English  |  正體中文  |  简体中文  |  Items with full text/Total items : 56570/90363 (63%)
Visitors : 11880780      Online Users : 48
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/987654321/117181

    Title: An exochitinase with N-acetyl-β-glucosaminidase activity from shrimp heads conversion by Streptomyces speibonae and its application in hydrolyzing β-chitin powder to produce N-acetyl-d-glucosamine
    Authors: Tran TN, Doan CT, Nguyen MT, Nguyen VB, Vo TPK, Nguyen AD, Wang SL*
    Keywords: exochitinase;β-chitin powder;N-acetyl-β-glucosaminidase;shrimp heads;Streptomyces speibonae
    Date: 2019-09-30
    Issue Date: 2019-10-01 12:10:42 (UTC+8)
    Publisher: MDPI
    Abstract: Marine chitinous byproducts possess significant applications in many fields. In this research, different kinds of fishery chitin-containing byproducts from shrimp (shrimp head powder (SHP) and demineralized shrimp shell powder), crab (demineralized crab shell powder), as well as squid (squid pen powder) were used to provide both carbon and nitrogen (C/N) nutrients for the production of an exochitinase via Streptomyces speibonae TKU048, a chitinolytic bacterium isolated from Taiwanese soils. S. speibonae TKU048 expressed the highest exochitinase productivity (45.668 U/mL) on 1.5% SHP-containing medium at 37 °C for 2 days. Molecular weight determination analysis basing on polyacrylamide gel electrophoresis revealed the mass of TKU048 exochitinase was approximately 21 kDa. The characterized exochitinase expressed some interesting properties, for example acidic pH optima (pH 3 and pH 5–7) and a higher temperature optimum (60 °C). Furthermore, the main hydrolysis mechanism of TKU048 exochitinase was N-acetyl-β-glucosaminidase-like activity; its most suitable substrate was β-chitin powder. The hydrolysis experiment revealed that TKU048 exochitinase was efficient in the cleavage of β-chitin powder, thereby releasing N-acetyl-d-glucosamine (GlcNAc, monomer unit of chitin structure) as the major product with 0.335 mg/mL of GlcNAc concentration and a yield of 73.64% after 96 h of incubation time. Thus, TKU048 exochitinase may have potential in GlcNAc production due to its N-acetyl-β-glucosaminidase-like activity.
    Relation: Polymers2019 11(10), p.1600
    DOI: 10.3390/polym11101600
    Appears in Collections:[Graduate Institute & Department of Chemistry] Journal Article

    Files in This Item:

    File Description 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