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Pregled bibliografske jedinice broj: 1144996

Activity and stability of lyophilized halohydrin dehalogenase


Marin, Petra; Majerić Elenkov, Maja
Activity and stability of lyophilized halohydrin dehalogenase // 6th International Conference on Biocatalysis in Non-Conventional Media (BNCM 2021)
Virtual conference, 2021. (poster, recenziran, sažetak, znanstveni)


CROSBI ID: 1144996 Za ispravke kontaktirajte CROSBI podršku putem web obrasca

Naslov
Activity and stability of lyophilized halohydrin dehalogenase

Autori
Marin, Petra ; Majerić Elenkov, Maja

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Skup
6th International Conference on Biocatalysis in Non-Conventional Media (BNCM 2021)

Mjesto i datum
Virtual conference, 06.-08. 05. 2021

Vrsta sudjelovanja
Poster

Vrsta recenzije
Recenziran

Ključne riječi
halohydrin dehalogenase ; protein stability ; lyophilization

Sažetak
Stability of enzymes has a significant impact on their use in an alternative reaction media. Presence of organic solvents or exposure to high temperatures leads to denaturation of enzymes since they have evolved to work in the cellular environment. Lyophilization is as an attractive solution for long-term storage of enzymes at ambient temperature. Also, it can be used as a method of enzyme stabilization for their application in non-aqueous media. Halohydrin dehalogeneses are enzymes that catalyse the formation and conversion of epoxides. Reactions are catalyzed in regioselective and enantioselective manner, making the enzymes attractive for biocatalysis. Enzyme from Agrobacterium radiobacter AD1 (HheC) is usually expressed in E.coli, isolated in TEMG buffer (50 mM Tris-SO4, 2 mM EDTA, 10 % glycerol and 1 mM mercaptoethanol), and usually is stored as a cell-free extract at -70 °C for at least three months without significant loss of activity. In this work, the stability of HheC is first evaluated in different buffers (TEMG, TEM and Tris-SO4) at different temperatures. With the aim of obtaining the optimal lyophilized formulation, different additives were tested for HheC stabilization. Lyophilized HheC was incubated at 50 °C to intensify the differences induced by additives. Enzyme activity is determined by following the absorbance at 310 nm.

Izvorni jezik
Engleski

Znanstvena područja
Kemija



POVEZANOST RADA


Projekti:
HRZZ-IP-2018-01-4493 - Enzimska sinteza fluoriranih kiralnih građevnih blokova (EnzyFluor) (Majerić-Elenkov, Maja, HRZZ - 2018-01) ( POIROT)

Ustanove:
Institut "Ruđer Bošković", Zagreb

Profili:

Avatar Url Maja Majerić-Elenkov (autor)


Citiraj ovu publikaciju:

Marin, Petra; Majerić Elenkov, Maja
Activity and stability of lyophilized halohydrin dehalogenase // 6th International Conference on Biocatalysis in Non-Conventional Media (BNCM 2021)
Virtual conference, 2021. (poster, recenziran, sažetak, znanstveni)
Marin, P. & Majerić Elenkov, M. (2021) Activity and stability of lyophilized halohydrin dehalogenase. U: 6th International Conference on Biocatalysis in Non-Conventional Media (BNCM 2021).
@article{article, year = {2021}, keywords = {halohydrin dehalogenase, protein stability, lyophilization}, title = {Activity and stability of lyophilized halohydrin dehalogenase}, keyword = {halohydrin dehalogenase, protein stability, lyophilization}, publisherplace = {Virtual conference} }
@article{article, year = {2021}, keywords = {halohydrin dehalogenase, protein stability, lyophilization}, title = {Activity and stability of lyophilized halohydrin dehalogenase}, keyword = {halohydrin dehalogenase, protein stability, lyophilization}, publisherplace = {Virtual conference} }




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