English  |  正體中文  |  简体中文  |  Items with full text/Total items : 62379/95055 (66%)
Visitors : 2294868      Online Users : 165
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: https://tkuir.lib.tku.edu.tw/dspace/handle/987654321/18862

    Title: A solvent stable metalloprotease produced by Bacillus sp. TKU004 and its application in the deproteinization of squid pen for β-chitin preparation
    Authors: Wang, San-lang;Kao, Te-yi;Wang, Chuan-lu;Yen, Yue-horng;Chern, Ming-kai;Chen, Yau-hung
    Contributors: 淡江大學生命科學研究所
    Keywords: Bacillus;Protease;Squid pen;Chitin;Deproteinization
    Date: 2006-08
    Issue Date: 2013-02-27 09:39:12 (UTC+8)
    Publisher: Philadelphia: Elsevier Inc.
    Abstract: A protease-producing bacterium was isolated and identified as Bacillus sp. TKU004. It thus can be used for deproteinization of squid pen in the preparation of β-chitin. The optimized condition for protease production was found when the culture was shaken at 30 °C for 4 days in 100 mL of medium containing 2% squid pen powder (SPP) (w/v), 0.1% K2HPO4, and 0.05% MgSO4. Under such condition, both the production of protease by Bacillus sp. TKU004 and the resulted protein removal of squid pen attained the optimum. They were 0.065 U/mL and 73%, respectively. An extracellular protease was purified from the culture supernatant of Bacillus sp. TKU004. The molecular weight of TKU004 protease was 27 and 57 kDa assayed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gel filtration, respectively. The optimum pH, optimum temperature, pH stability, thermal stability, Km, Vmax, and activation energy of TKU004 protease were 6–8, 60 °C, pH 5–8, 50 °C, 2.98 mg/mL, 0.14 U/mL, 8.31 J/(mol K), respectively. It was concluded that TKU004 protease is a Zn-containing metalloenzyme, and its dimeric structure contains at least one disulfide bond. The unique characteristic of TKU004 protease is that it retained more than 60% of its original activity after preincubation for 10 days at 25 °C in the presence of tested organic solvents (25%, v/v). This is also the first report of a strain being able to use squid pen as the sole carbon/nitrogen source for proteases production and being used for the reclamation of β-chitin from squid pen.
    Relation: Enzyme and Microbial Technology 39(4), pp.724-731
    DOI: 10.1016/j.enzmictec.2005.12.007
    Appears in Collections:[Graduate Institue of Life Sciences] Journal Article

    Files in This Item:

    File SizeFormat

    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