Production of xylanase from a novel engineered Pichia pastoris and application to enzymatic hydrolysis process for biorefinery

  • Chan Kyum Kim
  • , Han Suk Choi
  • , Sang Jun Lee
  • , Ja Hyun Lee
  • , Ju Hun Lee
  • , Hah Young Yoo
  • , Sung Ok Han
  • , Seung Wook Kim*
  • *Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    20 Citations (Scopus)

    Abstract

    In this study, the xylanase gene from Cellulomonas flavigena KCTC 9104 was cloned into pPICZαB and expressed in Pichia pastoris X-33. An extracellular endo-1,4-β-xylanase was produced by novel engineered P. pastoris (rXynCf) and purified by Ni-NTA affinity column. Characterization of rXynCf was performed and results are as follows: 38 kDa molecular weight, 55 °C optimum temperature and optimum pH of 6. Under the conditions, the Km and Vmax of rXynCf were 3.6 ± 0.08 mg/mL and 4505 ± 52 μmol/min mg, respectively. rXynCf was applied in enzymatic hydrolysis process for sugars production from lignocellulosic biomass. Empty fruit bunch (EFB) was selected as a feedstock, and the total sugars conversion was found to be 3.8%, meanwhile the conversion by alkaline pretreatment improved approximately 16-fold (61.1%). In addition, rXynCf shows similar xylose conversion to commercial xylanase. Therefore, due to its properties, rXynCf has considerable potential in biorefinery applications.

    Original languageEnglish
    Pages (from-to)130-135
    Number of pages6
    JournalProcess Biochemistry
    Volume65
    DOIs
    Publication statusPublished - 2018 Feb

    Bibliographical note

    Publisher Copyright:
    © 2017 Elsevier Ltd

    Keywords

    • Biorefinery
    • Cellulomonas flavigena
    • Enzymatic hydrolysis
    • Pichia pastoris
    • Xylanase

    ASJC Scopus subject areas

    • Bioengineering
    • Biochemistry
    • Applied Microbiology and Biotechnology

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