| RRC ID |
15825
|
| Author |
Ojima T, Saburi W, Sato H, Yamamoto T, Mori H, Matsui H.
|
| Title |
Biochemical characterization of a thermophilic cellobiose 2-epimerase from a thermohalophilic bacterium, Rhodothermus marinus JCM9785.
|
| Journal |
Biosci Biotechnol Biochem
|
| Abstract |
Cellobiose 2-epimerase (CE) reversibly converts glucose residue to mannose residue at the reducing end of β-1,4-linked oligosaccharides. It efficiently produces epilactose carrying prebiotic properties from lactose, but the utilization of known CEs is limited due to thermolability. We focused on thermoholophilic Rhodothermus marinus JCM9785 as a CE producer, since a CE-like gene was found in the genome of R. marinus DSM4252. CE activity was detected in the cell extract of R. marinus JCM9785. The deduced amino acid sequence of the CE gene from R. marinus JCM9785 (RmCE) was 94.2% identical to that from R. marinus DSM4252. The N-terminal amino acid sequence and tryptic peptide masses of the native enzyme matched those of RmCE. The recombinant RmCE was most active at 80 °C at pH 6.3, and stable in a range of pH 3.2-10.8 and below 80 °C. In contrast to other CEs, RmCE demonstrated higher preference for lactose over cellobiose.
|
| Volume |
75(11)
|
| Pages |
2162-8
|
| Published |
2011-1-1
|
| DOI |
10.1271/bbb.110456
|
| PII |
JST.JSTAGE/bbb/110456
|
| PMID |
22056431
|
| MeSH |
Amino Acid Sequence
Cellobiose / chemistry*
Cellobiose / genetics
Cellobiose / isolation & purification
Cloning, Molecular
Disaccharides / metabolism
Enzyme Stability
Hydrogen-Ion Concentration
Molecular Sequence Data
Racemases and Epimerases / chemistry*
Racemases and Epimerases / genetics
Racemases and Epimerases / isolation & purification
Recombinant Proteins / chemistry
Rhodothermus / enzymology*
Substrate Specificity
Temperature
|
| IF |
1.516
|
| Times Cited |
28
|
|
WOS Category
|
FOOD SCIENCE & TECHNOLOGY
BIOTECHNOLOGY & APPLIED MICROBIOLOGY
CHEMISTRY, APPLIED
BIOCHEMISTRY & MOLECULAR BIOLOGY
|
| Resource |
| General Microbes |
JCM 9785 |
