中大學術數位典藏-NCU Institutional Repository-提供博碩士論文、考古題、期刊論文、研究計畫等下載:Item 987654321/101479
English  |  正體中文  |  简体中文  |  Items with full text/Total items : 94201/94201 (100%)
Visitors : 81560555      Online Users : 3641
RC Version 7.0 © Powered By DSPACE, MIT. Enhanced by NTU Library IR team.
Scope Tips:
  • please add "double quotation mark" for query phrases to get precise results
  • please goto advance search for comprehansive author search
  • Adv. Search
    HomeLoginUploadHelpAboutAdminister Goto mobile version


    Please use this identifier to cite or link to this item: https://ir.lib.ncu.edu.tw/handle/987654321/101479


    Title: Imparting Functionality to Biocatalysts via Embedding Enzymes into Nanoporous Materials by a de Novo Approach: Size-Selective Sheltering of Catalase in Metal-Organic Framework Microcrystals
    Authors: 謝發坤;Shieh, Fa-Kuen;Wang, Shao-Chun;Yen, Chia-I;Wu, Chang-Cheng;Dutta, Saikat;Chou, Lien-Yang;Morabito, Joseph V;Hu, Pan;Hsu, Ming-Hua;Wu, Kevin C.-W;Tsung, Chia-Kuang
    Contributors: 理學院化學學系
    Keywords: Biocatalysis;biocatalysts;catalase;Catalase - chemistry;Catalase - metabolism;confocal microscopy;coordination polymers;crystals;electron microscopy;electrophoresis;Enzymes, Immobilized - chemistry;Enzymes, Immobilized - metabolism;hydrogen peroxide;Hydrogen Peroxide - metabolism;Imidazoles - chemistry;Kinetics;Models, Molecular;Nanopores;nitrogen;Organometallic Compounds - chemistry;Particle Size;Protein Conformation;proteinases;sorption;thermogravimetry;X-ray diffraction;Zeolites - chemistry
    Date: 2015-04-08
    Issue Date: 2026-04-21 14:35:15 (UTC+8)
    Publisher: American Chemical Society;United States: American Chemical Society
    Abstract: 摘要: We develop a new concept to impart new functions to biocatalysts by combining enzymes and metal–organic frameworks (MOFs). The proof-of-concept design is demonstrated by embedding catalase molecules into uniformly sized ZIF-90 crystals via a de novo approach. We have carried out electron microscopy, X-ray diffraction, nitrogen sorption, electrophoresis, thermogravimetric analysis, and confocal microscopy to confirm that the ∼10 nm catalase molecules are embedded in 2 μm single-crystalline ZIF-90 crystals with ∼5 wt % loading. Because catalase is immobilized and sheltered by the ZIF-90 crystals, the composites show activity in hydrogen peroxide degradation even in the presence of protease proteinase K.
    其他題名: J. Am. Chem. Soc
    出版者: United States: American Chemical Society
    出版日期: 2015-04-08
    出處: Journal of the American Chemical Society, 2015-04, Vol.137 (13), p.4276-4279
    資源來源: American Chemical Society Journals
    版權: Copyright © American Chemical Society
    識別號: ISSN: 0002-7863
    識別號: ISSN: 1520-5126
    識別號: EISSN: 1520-5126
    識別號: DOI: 10.1021/ja513058h
    識別號: PMID: 25781479
    Appears in Collections:[Department of Chemistry] journal & Dissertation

    Files in This Item:

    File Description SizeFormat
    index.html0KbHTML19View/Open


    All items in NCUIR are protected by copyright, with all rights reserved.

    社群 sharing

    ::: Copyright National Central University. | 國立中央大學圖書館版權所有 | 收藏本站 | 設為首頁 | 最佳瀏覽畫面: 1024*768 | 建站日期:8-24-2009 :::
    DSpace Software Copyright © 2002-2004  MIT &  Hewlett-Packard  /   Enhanced by   NTU Library IR team Copyright ©   - 隱私權政策聲明