IDEAS home Printed from https://ideas.repec.org/a/adp/jomcij/v10y2020i2p73-81.html
   My bibliography  Save this article

The Synergism of a Novel Thermostable Acetyl Xylan Esterase with Cellulase Degrade Wheat Straw

Author

Listed:
  • Xiaoshen Zhao
  • Jin Xu

    (School of Life Sciences and Biopharmaceuticals, Guangdong Pharmaceutical University, China)

  • Liyang Liu

    (Guangdong Key Laboratory of Bioactive Drug Research, China)

  • Zujun Deng
  • Shan Liu
  • Jeonyun Yun

    (Business School of Medicine, Guangdong Pharmaceutical University, China)

  • Xiong Xiao
  • He Li

    (Guangzhou Yachun Cosmetics Manufacturing Co., Ltd, China)

Abstract

Acetyl xylan esterase is one of the key enzymes in xylan degradation enzyme system. However, acetyl xylan esterase from natural microorganisms has low expression, low enzyme activity and impure product. In this study, a new xylanase gene, est1051, from the metagenomic library, was expressed in prokaryotic system. Enzymatic properties, including optimum temperature and pH, thermal and pH stability, organic solvent, metal ion and salt solution tolerance were explored. Finally, the synergism with cellulase on degrading straw was identified and evaluated. EST1051 displayed high homology with acetyl xylan esterases in amino acid sequences and conserved active sites. And EST1051 showed good stability across a broad temperature range, its enzymatic activities had been retained more than 50% between 4℃ and 50℃ after 24 hours of incubation.

Suggested Citation

  • Xiaoshen Zhao & Jin Xu & Liyang Liu & Zujun Deng & Shan Liu & Jeonyun Yun & Xiong Xiao & He Li, 2020. "The Synergism of a Novel Thermostable Acetyl Xylan Esterase with Cellulase Degrade Wheat Straw," Organic & Medicinal Chemistry International Journal, Juniper Publishers Inc., vol. 10(2), pages 73-81, December.
    • Handle: RePEc:adp:jomcij:v:10:y:2020:i:2:p:73-81
    DOI: 10.19080/OMCIJ.2020.10.555785
    as

    Download full text from publisher

    File URL: https://juniperpublishers.com/omcij/pdf/OMCIJ.MS.ID.555785.pdf
    Download Restriction: no
    File URL: https://juniperpublishers.com/omcij/OMCIJ.MS.ID.555785.php
    Download Restriction: no
    File URL: https://libkey.io/10.19080/OMCIJ.2020.10.555785?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:adp:jomcij:v:10:y:2020:i:2:p:73-81. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Robert Thomas (email available below). General contact details of provider: .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.