Improvement of Bacillus circulans -amylase activity attained using the ancestral mutation method

Protein Engineering, Design and Selection

Volumn 23, Issue 7, 2010, Pages 519-528

  Yamashiro, Kan ^a   Yokobori, Shin Ichi ^b   Koikeda, Satoshi ^a   Yamagishi, Akihiko ^b  

^a Amano Enzyme Inc   (Japan)

^b TOKYO UNIVERSITY OF PHARMACY AND LIFE SCIENCES   (Japan)

Author keywords

amylase; ancestral mutation method; Bacillus circulans; mesophile; thermostabilization

Indexed keywords

AMINO ACID RESIDUES; AMYLASE ACTIVITY; ANCESTRAL MUTATION METHOD; BACILLUS CIRCULANS; HIGHER PLANTS; MESOPHILES; MESOPHILIC; MUTATION SITES; PHYLOGENETIC TREES; PROTEIN ENGINEERING; THERMOPHILIC ENZYMES; THERMOSTABILIZATION; WILD TYPES;

AMINO ACIDS; BIOCHEMICAL ENGINEERING; CATALYSTS; ENZYMES; GENETIC ENGINEERING; ORGANIC ACIDS;

BACTERIOLOGY;

BETA AMYLASE;

AMINO ACID SEQUENCE; ARTICLE; BACILLUS CIRCULANS; CORRELATION ANALYSIS; DENATURATION; ENZYME ACTIVITY; ESCHERICHIA COLI; MUTATIONAL ANALYSIS; NONHUMAN; NUCLEOTIDE SEQUENCE; PHYLOGENETIC TREE; PRIORITY JOURNAL; PROTEIN EXPRESSION; TEMPERATURE SENSITIVITY; THERMOSTABILITY;

BACILLUS; BACTERIAL PROTEINS; BETA-AMYLASE; ENZYME STABILITY; HALF-LIFE; MODELS, MOLECULAR; MUTAGENESIS; PHYLOGENY; PROTEIN DENATURATION; PROTEIN ENGINEERING; TEMPERATURE;

BACILLUS CIRCULANS; BACTERIA (MICROORGANISMS); EMBRYOPHYTA;

EID: 77955959569     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzq021     Document Type: Article

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