Enhancement of stability of GL-7-ACA acylase immobilized on silica gel modified by epoxide silanization

Seung Won Park, Jeewon Lee, Suk In Hong, Seung Wook Kim

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

7-Aminocephalosporanic acid (7-ACA) produced by immobilized glutaryl-7-aminocephalosporanic acid (GL-7-ACA) acylase is an important starting material for the synthesis of semisynthetic cephalosporins. In this study, GL-7-ACA acylase was immobilized on silica gel modified with 3-glycidoxypropyltrimethoxysilane followed with glutaraldehyde for the production of 7-ACA. Through the experiments, optimal conditions on the immobilization of GL-7-ACA acylase were determined as follows; 12 mg/ml as an optimal concentration of GL-7-ACA acylase, 1.0 M phosphate buffer (pH 8.0) as a buffer solution, immobilization temperature of 20°C and immobilization time of 180 min. The activities of immobilized GL-7-ACA acylase obtained using low molecular weight materials were higher than that obtained immobilized GL-7-ACA acylase untreated with low molecular weight materials. Of noted importance, the highest activity of immobilized GL-7-ACA acylase was obtained by using the 0.6%(v/v) L-lysine. The effect of reducing agents in order to increase the stability of the linkage between the enzyme and the support were also investigated. The activity of immobilized GL-7-ACA acylase treated with 2%(w/w) sodium borohydride remained at almost 90% after 20 times of reuse.

Original languageEnglish
Pages (from-to)359-366
Number of pages8
JournalProcess Biochemistry
Volume39
Issue number3
DOIs
Publication statusPublished - 2003 Nov 28

Fingerprint

amidase
Epoxy Compounds
Silica Gel
Silica gel
Acids
Immobilization
Buffers
Molecular Weight
Molecular weight
glutaryl-7-aminocephalosporanic acid
Reducing Agents
Glutaral
Cephalosporins
Lysine
Reducing agents

Keywords

  • 3-Glycidoxypropyltrimethoxysilane
  • 7-ACA
  • Epoxide silanization
  • GL-7-ACA acylase
  • Immobilization

ASJC Scopus subject areas

  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Bioengineering

Cite this

Enhancement of stability of GL-7-ACA acylase immobilized on silica gel modified by epoxide silanization. / Park, Seung Won; Lee, Jeewon; Hong, Suk In; Kim, Seung Wook.

In: Process Biochemistry, Vol. 39, No. 3, 28.11.2003, p. 359-366.

Research output: Contribution to journalArticle

@article{dc56b1e45b0f41988c679a4e2f289c88,
title = "Enhancement of stability of GL-7-ACA acylase immobilized on silica gel modified by epoxide silanization",
abstract = "7-Aminocephalosporanic acid (7-ACA) produced by immobilized glutaryl-7-aminocephalosporanic acid (GL-7-ACA) acylase is an important starting material for the synthesis of semisynthetic cephalosporins. In this study, GL-7-ACA acylase was immobilized on silica gel modified with 3-glycidoxypropyltrimethoxysilane followed with glutaraldehyde for the production of 7-ACA. Through the experiments, optimal conditions on the immobilization of GL-7-ACA acylase were determined as follows; 12 mg/ml as an optimal concentration of GL-7-ACA acylase, 1.0 M phosphate buffer (pH 8.0) as a buffer solution, immobilization temperature of 20°C and immobilization time of 180 min. The activities of immobilized GL-7-ACA acylase obtained using low molecular weight materials were higher than that obtained immobilized GL-7-ACA acylase untreated with low molecular weight materials. Of noted importance, the highest activity of immobilized GL-7-ACA acylase was obtained by using the 0.6{\%}(v/v) L-lysine. The effect of reducing agents in order to increase the stability of the linkage between the enzyme and the support were also investigated. The activity of immobilized GL-7-ACA acylase treated with 2{\%}(w/w) sodium borohydride remained at almost 90{\%} after 20 times of reuse.",
keywords = "3-Glycidoxypropyltrimethoxysilane, 7-ACA, Epoxide silanization, GL-7-ACA acylase, Immobilization",
author = "Park, {Seung Won} and Jeewon Lee and Hong, {Suk In} and Kim, {Seung Wook}",
year = "2003",
month = "11",
day = "28",
doi = "10.1016/S0032-9592(03)00090-6",
language = "English",
volume = "39",
pages = "359--366",
journal = "Process Biochemistry",
issn = "1359-5113",
publisher = "Elsevier BV",
number = "3",

}

TY - JOUR

T1 - Enhancement of stability of GL-7-ACA acylase immobilized on silica gel modified by epoxide silanization

AU - Park, Seung Won

AU - Lee, Jeewon

AU - Hong, Suk In

AU - Kim, Seung Wook

PY - 2003/11/28

Y1 - 2003/11/28

N2 - 7-Aminocephalosporanic acid (7-ACA) produced by immobilized glutaryl-7-aminocephalosporanic acid (GL-7-ACA) acylase is an important starting material for the synthesis of semisynthetic cephalosporins. In this study, GL-7-ACA acylase was immobilized on silica gel modified with 3-glycidoxypropyltrimethoxysilane followed with glutaraldehyde for the production of 7-ACA. Through the experiments, optimal conditions on the immobilization of GL-7-ACA acylase were determined as follows; 12 mg/ml as an optimal concentration of GL-7-ACA acylase, 1.0 M phosphate buffer (pH 8.0) as a buffer solution, immobilization temperature of 20°C and immobilization time of 180 min. The activities of immobilized GL-7-ACA acylase obtained using low molecular weight materials were higher than that obtained immobilized GL-7-ACA acylase untreated with low molecular weight materials. Of noted importance, the highest activity of immobilized GL-7-ACA acylase was obtained by using the 0.6%(v/v) L-lysine. The effect of reducing agents in order to increase the stability of the linkage between the enzyme and the support were also investigated. The activity of immobilized GL-7-ACA acylase treated with 2%(w/w) sodium borohydride remained at almost 90% after 20 times of reuse.

AB - 7-Aminocephalosporanic acid (7-ACA) produced by immobilized glutaryl-7-aminocephalosporanic acid (GL-7-ACA) acylase is an important starting material for the synthesis of semisynthetic cephalosporins. In this study, GL-7-ACA acylase was immobilized on silica gel modified with 3-glycidoxypropyltrimethoxysilane followed with glutaraldehyde for the production of 7-ACA. Through the experiments, optimal conditions on the immobilization of GL-7-ACA acylase were determined as follows; 12 mg/ml as an optimal concentration of GL-7-ACA acylase, 1.0 M phosphate buffer (pH 8.0) as a buffer solution, immobilization temperature of 20°C and immobilization time of 180 min. The activities of immobilized GL-7-ACA acylase obtained using low molecular weight materials were higher than that obtained immobilized GL-7-ACA acylase untreated with low molecular weight materials. Of noted importance, the highest activity of immobilized GL-7-ACA acylase was obtained by using the 0.6%(v/v) L-lysine. The effect of reducing agents in order to increase the stability of the linkage between the enzyme and the support were also investigated. The activity of immobilized GL-7-ACA acylase treated with 2%(w/w) sodium borohydride remained at almost 90% after 20 times of reuse.

KW - 3-Glycidoxypropyltrimethoxysilane

KW - 7-ACA

KW - Epoxide silanization

KW - GL-7-ACA acylase

KW - Immobilization

UR - http://www.scopus.com/inward/record.url?scp=0344153359&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0344153359&partnerID=8YFLogxK

U2 - 10.1016/S0032-9592(03)00090-6

DO - 10.1016/S0032-9592(03)00090-6

M3 - Article

AN - SCOPUS:0344153359

VL - 39

SP - 359

EP - 366

JO - Process Biochemistry

JF - Process Biochemistry

SN - 1359-5113

IS - 3

ER -