Applied Microbiology and Biotechnology

, Volume 73, Issue 6, pp 1331–1339

Cloning and functional expression of thermostable β-glucosidase gene from Thermoascus aurantiacus

Biotechnologically Relevant Enzymes and Proteins

DOI: 10.1007/s00253-006-0618-9

Cite this article as:
Hong, J., Tamaki, H. & Kumagai, H. Appl Microbiol Biotechnol (2007) 73: 1331. doi:10.1007/s00253-006-0618-9

Abstract

A thermostable β-glucosidase (BGLI) was purified from Thermoascus aurantiacus IFO9748, and the gene (bgl1) encoding this enzyme was cloned and expressed in yeast Pichia pastoris. The deduced amino acid sequence encoded by bgl1 showed high similarity with the sequence of glycoside hydrolase family 3. The recombinant enzyme was purified and subjected to enzymatic characterization. Recombinant BGLI retained more than 70% of its initial activity after 1 h of incubation at 60°C and was stable in the pH range 3–8. The optimal temperature for enzyme activity was about 70°C and the optimal pH was about 5. P. pastoris expressing recombinant BGLI became able to utilize cellobiose as a carbon source.

Copyright information

© Springer-Verlag 2006

Authors and Affiliations

  1. 1.Laboratory of Applied Microbiology, Research Institute of Bioresources and BiotechnologyIshikawa Prefectural UniversityIshikawaJapan
  2. 2.Division of Integrated Life Science, Graduate School of BiostudiesKyoto UniversityKyotoJapan

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