Characterization of a new and thermostable esterase from a metagenomic library

Microbiological Research

Volumn 168, Issue 9, 2013, Pages 589-597

  Zhu, Yanbing ^a,b   Li, Jianbo ^c   Cai, Huinong ^b   Ni, Hui ^b   Xiao, Anfeng ^b   Hou, Luhong ^a  

^a SOA Fujian Collaborative Innovation Center for Exploitation and Utilization of Marine Biological Resources Key Laboratory of Marine Genetic   (China)

^b JIMEI UNIVERSITY   (China)

^c XIAMEN UNIVERSITY   (China)

Author keywords

Characterization; Esterase; Metagenome

Indexed keywords

CATALYTIC MECHANISMS; ESTERASE; ESTERASE ACTIVITIES; METAGENOMES; METAGENOMIC LIBRARIES; P-NITROPHENYL ACETATE; PHENYLMETHYLSULFONYL FLUORIDE; THERMOSTABLE ESTERASE;

AMINO ACIDS; BACTERIOLOGY; CHARACTERIZATION; CLONING; ENZYMES; ESCHERICHIA COLI; ESTERS; GENE ENCODING; SUBSTRATES;

CATALYST ACTIVITY;

ACETATE; AMINO ACID; DEEP-SEA ORGANISM; ENZYME; FLUORIDE; GENE; HOMOGENEITY; HOMOLOGY; INCUBATION; PROTEIN; SEDIMENT;

PACIFIC OCEAN; PACIFIC OCEAN (EAST);

BACILLUS SP. H-257; ESCHERICHIA COLI;

BENZYLSULFONYL FLUORIDE; ENZYME INHIBITOR; ESTERASE; RECOMBINANT PROTEIN;

ARTICLE; CHARACTERIZATION; CHEMICAL STRUCTURE; CHEMISTRY; DNA SEQUENCE; ENZYME SPECIFICITY; ENZYME STABILITY; GENE EXPRESSION; GENE LIBRARY; GENETICS; HYDROTHERMAL VENT; ISOLATION AND PURIFICATION; METABOLISM; METAGENOME; MOLECULAR CLONING; MOLECULAR GENETICS; MOLECULAR WEIGHT; NUCLEOTIDE SEQUENCE; OPEN READING FRAME; PH; PROTEIN CONFORMATION; SEDIMENT; TEMPERATURE;

CHARACTERIZATION; ESTERASE; METAGENOME;

CLONING, MOLECULAR; ENZYME INHIBITORS; ENZYME STABILITY; ESTERASES; GENE EXPRESSION; GENE LIBRARY; GEOLOGIC SEDIMENTS; HYDROGEN-ION CONCENTRATION; HYDROTHERMAL VENTS; METAGENOME; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; OPEN READING FRAMES; PHENYLMETHYLSULFONYL FLUORIDE; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SEQUENCE ANALYSIS, DNA; SUBSTRATE SPECIFICITY; TEMPERATURE;

EID: 84883137461     PISSN: 09445013     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.micres.2013.04.004     Document Type: Article

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