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Applied and Environmental Microbiology, October 2004, p. 5988-5995, Vol. 70, No. 10
0099-2240/04/$08.00+0     DOI: 10.1128/AEM.70.10.5988-5995.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Enzymatic Analysis of an Amylolytic Enzyme from the Hyperthermophilic Archaeon Pyrococcus furiosus Reveals Its Novel Catalytic Properties as both an {alpha}-Amylase and a Cyclodextrin-Hydrolyzing Enzyme

Sung-Jae Yang,1 Hee-Seob Lee,1 Cheon-Seok Park,2 Yong-Ro Kim,3 Tae-Wha Moon,1* and Kwan-Hwa Park1*

National Laboratory for Functional Food Carbohydrates, Center for Agricultural Biomaterials, and Department of Food Science and Technology,1 School of Biological Resources and Materials Engineering, Seoul National University, Seoul,3 Department of Food Science and Technology, Kyunghee University, Yongin, Korea2

Received 11 February 2004/ Accepted 11 June 2004

Genomic analysis of the hyperthermophilic archaeon Pyrococcus furiosus revealed the presence of an open reading frame (ORF PF1939) similar to the enzymes in glycoside hydrolase family 13. This amylolytic enzyme, designated PFTA (Pyrococcus furiosus thermostable amylase), was cloned and expressed in Escherichia coli. The recombinant PFTA was extremely thermostable, with an optimum temperature of 90°C. The substrate specificity of PFTA suggests that it possesses characteristics of both {alpha}-amylase and cyclodextrin-hydrolyzing enzyme. Like typical {alpha}-amylases, PFTA hydrolyzed maltooligosaccharides and starch to produce mainly maltotriose and maltotetraose. However, it could also attack and degrade pullulan and ß-cyclodextrin, which are resistant to {alpha}-amylase, to primarily produce panose and maltoheptaose, respectively. Furthermore, acarbose, a potent {alpha}-amylase inhibitor, was drastically degraded by PFTA, as is typical of cyclodextrin-hydrolyzing enzymes. These results confirm that PFTA possesses novel catalytic properties characteristic of both {alpha}-amylase and cyclodextrin-hydrolyzing enzyme.

* Corresponding author. Mailing address: Department of Food Science and Technology, Seoul National University, Shillim-dong, Kwanak-gu, Seoul 151-742, Korea. Phone: 82-2-8804854/8804852. Fax: 82-2-8735095. E-mail: twmoon{at}snu.ac.kr; parkkh{at}plaza.snu.ac.kr.

Applied and Environmental Microbiology, October 2004, p. 5988-5995, Vol. 70, No. 10
0099-2240/04/$08.00+0     DOI: 10.1128/AEM.70.10.5988-5995.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Yang, S.-J., Min, B.-C., Kim, Y.-W., Jang, S.-M., Lee, B.-H., Park, K.-H. (2007). Changes in the Catalytic Properties of Pyrococcus furiosus Thermostable Amylase by Mutagenesis of the Substrate Binding Sites. Appl. Environ. Microbiol. 73: 5607-5612 [Abstract] [Full Text]  
  • Lee, H.-S., Shockley, K. R., Schut, G. J., Conners, S. B., Montero, C. I., Johnson, M. R., Chou, C.-J., Bridger, S. L., Wigner, N., Brehm, S. D., Jenney, F. E. Jr., Comfort, D. A., Kelly, R. M., Adams, M. W. W. (2006). Transcriptional and Biochemical Analysis of Starch Metabolism in the Hyperthermophilic Archaeon Pyrococcus furiosus. J. Bacteriol. 188: 2115-2125 [Abstract] [Full Text]  


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