Analysis and enhancement of bioconversion of D-phenylalanine catalyzed by hydantoinase and N-carbamoylase

Zhong Yao; Shu Zhu; Jia Huang Li; Chun Yan Tu; Su Ping Li; Ping Wei

Analysis and enhancement of bioconversion of D-phenylalanine catalyzed by hydantoinase and N-carbamoylase

Zhong Yao, Shu Zhu, Jia Huang Li, Chun Yan Tu, Su Ping Li, Ping Wei

Nanjing Tech University

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

Abstract

The free cells containing D-HEn and N-CAEn activity were obtained by fermentation using Pseudomonas sp.js-01 screened. It is demonstrated that the low activity of N-CAEn was the limiting factor of the whole conversion process by the dynamic parameters determination and conversion experiment. D-HEn and N-CAEn were separated using HIC, and the ratio of the two enzymes is adjusted and the experiment results show that the conversion process is promoted sharply. The conversion ratio of D-Phe with D-HEn\N-CAEn as 1:4 within 6 h is two times more than that as 1:1.

Original language	English
Pages (from-to)	44-46
Number of pages	3
Journal	Xiandai Huagong/Modern Chemical Industry
Volume	24
Issue number	5
State	Published - May 2004

Keywords

5-benzylhydantoin
D-hydantoinase
D-phenylalanine
N-carbamoylase

Cite this

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title = "Analysis and enhancement of bioconversion of D-phenylalanine catalyzed by hydantoinase and N-carbamoylase",

abstract = "The free cells containing D-HEn and N-CAEn activity were obtained by fermentation using Pseudomonas sp.js-01 screened. It is demonstrated that the low activity of N-CAEn was the limiting factor of the whole conversion process by the dynamic parameters determination and conversion experiment. D-HEn and N-CAEn were separated using HIC, and the ratio of the two enzymes is adjusted and the experiment results show that the conversion process is promoted sharply. The conversion ratio of D-Phe with D-HEn\N-CAEn as 1:4 within 6 h is two times more than that as 1:1.",

keywords = "5-benzylhydantoin, D-hydantoinase, D-phenylalanine, N-carbamoylase",

author = "Zhong Yao and Shu Zhu and Li, {Jia Huang} and Tu, {Chun Yan} and Li, {Su Ping} and Ping Wei",

year = "2004",

month = may,

language = "英语",

volume = "24",

pages = "44--46",

journal = "Xiandai Huagong/Modern Chemical Industry",

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TY - JOUR

T1 - Analysis and enhancement of bioconversion of D-phenylalanine catalyzed by hydantoinase and N-carbamoylase

AU - Yao, Zhong

AU - Zhu, Shu

AU - Li, Jia Huang

AU - Tu, Chun Yan

AU - Li, Su Ping

AU - Wei, Ping

PY - 2004/5

Y1 - 2004/5

N2 - The free cells containing D-HEn and N-CAEn activity were obtained by fermentation using Pseudomonas sp.js-01 screened. It is demonstrated that the low activity of N-CAEn was the limiting factor of the whole conversion process by the dynamic parameters determination and conversion experiment. D-HEn and N-CAEn were separated using HIC, and the ratio of the two enzymes is adjusted and the experiment results show that the conversion process is promoted sharply. The conversion ratio of D-Phe with D-HEn\N-CAEn as 1:4 within 6 h is two times more than that as 1:1.

AB - The free cells containing D-HEn and N-CAEn activity were obtained by fermentation using Pseudomonas sp.js-01 screened. It is demonstrated that the low activity of N-CAEn was the limiting factor of the whole conversion process by the dynamic parameters determination and conversion experiment. D-HEn and N-CAEn were separated using HIC, and the ratio of the two enzymes is adjusted and the experiment results show that the conversion process is promoted sharply. The conversion ratio of D-Phe with D-HEn\N-CAEn as 1:4 within 6 h is two times more than that as 1:1.

KW - 5-benzylhydantoin

KW - D-hydantoinase

KW - D-phenylalanine

KW - N-carbamoylase

UR - http://www.scopus.com/inward/record.url?scp=3142740933&partnerID=8YFLogxK

M3 - 文章

AN - SCOPUS:3142740933

SN - 0253-4320

VL - 24

SP - 44

EP - 46

JO - Xiandai Huagong/Modern Chemical Industry

JF - Xiandai Huagong/Modern Chemical Industry

IS - 5

ER -

Analysis and enhancement of bioconversion of D-phenylalanine catalyzed by hydantoinase and N-carbamoylase

Abstract

Keywords

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