α-Amylase (AmyP) of glycoside hydrolase subfamily GH13-37 is resistant to various toxic compounds

Journal of Molecular Catalysis B: Enzymatic

Volumn 98, Issue , 2013, Pages 114-118

  Peng, Hui ^a   Wang, Ying ^a   Zheng, Yunyun ^a   Wang, Min ^a   Xiao, Yazhong ^a   Gao, Yi ^a  

^a ANHUI UNIVERSITY   (China)

Author keywords

Amylase; Organic solvent tolerant; Oxidizing agents stable; Reducing agents stable; Surfactant stable

Indexed keywords

GLYCOSIDE HYDROLASES; HYDROPHILIC SOLVENTS; HYDROPHOBIC SOLVENT; METAGENOMIC LIBRARIES; OPTIMAL CONCENTRATION; OXIDIZING AGENTS; SEQUENCE SIMILARITY; SOLVENT TOLERANT;

METAL IONS; OXIDATION;

AMYLASES;

1,4 BUTANEDIOL; ALCOHOL; AMYLASE; ANIONIC SURFACTANT; CALCIUM; CUPROUS ION; CYCLOHEXANE; DIMETHYL SULFOXIDE; GLYCOSIDASE; HEXANE; IRON; LITHIUM ION; MANGANESE; MERCAPTOETHANOL; MERCURY; NICKEL; OCTANE; OCTANOL; ORGANIC SOLVENT; OXIDIZING AGENT; POLYSORBATE 20; POLYSORBATE 40; SODIUM CHLORIDE; SOLVENT; TOLUENE; TRITON X 100; ZINC;

ALICYCLOBACILLUS ACIDOCALDARIUS; ARTICLE; BACILLUS; CONCENTRATION (PARAMETERS); CONFORMATIONAL TRANSITION; ENZYME ACTIVITY; ENZYME INACTIVATION; ENZYME STABILITY; ESCHERICHIA COLI; HYDROPHILICITY; HYDROPHOBICITY; METAGENOMICS; NONHUMAN; PROTEIN EXPRESSION; SACCHAROPOLYSPORA; STREPTOMYCES;

EID: 84887089439     PISSN: 13811177     EISSN: 18733158     Source Type: Journal    
DOI: 10.1016/j.molcatb.2013.10.003     Document Type: Article

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