English  |  正體中文  |  简体中文  |  Items with full text/Total items : 51483/86598 (59%)
Visitors : 8245279      Online Users : 103
RC Version 7.0 © Powered By DSPACE, MIT. Enhanced by NTU Library & TKU 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: http://tkuir.lib.tku.edu.tw:8080/dspace/handle/987654321/18867


    Title: Purification and characterization of protease and chitinase from Bacillus cereus TKU006 and conversion of marine wastes by these enzymes
    Authors: Wang, San-Lang;Chao, Chia-Hsing;Liang, Tzu-Wen;Chen, Chung-Chih
    Contributors: 淡江大學化學學系
    Keywords: Protease;Chitinase;Antioxidant;Shrimp shells;Bacillus cereus
    Date: 2009-06
    Issue Date: 2013-02-27 09:32:00 (UTC+8)
    Publisher: Secaucus: Springer New York LLC
    Abstract: A chitinase- and protease-producing bacterium was isolated and identified as Bacillus cereus TKU006. The better condition on our tests for protease and chitinase production was found when the culture was shaken at 25°C for 2 days in 25 mL of medium containing 2% shrimp shell powder (w/v), 0.1% K2HPO4, and 0.05% MgSO4·7H2O. The molecular masses of TKU006 protease and chitinase determined by sodium dodecyl sulfate (SDS)–polyacrylamide gel electrophoresis were approximately 39 and 35 kDa, respectively. The optimum pH, optimum temperature, pH stability, and thermal stability of TKU006 protease and chitinase were 9, 50°C, 3–11, 50°C and 5, 40°C, 3–11, 60°C, respectively. TKU006 protease was inhibited completely by EDTA, indicating that the TKU006 protease was a metalloprotease. The TKU006 protease and chitinase retained 61%, 60%, 73%, and 100% and 60%, 60%, 71%, and 96% of its original activity in the presence of 2% Tween 20, 2% Tween 40, 2% Triton X-100, and 1 mM SDS, respectively. The antioxidant activity of TKU006 culture supernatant was determined through the scavenging ability on DPPH with 70% per milliliter. In conclusion, the novelties of the TKU006 protease and chitinase include its high stability to the surfactants and pH. Besides, with this method, we have shown that marine wastes can be utilized to generate a high-value-added product and have revealed its hidden potential in the production of functional foods.
    Relation: Marine Biotechnology 11(3), pp.334-344
    DOI: 10.1007/s10126-008-9149-y
    Appears in Collections:[化學學系暨研究所] 期刊論文

    Files in This Item:

    File SizeFormat
    index.html0KbHTML201View/Open

    All items in 機構典藏 are protected by copyright, with all rights reserved.


    DSpace Software Copyright © 2002-2004  MIT &  Hewlett-Packard  /   Enhanced by   NTU Library & TKU Library IR teams. Copyright ©   - Feedback