Characterization of a novel salt-, xylose- and alkali-tolerant GH43 bifunctional ß-xylosidase/α-l-arabinofuranosidase from the gut bacterial genome.
J Biosci Bioeng
; 128(4): 429-437, 2019 Oct.
Article
in En
| MEDLINE
| ID: mdl-31109875
ABSTRACT
A GH43 bifunctional ß-xylosidase encoding gene (XylRBM26) was cloned from Massilia sp. RBM26 and successfully expressed in Escherichia coli. Recombinant XylRBM26 exhibited ß-xylosidase and α-l-arabinofuranosidase activities. When 4-nitrophenyl-ß-d-xylopyranoside was used as a substrate, the enzyme reached optimal activity at pH 6.5 and 50°C and remained stable at pH 5.0-10.0. Purified XylRBM26 presented good salt tolerance and retained 96.6% activity in 3.5 M NaCl and 77.9% initial activity even in 4.0 M NaCl. In addition, it exhibited high tolerance to xylose with Ki value of 500 mM. This study was the first to identify and characterize NaCl-tolerant ß-xylosidase/α-l-arabinofuranosidase from the gut microbiota. The enzyme's salt, xylose, and alkali stability and resistance to various chemicals make it a potential biocatalyst for the saccharification of lignocellulose, the food industry, and industrial processes conducted in sea water.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Xylosidases
/
Genome, Bacterial
/
Gastrointestinal Microbiome
/
Glycoside Hydrolases
Language:
En
Journal:
J Biosci Bioeng
Journal subject:
ENGENHARIA BIOMEDICA
/
MICROBIOLOGIA
Year:
2019
Document type:
Article