Naslov
Validation of kinetic model of halohydrin dehalogenase-catalysed synthesis of (R)- epichlorohydrin

Autori
Ćevid, Ivana ; Milčić, Nevena ; Majerić Elenkov, Maja ; Findrik Blažević, Zvjezdana

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

Izvornik
27th Croatian Meeting of Chemists and Chemical Engineers and 5th Symposium Vladimir Prelog : Book of Abstracts / Marković, Dean ; Meštrović, Ernest ; Namjesnik, Danijel ; Tomašić, Vesna - Zagreb : Hrvatsko kemijsko društvo, 2021, 302-302

Skup
27. hrvatski skup kemičara i kemijskih inženjera (27HSKIKI) ; 5. simpozij Vladimir Prelog

Mjesto i datum
Veli Lošinj, Hrvatska, 05.10.2021. - 08.10.2021

Vrsta sudjelovanja
Poster

Vrsta recenzije
Recenziran

Ključne riječi
validation ; halohydrin dehalogenase ; (R)-epichlorohydrin

Sažetak
Epichlorohydrin (ECH) is a valuable product that is commonly used as an intermediate in the preparation of synthetic rubbers, as a starting material in the production of insecticides, pharmaceuticals, etc. [1] This prominent product can be obtained through biocatalysis. Halohydrin dehalogenases (HHDHs) are adaptable and important biocatalysts that are mostly used for the industrial synthesis of enantiopure ECH. [2] The reasons why the biocatalytic approach takes precedence over the traditional one are high enantioselectivity, low production cost, extensive enzyme sources and environmentally friendly conditions of this synthesis. [3] The operational stability of an enzyme generally relates to the retention of activity when an enzyme is in use. On an industrial level, the long-term operational stability of biocatalysts is of crucial importance for deciding whether a process can be viable as opposed to the traditional approach. [4] Operational stability is necessary to determine at which process conditions enzyme can work properly. In this work the kinetic model of HheB2-T120A- catalysed synthesis of (R)-ECH from 1, 3-dichloro- 2-propanol was developed. Model validation was performed in batch reactor experiments. It was found that a substrate (1, 3-dichloro-2-propanol) deactivates the enzyme and the rate of deactivation is dependent upon its concentration. ACKNOWLEDGEMENTS: This work was supported by CATPHARMA (KK.01.1.1.04.0013). REFERENCES [1] Y. Bespalko et al., International Journal of Chemical Kinetics 2021, 53(3), 356-368. [2] Z. Findrik Blažević et al., Advanced Synthesis and Catalysis 2021, 363(2), 388-410. [3] X. J. Zhang et al., Bioresource Technology 2018, 263, 483-490. [4] G. A. Drago, T. D. Gibson, Enzyme Stability and Stabilisation: Apllications and Case Studies, Engineering and Manufacturing for Biotechnology 2002, 4, 361-376.

Izvorni jezik
Engleski

Znanstvena područja
Kemijsko inženjerstvo, Biotehnologija

POVEZANOST RADA