Properties of a thermoactive β-1,3-1,4-glucanase (lichenase) from Clostridium thermocellum expressed in Escherichia coli

Biochemical and Biophysical Research Communications

Volumn 177, Issue 1, 1991, Pages 447-452

  Schimming, Silke ^a   Schwarz, Wolfgang H ^a   Staudenbauer, Walter L ^a  

^a TECHNICAL UNIVERSITY OF MUNICH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

DNA; GLUCAN GLUCOSIDASE; LICHENASE; UNCLASSIFIED DRUG;

ARTICLE; BACTERIUM; BEER; NONHUMAN; PRIORITY JOURNAL; RECOMBINANT DNA TECHNOLOGY;

CLONING, MOLECULAR; CLOSTRIDIUM; ESCHERICHIA COLI; GLYCOSIDE HYDROLASES; HEAT; HYDROGEN-ION CONCENTRATION; KINETICS; RECOMBINANT PROTEINS; RESTRICTION MAPPING; SUBSTRATE SPECIFICITY; SUPPORT, NON-U.S. GOV'T; THERMODYNAMICS;

BACTERIA (MICROORGANISMS); CLOSTRIDIUM THERMOCELLUM; ESCHERICHIA COLI; HORDEUM VULGARE SUBSP. VULGARE;

EID: 0025772933     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/0006-291X(91)92004-4     Document Type: Article

References (18)

1. Molecular cloning of a gene coding for thermostable beta-glucanase fromBacillus macerans
2. Purification and properties of a 1,3-1,4-beta-D-glucanase (lichenase, 1,3-1,4-beta-D-glucan 4-glucanohydrolase, EC 3.2.1.73) from Bacteroides succinogenes cloned in Escherichia coli.
3. A rapid, sensitive, and versatile assay for protein using Coomassie brilliant blue G250