Genetic and Structural Characterization of a Thermo-Tolerant, Cold-Active, and Acidic Endo-β-1,4-glucanase from Antarctic Springtail, Cryptopygus antarcticus

Jung Min Song, Seung Kon Hong, Young Jun An, Mee Hye Kang, Kwon Ho Hong, Youn Ho Lee, Sun Shin Cha

Research output: Contribution to journalArticlepeer-review

23 Scopus citations

Abstract

The CaCel gene from Antarctic springtail Cryptopygus antarcticus codes for a cellulase belonging to the glycosyl hydrolase family 45 (GHF45). Phylogenetic, biochemical, and structural analyses revealed that the CaCel gene product (CaCel) is closely related to fungal GHF45 endo-β-1,4-glucanases. The organization of five introns within the open reading frame of the CaCel gene indicates its endogenous origin in the genome of the species, which suggests the horizontal transfer of the gene from fungi to the springtail. CaCel exhibited optimal activity at pH 3.5, retained 80% of its activity at 0-10 °C, and maintained a half-life of 4 h at 70 °C. Based on the structural comparison between CaCel and a fungal homologue, we deduced the structural basis for the unusual characteristics of CaCel. Under acidic conditions at 50 °C, CaCel was effective to digest the green algae (Ulva pertusa), suggesting that it could be exploited for biofuel production from seaweeds.

Original languageEnglish
Pages (from-to)1630-1640
Number of pages11
JournalJournal of Agricultural and Food Chemistry
Volume65
Issue number8
DOIs
StatePublished - 1 Mar 2017

Bibliographical note

Publisher Copyright:
© 2017 American Chemical Society.

Keywords

  • Cryptopygus antarcticus
  • biochemical and structural features
  • biofuel production from seaweeds
  • cold-active cellulase
  • endo-β-1,4-glucanase
  • horizontal gene transfer

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