Characterization of an L-arabinose isomerase from Bacillus coagulans NL01 and its application for D-tagatose production

BMC Biotechnology

Volumn 16, Issue 1, 2016, Pages

  Mei, Wending ^a   Wang, Lu ^a   Zang, Ying ^a   Zheng, Zhaojuan ^a   Ouyang, Jia ^a,b  

^a NANJING FORESTRY UNIVERSITY   (China)

^b BEIJING UNIVERSITY OF POSTS AND TELECOMMUNICATIONS   (China)

Author keywords

Bacillus coagulans; Biotransformation; D tagatose; L arabinose isomerase

Indexed keywords

BACTERIOLOGY; BIOCONVERSION; ENERGY EFFICIENCY; ESCHERICHIA COLI; PURIFICATION; REACTION KINETICS;

BACILLUS COAGULANS; BIOTRANSFORMATION; BIOTRANSFORMATION SYSTEM; CATALYTIC EFFICIENCIES; D-TAGATOSE; ESCHERICHIA COLI BL21; L-ARABINOSE ISOMERASE; SUBSTRATE SPECIFICITY;

CLONING;

ARABINOSE; ISOMERASE; TAGATOSE; GALACTOSE; HEXOSE; L-ARABINOSE ISOMERASE; PROTEIN BINDING; RECOMBINANT PROTEIN; SWEETENING AGENT;

ARTICLE; BACILLUS COAGULANS; BACILLUS COAGULANS NL01; BACTERIAL CELL; CARBOHYDRATE ANALYSIS; CARBOHYDRATE SYNTHESIS; CATALYSIS; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; ESCHERICHIA COLI; GENETIC CODE; MOLECULAR CLONING; NONHUMAN; PH; THERMOSTABILITY; BINDING SITE; CHEMICAL MODEL; CHEMISTRY; CLASSIFICATION; ENZYME ACTIVATION; ENZYME SPECIFICITY; ENZYME STABILITY; ENZYMOLOGY; GENETICS; METABOLISM; MOLECULAR DOCKING; SPECIES DIFFERENCE; SYNTHESIS;

ALDOSE-KETOSE ISOMERASES; BACILLUS COAGULANS; BINDING SITES; CLONING, MOLECULAR; ENZYME ACTIVATION; ENZYME STABILITY; ESCHERICHIA COLI; GALACTOSE; HEXOSES; MODELS, CHEMICAL; MOLECULAR DOCKING SIMULATION; PROTEIN BINDING; RECOMBINANT PROTEINS; SPECIES SPECIFICITY; SUBSTRATE SPECIFICITY; SWEETENING AGENTS;

EID: 84976870686     PISSN: None     EISSN: 14726750     Source Type: Journal    
DOI: 10.1186/s12896-016-0286-5     Document Type: Article

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