Thermal and operational characteristics of glutaryl-7-aminocephalosporanic acid acylase immobilized on silica gel modified by epoxide silanization

Jung Soo Lim, Seung Won Park, Seung Wook Kim

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

In this study, an investigation was performed into the thermal and operational characteristics of glutaryl-7-aminocephalosporanic acid (GL-7-ACA) acylase (EC 3.5.1.-) immobilized on silica gel that had been modified by epoxide silanization. The pH values for the optimum activity of free and immobilized GL-7-ACA acylase were almost the same. However, the pH-dependent activity profile for the immobilized GL-7-ACA acylase is considerably expanded. Both free and immobilized enzymes generally had the highest activity at 50°C. In thermodynamic studies, it was found that immobilization using epoxide silanization made GL-7-ACA acylase thermodynamically stable. In the results of repeated batch production of 7-ACA, 89.0 and 83.5% of the 7-ACA produced at the initial cycle were maintained after 20 times of recycle at 25°C and 30°C, respectively. Hence it was suggested that mass production of 7-ACA at 25°C using immobilized GL-7-ACA acylase by epoxide silanization would be possible on a large scale.

Original languageEnglish
Pages (from-to)39-44
Number of pages6
JournalWorld Journal of Microbiology and Biotechnology
Volume22
Issue number1
DOIs
Publication statusPublished - 2006 Jan 1

Fingerprint

amidase
Epoxy Compounds
Silica Gel
silica gel
epoxides
Hot Temperature
heat
acids
Immobilized Enzymes
immobilized enzymes
Thermodynamics
Immobilization
thermodynamics
glutaryl-7-aminocephalosporanic acid

Keywords

  • Epoxide silanization
  • GL-7-ACA Acylase
  • Immobilization
  • Repeated batch reaction
  • Thermodynamics

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Plant Science
  • Biochemistry
  • Food Science
  • Microbiology
  • Biotechnology

Cite this

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abstract = "In this study, an investigation was performed into the thermal and operational characteristics of glutaryl-7-aminocephalosporanic acid (GL-7-ACA) acylase (EC 3.5.1.-) immobilized on silica gel that had been modified by epoxide silanization. The pH values for the optimum activity of free and immobilized GL-7-ACA acylase were almost the same. However, the pH-dependent activity profile for the immobilized GL-7-ACA acylase is considerably expanded. Both free and immobilized enzymes generally had the highest activity at 50°C. In thermodynamic studies, it was found that immobilization using epoxide silanization made GL-7-ACA acylase thermodynamically stable. In the results of repeated batch production of 7-ACA, 89.0 and 83.5{\%} of the 7-ACA produced at the initial cycle were maintained after 20 times of recycle at 25°C and 30°C, respectively. Hence it was suggested that mass production of 7-ACA at 25°C using immobilized GL-7-ACA acylase by epoxide silanization would be possible on a large scale.",
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N2 - In this study, an investigation was performed into the thermal and operational characteristics of glutaryl-7-aminocephalosporanic acid (GL-7-ACA) acylase (EC 3.5.1.-) immobilized on silica gel that had been modified by epoxide silanization. The pH values for the optimum activity of free and immobilized GL-7-ACA acylase were almost the same. However, the pH-dependent activity profile for the immobilized GL-7-ACA acylase is considerably expanded. Both free and immobilized enzymes generally had the highest activity at 50°C. In thermodynamic studies, it was found that immobilization using epoxide silanization made GL-7-ACA acylase thermodynamically stable. In the results of repeated batch production of 7-ACA, 89.0 and 83.5% of the 7-ACA produced at the initial cycle were maintained after 20 times of recycle at 25°C and 30°C, respectively. Hence it was suggested that mass production of 7-ACA at 25°C using immobilized GL-7-ACA acylase by epoxide silanization would be possible on a large scale.

AB - In this study, an investigation was performed into the thermal and operational characteristics of glutaryl-7-aminocephalosporanic acid (GL-7-ACA) acylase (EC 3.5.1.-) immobilized on silica gel that had been modified by epoxide silanization. The pH values for the optimum activity of free and immobilized GL-7-ACA acylase were almost the same. However, the pH-dependent activity profile for the immobilized GL-7-ACA acylase is considerably expanded. Both free and immobilized enzymes generally had the highest activity at 50°C. In thermodynamic studies, it was found that immobilization using epoxide silanization made GL-7-ACA acylase thermodynamically stable. In the results of repeated batch production of 7-ACA, 89.0 and 83.5% of the 7-ACA produced at the initial cycle were maintained after 20 times of recycle at 25°C and 30°C, respectively. Hence it was suggested that mass production of 7-ACA at 25°C using immobilized GL-7-ACA acylase by epoxide silanization would be possible on a large scale.

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