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Acid xylanase from yeast Cryptococcus sp. S-2: purification, characterization, cloning, and sequencing

H Iefuji1, M Chino, M Kato

  • 1National Research Institute of Brewing, Higashi-hiroshima, Japan.

Bioscience, Biotechnology, and Biochemistry
|August 1, 1996
PubMed
Summary

Researchers isolated and purified an acidophilic endoxylanase (xyn-CS2) from yeast Cryptococcus sp. S-2. This enzyme exhibits high activity at low pH, suggesting unique catalytic properties for xylan degradation.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Microbiology

Background:

  • Xylan-degrading enzymes are crucial for biomass processing.
  • Acidophilic enzymes are valuable for industrial applications under acidic conditions.
  • The yeast Cryptococcus sp. S-2 is a potential source of novel enzymes.

Purpose of the Study:

  • To isolate and characterize a novel xylan-degrading enzyme from Cryptococcus sp. S-2.
  • To investigate the biochemical properties of the purified enzyme, focusing on its pH profile.
  • To analyze the enzyme's amino acid sequence and compare it with known xylanases.

Main Methods:

  • Enzyme isolation and purification from yeast culture supernatant.
  • Biochemical characterization including molecular weight, isoelectric point, and pH optimum determination.

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  • cDNA cloning, sequencing, and deduced amino acid sequence analysis.
  • Comparison of the deduced sequence with known xylanase families.

    • Main Results:

    • A low-molecular-weight endoxylanase (xyn-CS2) was successfully isolated and purified.
    • The enzyme exhibited an unusual pH optimum of 2.0, retaining significant activity at pH 1.0.
    • The deduced amino acid sequence revealed similarities to family-G xylanases and contained unique cysteine residues.
    • The molecular weight was determined to be 22,000, with an isoelectric point of 7.4.

    Conclusions:

    • Cryptococcus sp. S-2 produces an acidophilic endoxylanase (xyn-CS2) with unique properties.
    • The enzyme's acidophilic nature may be linked to the presence of unique cysteine residues in its catalytic region.
    • This novel enzyme holds potential for applications in acidic environments for xylan degradation.