화학공학소재연구정보센터
홈 로그인 로그아웃 연락처 사이트맵
Korean Journal of Chemical Engineering, Vol.26, No.4, 1065-1069, July, 2009
DOI10.1007/s11814-009-0177-8  Export Citation
Improvement of the catalytic performance of immobilized penicillin acylase through assembly of macromolecular reagents in nanopore to create a crowding environment
Cheng Zhou1, 2, Anming Wang1, 2, Zhiqiang Du1, 2, Shemin Zhu1, 3, and Shubao Shen1, 2, †
  • 1National Engineering Research Center for Biotechnology, Nanjing University of Technology, Nanjing 210009, P. R. China
  • 2College of Life Science and Pharmaceutical Engineering, Nanjing University of Technology, Nanjing 210009, P. R. China
  • 3College of Materials Science and Engineering, Nanjing University of Technology, Nanjing 210009, P. R. China
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Macromolecular reagents were co-assembled with penicillin acylase (PA) and immobilized in mesocellular siliceous foams (MCFs) to resemble living cells. Types and concentrations of macromolecules were studied. The catalytic characteristic and stability of PA preparations were also investigated. PA assembled with dextran 10 k in MCFs showed maximum specific activity, 1.32-fold of that of the solely immobilized PA. The optimum pH of dextran and BSA derivatives shifted to neutrality, and the optimum temperature increased by 10 ℃. Also, Km of BSA derivative of PA declined 56.7% compared to solely immobilized PA, while the Kcat/Km of PA assembled with BSA was enhanced to 147%. After incubation at 50 ℃ for 6 h, residual activity of PA assembled with BSA exhibited 53.0%. The ficoll derivative showed 82.8% of its initial activity at 4 ℃ after 8-week storage. The results indicated that macromolecular reagents assembled with PA in MCFs could dramatically improve the catalytic performance and stability of im- mobilized enzyme.
Keywords:Penicillin Acylase;Immobilization;Covalent;Mesocellular Siliceous Foams;Macromolecular Crowding
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