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Xylosidases associated with the cell surface of Penicillium herquei IFO 4674

Tatsuo Ito1, Eiji Yokoyama, Hiroaki Sato

  • 1Department of Applied Biological Chemistry, Faculty of Agriculture, Meijo University, Nagoya 468-8502, Japan.

Journal of Bioscience and Bioengineering
|October 20, 2005
PubMed

Insights

Penicillium herquei produced two beta-xylosidases, S1 and S2, with distinct properties. S1 showed transxylosylation activity and glycerol activation, unlike S2, whose gene was cloned and characterized.

Area of Science:

  • Biochemistry
  • Enzymology
  • Molecular Biology

Background:

  • Filamentous fungi like Penicillium herquei are sources of enzymes.
  • Hydrolases are crucial for breaking down polysaccharides.
  • Beta-xylosidases play a role in carbohydrate metabolism.

Purpose of the Study:

  • To purify and characterize beta-xylosidases from Penicillium herquei.
  • To investigate the enzymatic properties and gene of beta-xylosidase S2.

Main Methods:

  • Purification of beta-xylosidases S1 and S2.
  • Mass spectrometry (MALDI-TOF-MS) for molecular mass determination.
  • Polymerase chain reaction (PCR) for gene cloning.

Main Results:

  • Two beta-xylosidases, S1 (103,700 Da) and S2 (37,460 Da), were purified.
  • S1 exhibited optimal activity at pH 4.0, was activated by glycerol, and showed transxylosylation.
  • S2 had optimal activity at pH 6.5, was unaffected or inhibited by glycerol, and lacked transxylosylation. The s2 gene encoded 335 amino acids.

Conclusions:

  • Penicillium herquei secretes distinct beta-xylosidases with differing biochemical properties.
  • The cloned s2 gene encodes a non-secreted beta-xylosidase belonging to glycoside hydrolase family 43.
  • Enzyme S1 possesses unique characteristics, including transxylosylation and glycerol activation, suggesting potential applications.

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