Hyperthermostabilization of Bacillus licheniformis α-amylase and modulation of its stability over a 50°C temperature range

Protein Engineering

Volumn 16, Issue 4, 2003, Pages 287-293

  Declerck, Nathalie ^a,d   Machius, Mischa ^b   Joyet, Philippe ^a   Wiegand, Georg ^c   Huber, Robert ^c   Gaillardin, Claude ^a  

^a CNRS   (France)

^b UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

^c MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

^d INSERM   (France)

Author keywords

Bacterial amylase; Enzyme engineering; Mutagenesis; Protein modelling; Thermostability

Indexed keywords

AMYLASE; ASPARAGINE; ENZYME VARIANT; GLUTAMINE; SERINE; STARCH; TYROSINE;

AMINO ACID SUBSTITUTION; ARTICLE; BACILLUS LICHENIFORMIS; BINDING SITE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME ENGINEERING; ENZYME INACTIVATION; ENZYME STABILITY; HIGH TEMPERATURE; METAL BINDING; MOLECULAR MODEL; MUTAGENESIS; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; THERMOSTABILITY;

BACILLUS LICHENIFORMIS; BACTERIA (MICROORGANISMS); POSIBACTERIA;

EID: 0037900194     PISSN: 02692139     EISSN: None     Source Type: Journal    
DOI: 10.1093/proeng/gzg032     Document Type: Article

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