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      KCI등재 SCIE SCOPUS

      Post-immobilization of Modified Macromolecular Reagents using Assembled Penicillin Acylase for Microenvironmental Regulation of Nanopores and Enhancement of Enzyme Stability

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      https://www.riss.kr/link?id=A104469101

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      다국어 초록 (Multilingual Abstract)

      Penicillin acylase (PA) is known to regulate the microenvironment of nanospores. In this study, nanopores containing chemically-modified macromolecules co-assembled with immobilized PA were constructed. We also investigated the various types of functi...

      Penicillin acylase (PA) is known to regulate the microenvironment of nanospores. In this study, nanopores containing chemically-modified macromolecules co-assembled with immobilized PA were constructed. We also investigated the various types of functionalized mesocellular siliceous foams (MCFs) commonly used for the immobilization of PA by measuring the catalytic performance and stability of each PA preparation. Amino-MCF activated by p-benzoquinone was chosen as the optimum support for PA immobilization. Successful modification of macromolecules was verified by FT-IR and ultraviolet (UV)spectroscopy. The specific activity of PA co-assembled with dextran 10 k was 99.1 U/mg, which was 1.5-fold that of pristine immobilized PA, while the optimum pH was shifted to neutral. Compared to pristine immobilized and free PA, the optimum temperatures for the modified PA were 5 and 10oC higher, respectively. The residual activity of the ficoll derivative of PA after treatment at 50oC for 6 h was 70%, and this was later increased to 214.5% compared to that of pristine immobilized PA. The dextran 10 k derivative of PA exhibited 90.2% residual activity after 25times of continuous use. The results show that chemicallymodified macromolecules co-assembled with PA in amino-MCF provided a suitable microenvironment for enzyme stability.

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      참고문헌 (Reference)

      1 Chandel, A. K, "The realm of penicillin G acylase in β­lactam antibiotics" 42 : 199-207, 2008

      2 Minton,A.P, "The influence of macromolecular crowd­ing and macromolecular confinement on biochemical reactions in physiological media" 276 : 10577-10580, 2001

      3 Zhang, Z. D, "Stabilization mechanism of MPEG modified trypsin based on thermal in­activation kinetic analysis and molecular modeling computation" 14 : 85-94, 2001

      4 Cheung, M. S, "Nanopore-protein interactions dramatically alter stability and yield of the native state in restricted spaces" 357 : 632-643, 2006

      5 Yvonne Chow, "Modeling and Optimization of Methanolas a Cosolvent in Amoxicillin Synthesisand Its Advantage over Ethylene Glycol" 한국생물공학회 12 (12): 390-398, 2007

      6 Schmidt-Winkel, P, "Mesocellular siliceous foams with uniformly sized cells and windows" 121 : 254-255, 1999

      7 Cheng Zhou, "Improvement of the catalytic performance of immobilized penicillin acylase through assembly of macromolecular reagents in nanopore to create a crowding environment" 한국화학공학회 26 (26): 1065-1069, 2009

      8 Tischer, W, "Immobilized enzymes: crystals or carriers?" 17 : 326-335, 1999

      9 Kallenberg, A. I, "Immobilization of penicillin G acylase: The key to optimum performance" 347 : 905-926, 2005

      10 Kim, H, "Immobilization of a heteropolyacid catalyst on the aminopropyl-functionalized mesostructured cellular foam(MCF)silica.Mater.Res.Bull" 42 : 2132-2142, 2007

      1 Chandel, A. K, "The realm of penicillin G acylase in β­lactam antibiotics" 42 : 199-207, 2008

      2 Minton,A.P, "The influence of macromolecular crowd­ing and macromolecular confinement on biochemical reactions in physiological media" 276 : 10577-10580, 2001

      3 Zhang, Z. D, "Stabilization mechanism of MPEG modified trypsin based on thermal in­activation kinetic analysis and molecular modeling computation" 14 : 85-94, 2001

      4 Cheung, M. S, "Nanopore-protein interactions dramatically alter stability and yield of the native state in restricted spaces" 357 : 632-643, 2006

      5 Yvonne Chow, "Modeling and Optimization of Methanolas a Cosolvent in Amoxicillin Synthesisand Its Advantage over Ethylene Glycol" 한국생물공학회 12 (12): 390-398, 2007

      6 Schmidt-Winkel, P, "Mesocellular siliceous foams with uniformly sized cells and windows" 121 : 254-255, 1999

      7 Cheng Zhou, "Improvement of the catalytic performance of immobilized penicillin acylase through assembly of macromolecular reagents in nanopore to create a crowding environment" 한국화학공학회 26 (26): 1065-1069, 2009

      8 Tischer, W, "Immobilized enzymes: crystals or carriers?" 17 : 326-335, 1999

      9 Kallenberg, A. I, "Immobilization of penicillin G acylase: The key to optimum performance" 347 : 905-926, 2005

      10 Kim, H, "Immobilization of a heteropolyacid catalyst on the aminopropyl-functionalized mesostructured cellular foam(MCF)silica.Mater.Res.Bull" 42 : 2132-2142, 2007

      11 Fernandez-Lafuente, R, "Facile synthesis of artificial enzyme nano-environment via solid-phase chemistry of im­mobilized derivatives: dramatic stabilization of penicillin acylase versus organic solvents" 24 : 96-103, 1999

      12 Shewale, J. G, "Evaluation of determination of 6-aminopenicillanic acid by p­dimethyl aminobenzaldedyde" 1 : 69-72, 1987

      13 Xue, P, "Epoxy-functionalized mesostructured cellular foams as effective support for covalent immobilization of penicillin G acylase" 255 : 165-1630, 2008

      14 Wang, A. M, "Enhancement of microwave-assisted covalent immobilization of penicillin acylase using macromolecular crowding and glycine quenching" 107 : 219-224, 2009

      15 Chaijitrsakool, T, "Effects of pore characters of mesoporous resorcinol-formaldehyde carbon gels on enzyme immobilization" 55 : 137-141, 2008

      16 Wilson, L, "Co-aggregation of penicillin G acylase and polyionic polymers: an easy methodology to prepare enzyme biocatalysts stable in organic media" 5 : 852-857, 2004

      17 Van Langen, L. M, "Active site titration as a tool for the evaluation of immobilization procedures of penicillin acylase" 79 : 224-228, 2002

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      2023 평가예정 해외DB학술지평가 신청대상 (해외등재 학술지 평가)
      2020-01-01 평가 등재학술지 유지 (해외등재 학술지 평가) KCI등재
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      2007-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2004-01-01 평가 등재학술지 선정 (등재후보2차) KCI등재
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      2001-07-01 평가 등재후보학술지 선정 (신규평가) KCI등재후보
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      기준연도 WOS-KCI 통합IF(2년) KCIF(2년) KCIF(3년)
      2016 1.14 0.13 0.75
      KCIF(4년) KCIF(5년) 중심성지수(3년) 즉시성지수
      0.57 0.46 0.239 0.02
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