Thermostable Esterase estUT1 from Ureibacillus thermosphaericus: Effect of TrxA Tag on the Enzyme Properties
Full article
| Общее |
Language:
Английский,
Genre:
Full article,
Status:
Published,
Source type:
Translated
|
| Journal |
Catalysis in Industry
ISSN: 2070-0504
, E-ISSN: 2070-0555
|
| Output data |
Year: 2020,
Volume: 12,
Number: 2,
Pages: 148-154
Pages count
: 7
DOI:
10.1134/S2070050420020099
|
| Tags |
esterase, Ureibacillus thermosphaericus, TrxA, thermostability |
| Authors |
Sorokina K.N.
1
,
Samoylova Yu.V.
1
,
Parmon V.N.
1
|
| Affiliations |
| 1 |
Boreskov Institute of Catalysis, Siberian Branch, Russian Academy of Sciences, Novosibirsk, 630090 Russia
|
|
Funding (1)
|
1
|
Federal Agency for Scientific Organizations
|
0303-2016-0012 (V.47.1.4.)
|
The thermostable esterase from the bacterium Ureibacillus thermosphaericus was expressed with Trx tag from plasmid pET32b-estUT1 under T7 promoter in E. coli BL21(DE3). The specific activity and relative thermal stability of the tagged enzyme increased from 45.2 to 65.8% (1 h at 70°С). The additional TrxA tag does not affect the pH optimum of enzyme activity and substrate specificity. At the same time, the absence of the TrxA tag resulted in a significant increase in the stability of estUT1 in during incubation with various chemicals, including ethanol and methanol. The maximum catalytic efficiency (kcat/KM) for esterase was observed in the absence of the TrxA tag and was 280.0 s−1 mM−1. Thereby fusion with TrxA tag promotes the enzyme secretion in the dissolved form, but reduces its thermal stability.