ee) with 45.8% substrate conversion after 4h. The thermal stability and operational stability of immobilized PGA were examined. Furthermore, the preparation of L-Tle was successfully performed in a recirculating packed bed reactor (RPBR) system and immobilized PGA exhibited a long-term stability for 51 days with a slight decrease of activity. The isolated D-enantiomer was racemized at 160°C for 15min and reused as substrate. The results obtained clearly demonstrated a potential for industrial application of immobilized PGA in the preparation of L-Tle through enantioselective hydrolysis of its N-phenylacetyl derivative.

KW - -tert-leucine

KW - Biocatalysis

KW - Bioprocess design

KW - Immobilized penicillin G acylase

KW - Optimization

KW - Packed bed bioreactors

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DO - 10.1016/j.bej.2013.12.016

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JO - Biochemical Engineering Journal

JF - Biochemical Engineering Journal

ER -

Efficient preparation of enantiopure l-tert-leucine through immobilized penicillin G acylase catalyzed kinetic resolution in aqueous medium

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