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

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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
Issue number1
Publication statusPublished - 2006 Jan 1



  • 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

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