Enhancement of hydrolytic activity of thermophilic alkalophilic α-amylase from Bacillus sp. AAH-31 through optimization of amino acid residues surrounding the substrate binding site

Biochemical Engineering Journal

Volumn 86, Issue , 2014, Pages 8-15

  Tamamura, Naoya ^a   Saburi, Wataru ^a   Mukai, Atsushi ^a   Morimoto, Naoki ^b   Takehana, Toshihiko ^b   Koike, Seiji ^b   Matsui, Hirokazu ^a   Mori, Haruhide ^a  

^a HOKKAIDO UNIVERSITY   (Japan)

^b ADEKA CORPORATION   (Japan)

Author keywords

Amylase; Enzyme activity; Enzyme production; Glycoside hydrolase family 13; Mutagenesis; Starch

Indexed keywords

AMINO ACIDS; BACTERIOLOGY; ENZYME ACTIVITY; MUTAGENESIS; OPTIMIZATION; STARCH;

ALKALOPHILIC; AMINO ACID RESIDUES; ENZYME PRODUCTION; GLYCOSIDE HYDROLASES; HYDROLYTIC ACTIVITIES; SINGLE MUTATION; SOLUBLE STARCH; SUBSTRATE-BINDING SITES;

AMYLASES;

ALANINE; AMINO ACID; AMYLASE; BACTERIAL ENZYME; DOUBLE MUTANT ENZYME; GLUTAMIC ACID; GLYCINE; H431A/K549M; HISTIDINE; I509A/K549M; ISOLEUCINE; LYSINE; METHIONINE; QUADRUPLE MUTANT ENZYME; SERINE; TRIPLE MUTANT ENZYME; TYROSINE; UNCLASSIFIED DRUG; Y426S/K549M;

ALKALINITY; AMINO ACID ANALYSIS; AMINO ACID SEQUENCE; ARTICLE; BACILLUS; BACILLUS SP AAH31; BACTERIAL MUTATION; BACTERIAL STRAIN; BINDING SITE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME STABILITY; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; HYDROLYSIS KINETICS; MUTANT; NONHUMAN; PRIORITY JOURNAL; THERMOSTABILITY; WILD TYPE;

EID: 84896140132     PISSN: 1369703X     EISSN: 1873295X     Source Type: Journal    
DOI: 10.1016/j.bej.2014.02.014     Document Type: Article

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