Special Feature

User Panel

My Panel

My Panel

Bookmark Science Articles

Recent News
Bookmark / Share This Science Site

Characterization of Fusarium oxysporum beta-1,6-galactanase, an enzyme that hydrolyzes larch wood arabinogalactan.

Characterization of Fusarium oxysporum beta-1,6-galactanase, an enzyme that hydrolyzes larch wood arabinogalactan. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

  • Abstract Text of This Paper
  • Journal Published
  • MeSH Keywords of This Abstract
  • Chemicals and Substances Used in this Paper
  • Grants and Granting Agency of this Research
  • Database Accession Numbers Used in this Paper
  • Related Papers
  • Related Research Tags
  • Rate this Research Paper
  • Characterization of Fusarium oxysporum beta-1,6-galactanase, an enzyme that hydrolyzes larch wood arabinogalactan. Abstract Text:

    tatsuji sakamotoTatsuji Sakamoto,yuya taniguchiYuya Taniguchi,shiho suzukiShiho Suzuki,hideshi iharaHideshi Ihara,haruhiko kawasakiHaruhiko Kawasaki,tatsuji sakamotoTatsuji Sakamoto,yuya taniguchiYuya Taniguchi,shiho suzukiShiho Suzuki,hideshi iharaHideshi Ihara,haruhiko kawasakiHaruhiko Kawasaki,

    A type II arabinogalactan-degrading enzyme (FoGal1) was purified from Fusarium oxysporum 12S, and the corresponding cDNA was isolated. FoGal1 had high similarity to enzymes of glycoside hydrolase family 5. Treatment of larch wood arabinogalactan with the recombinant enzyme indicated that FoGal1 is a beta-1,6-galactanase that preferentially debranches beta-1,6-galactobiose from the substrate.

    Characterization of Fusarium oxysporum beta-1,6-galactanase, an enzyme that hydrolyzes larch wood arabinogalactan. Publishing Authors By Initials

    t sakamotoT Sakamoto,y taniguchiY Taniguchi,s suzukiS Suzuki,h iharaH Ihara,h kawasakiH Kawasaki,t sakamotoT Sakamoto,y taniguchiY Taniguchi,s suzukiS Suzuki,h iharaH Ihara,h kawasakiH Kawasaki,

    For similar abstracts research abstracts see: abstracts research

    PUBMED ID PMID:

    MEDLINE DATE:

    Characterization of Fusarium oxysporum beta-1,6-galactanase, an enzyme that hydrolyzes larch wood arabinogalactan. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: Applied and environmental microbiology

    VOLUME: 73

    Page Numbers: 3109-12

    Journal Abbreviation:

    ISSN: 0099-2240

    DAY: 9

    MONTH: 03

    YEAR: 2007

    Characterization of Fusarium oxysporum beta-1,6-galactanase, an enzyme that hydrolyzes larch wood arabinogalactan. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 7605801

    Characterization of Fusarium oxysporum beta-1,6-galactanase, an enzyme that hydrolyzes larch wood arabinogalactan. Keywords Mesh Terms:

    KEYWORDS:

    MESH TERMS:

    Chemical & Substance for Abstract: Characterization of Fusarium oxysporum beta-1,6-galactanase, an enzyme that hydrolyzes larch wood arabinogalactan. Information

    Substance Name:

    Registry Number:

    Grant and Affiliation Information for Characterization of Fusarium oxysporum beta-1,6-galactanase, an enzyme that hydrolyzes larch wood arabinogalactan.

    AFFILIATION: Division of Applied Life Sciences, Graduate School of Life and Environmental Sciences, Osaka Prefecture University, Osaka 599-8531, Japan. sakamoto@biochem.osakafu-u.ac.jp

    Country: United States

    United States Research PublicationUnited States Research Publication

    AGENCY:

    GRANT:

    ACRONYM:

    MEDLINETA: Appl Environ Microbiol

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER:

    Number Hits: 0

    Characterization of Fusarium oxysporum beta-1,6-galactanase, an enzyme that hydrolyzes larch wood arabinogalactan Related Publications

     

    Molecular Station USER Menu

    Welcome to Molecular Station!

    You have to register before you can post on our forums or use our advanced features. Register Now! Its Free and Fast!

    Already registered? Login now below.

    User Name:

    Password:

    Already registered and Forgot your password? Click below to recover it.

    Recover Lost Password

    Join now - it's fast and free!

    Molecular Station is THE largest network of researchers, scientists and science lovers anywhere!

    Research Terms of Usage and Disclaimer
    Home
    Features

    Protocols

    DNA Forum

    Science Forum

    DNA Forum
    Biology Forum

    Science News


    [CaRP] XML error: Invalid document end at line 2

    For more click here:Science News