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Hyperthermostable endoglucanase from Pyrococcus horikoshii.

Susumu Ando1, Hiroyasu Ishida, Yoshitsugu Kosugi

  • 1National Institute of Advanced Industrial Science and Technology, Kansai, Ikeda, Osaka 563-8577, Japan. andosusumu@hotmail.com

Applied and Environmental Microbiology
|January 5, 2002
PubMed
Summary

Researchers discovered a hyperthermostable endoglucanase from Pyrococcus horikoshii. This enzyme efficiently hydrolyzes cellulose, showing potential for industrial applications like cotton biopolishing at high temperatures.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Microbial biotechnology

Background:

  • Hyperthermophilic archaea, such as Pyrococcus horikoshii, are sources of robust enzymes.
  • Endoglucanases are crucial for cellulose hydrolysis, with industrial applications in various sectors.
  • Glycosidase family 5 enzymes are widespread but hyperthermostable variants with cellulose as a preferred substrate are rare.

Purpose of the Study:

  • To express and characterize an endoglucanase homolog from Pyrococcus horikoshii.
  • To investigate the substrate specificity and optimal conditions for the enzyme's activity.
  • To assess the potential industrial utility of this hyperthermostable endoglucanase.

Main Methods:

  • Gene expression of the Pyrococcus horikoshii endoglucanase homolog in Escherichia coli.

Related Experiment Videos

  • Enzymatic assays using various cellulosic substrates (Avicel, carboxymethyl cellulose) and beta-glucose oligomers.
  • Determination of enzyme stability at high temperatures.

    • Main Results:

    • Successfully expressed a hyperthermostable endoglucanase.
    • The enzyme demonstrated efficient hydrolysis of cellulose and beta-glucose oligomers.
    • This represents the first glycosidase family 5 endoglucanase from Pyrococcus species with cellulose as the optimal substrate.

    Conclusions:

    • The characterized endoglucanase is a novel hyperthermostable enzyme with significant potential for industrial cellulose hydrolysis.
    • Its high thermal stability and substrate preference make it suitable for applications like cotton biopolishing.
    • This discovery expands the toolkit of enzymes available for high-temperature biotechnological processes.