A novel domain arrangement in a monomeric cyclodextrin-hydrolyzing enzyme from the hyperthermophile Pyrococcus furiosus

Author:

Park Jong-Tae,Song Hyung-Nam,Jung Tae-Yang,Lee Myoung-Hee,Park Sung-Goo,Woo Eui-Jeon,Park Kwan-Hwa

Funder

Marine & Extreme Genome Research Center program from the Ministry of Land, Transport and Maritime Affairs, Republic of Korea

Mid-career Researcher Program through the National Research Foundation (NRF) in the Ministry of Education, Science and Technology

Next-Generation BioGreen 21 Program

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry

Reference35 articles.

1. Industrial relevance of thermophilic archaea;Egorova;Curr. Opin. Microbiol.,2005

2. Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability;Vieille;Microbiol. Mol. Biol. Rev.,2001

3. Properties and applications of starch-converting enzymes of the α-amylase family;van der Maarel;J. Biotechnol.,2002

4. Properties of a novel thermostable glucoamylase from the hyperthermophilic archaeon Sulfolobus solfataricus in relation to starch processing;Kim;Appl. Environ. Microbiol.,2004

5. Characterization and application of a novel thermostable glucoamylase cloned from a hyperthermophilic archaeon Sulfolobus tokodaii;Njoroge;Food Sci. Biotechnol.,2005

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