Characterization of the 4,6-α-glucanotransferase GTFB enzyme of Lactobacillus reuteri 121 isolated from inclusion bodies

BMC Biotechnology

Volumn 15, Issue 1, 2015, Pages

  Bai, Yuxiang ^a,c   van der Kaaij, Rachel Maria ^a   Jacob Woortman, Albert Jan ^b   Jin, Zhengyu ^c   Dijkhuizen, Lubbert ^a  

^a UNIVERSITY OF GRONINGEN   (Netherlands)

^b UNIVERSITY OF GRONINGEN   (Netherlands)

^c JIANGNAN UNIVERSITY   (China)

Author keywords

4,6 glucanotransferase; Dietary fiber; GTFB enzyme; Inclusion bodies; Lactobacillus reuteri; Modified starch

Indexed keywords

ESCHERICHIA COLI; HYDROLYSIS; STABILITY; STARCH;

DIETARY FIBERS; GLUCANOTRANSFERASE; INCLUSION BODIES; LACTOBACILLUS REUTERI; MODIFIED STARCHES;

ENZYMES;

4,6 ALPHA GLUCANOTRANSFERASE GTFB; GLYCOSIDASE; UNCLASSIFIED DRUG; 4 ALPHA-GLUCANOTRANSFERASE; BACTERIAL PROTEIN; GLYCOGEN DEBRANCHING ENZYME;

ANION EXCHANGE CHROMATOGRAPHY; ARTICLE; BACTERIUM ISOLATE; BIOACCUMULATION; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME DENATURATION; ESCHERICHIA COLI; HIGH PH ANION EXCHANGE CHROMATOGRAPHY; INFRARED SPECTROSCOPY; LACTOBACILLUS REUTERI; NONHUMAN; PROTEIN EXPRESSION; PROTEIN HYDROLYSIS; PROTEIN REFOLDING; PROTON NUCLEAR MAGNETIC RESONANCE; SIZE EXCLUSION CHROMATOGRAPHY; THERMOSTABILITY; BIOSYNTHESIS; CELL INCLUSION; CHEMISTRY; COMPARATIVE STUDY; ENZYME SPECIFICITY; ENZYME STABILITY; ENZYMOLOGY; GENETICS; ISOLATION AND PURIFICATION; METABOLISM; MOLECULAR MODEL; PROTEIN DENATURATION; PROTEIN SECONDARY STRUCTURE; SOLUBILITY;

BACTERIAL PROTEINS; ENZYME STABILITY; ESCHERICHIA COLI; GLYCOGEN DEBRANCHING ENZYME SYSTEM; INCLUSION BODIES; LACTOBACILLUS REUTERI; MODELS, MOLECULAR; PROTEIN DENATURATION; PROTEIN REFOLDING; PROTEIN STRUCTURE, SECONDARY; SOLUBILITY; SUBSTRATE SPECIFICITY;

EID: 84931055313     PISSN: None     EISSN: 14726750     Source Type: Journal    
DOI: 10.1186/s12896-015-0163-7     Document Type: Article

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