Structure-based replacement of methionine residues at the catalytic domains with serine significantly improves the oxidative stability of alkaline amylase from alkaliphilic Alkalimonas amylolytica

Biotechnology Progress

Volumn 28, Issue 5, 2012, Pages 1271-1277

  Yang, Haiquan ^a   Liu, Long ^a   Li, Jianghua ^a   Du, Guocheng ^a   Chen, Jian ^a  

^a JIANGNAN UNIVERSITY   (China)

Author keywords

Alkaline amylase; Methionine; Oxidative stability; Serine; Site directed mutagenesis

Indexed keywords

ALKALIPHILIC; AMINO ACID SEQUENCE; CATALYTIC DOMAINS; CATALYTIC EFFICIENCIES; CHEMICAL OXIDATION; ENZYME STRUCTURES; HIGH RESISTANCE; METHIONINE; METHIONINE RESIDUES; MUTANT ENZYMES; OXIDATIVE STABILITY; PH STABILITY; POTENTIAL APPLICATIONS; SERINE; SITE DIRECTED MUTAGENESIS; SODIUM DODECYL SULFATE; STRUCTURE-BASED; TEMPERATURE RANGE; WILD-TYPE ENZYMES;

ALKALINITY; AMINO ACIDS; OXIDATION RESISTANCE; PH EFFECTS; SODIUM; SODIUM SULFATE; SURFACE ACTIVE AGENTS; TEXTILE INDUSTRY;

AMYLASES;

ALKALI; AMYLASE; BACTERIAL PROTEIN; METHIONINE; SERINE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVE SITE; ENZYME STABILITY; ENZYMOLOGY; GAMMAPROTEOBACTERIA; GENETICS; KINETICS; METABOLISM; OXIDATION REDUCTION REACTION; PH; SITE DIRECTED MUTAGENESIS; TEMPERATURE;

ALKALIES; ALPHA-AMYLASES; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; CATALYTIC DOMAIN; ENZYME STABILITY; GAMMAPROTEOBACTERIA; HYDROGEN-ION CONCENTRATION; KINETICS; METHIONINE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; SERINE; TEMPERATURE;

ALKALIMONAS AMYLOLYTICA;

EID: 84867399854     PISSN: 87567938     EISSN: 15206033     Source Type: Journal    
DOI: 10.1002/btpr.1611     Document Type: Article

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