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Thermostable Esterase estUT1 from Ureibacillus thermosphaericus: Effect of TrxA Tag on the Enzyme Properties Full article

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.)

Abstract: 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.
Cite: Sorokina K.N. , Samoylova Y.V. , Parmon V.N.
Thermostable Esterase estUT1 from Ureibacillus thermosphaericus: Effect of TrxA Tag on the Enzyme Properties
Catalysis in Industry. 2020. V.12. N2. P.148-154. DOI: 10.1134/S2070050420020099 WOS Scopus РИНЦ OpenAlex
Original: Сорокина К.Н. , Самойлова Ю.В. , Пармон В.Н.
Термостабильная эстераза estUT1 бактерии Ureibacillus thermosphaericus: влияние дополнительного процессируемого домена TrxA на свойства фермента
Катализ в промышленности. 2019. Т.19. №5. С.399-407. DOI: 10.18412/1816-0387-2019-5-399-407RSCI РИНЦ ANCAN OpenAlex
Dates:
Submitted: May 6, 2019
Accepted: Jun 24, 2019
Published print: Apr 1, 2020
Published online: Jun 25, 2020
Identifiers:
Web of science: WOS:000543047100009
Scopus: 2-s2.0-85087060956
Elibrary: 43303009
OpenAlex: W3037878167
Citing:
DB Citing
Scopus 3
Web of science 3
Elibrary 3
OpenAlex 3
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