Studies on the specificity of Candida rugosa lipase catalyzed esterification reactions in organic media
Ispitivanje specifičnosti lipaze iz Candida rugosa u reakciji esterifikacije u organskom rastvaraču
Аутори
Bezbradica, DejanKaralazić, Ivana
Ognjanović, Nevena
Mijin, Dušan
Šiler-Marinković, Slavica
Knežević, Zorica
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
In this study, the feasibility of the synthesis of various flavor esters catalyzed by a commercial lipase from Candida rugosa was investigated and the process parameters were optimized. Lipase from C. rugosa successfully catalyzed the synthesis of 19 esters. The highest yields, of more than 90 % after 20 h, were observed in the synthesis of short-chain esters, pentyl propanoate, isopentyl butanoate, and butyl butanoate. Increasing the number of carbon atoms of both substrates above 8 caused a significant decrease of the initial reaction rates and the final yields. The enzyme showed surprisingly low affinity towards pentanoic acid and hexanoic acid, compared with the higher homologues, octanoic acid and decanoic acid. In addition to the number of carbon atoms, the structure of the substrates had a significant influence on the enzyme activity. Namely, the activity of the enzyme towards isopropanol was significantly lower compared with n-propanol. Additionally, cis-9-octadecenoic acid was... a better substrate than octadecanoic acid, its saturated analogue.
Cilj ovog rada je bio ispitivanje mogućnosti sinteze različitih estara pomoću lipaze iz Candida rugosa kao i optimizacija procesnih parametara. Pokazano je da se data lipaza može koristiti kao efikasan biokatalizator za dobijanje devetnaest različitih estara. Najveći prinosi, veći od 90%, dobijeni su u slučaju sinteze nižih estara kao što su pentil-propanoat, 2-metilbutil-butanoat i butil-butanoat. Početna brzina sinteze estara i krajnji prinosi bili su znatno niži sa supstratima koji sadrže više od 8 ugljenikovih atoma. Enzim je pokazao iznenađujuće mali afinitet prema pentanskoj i heksanskoj kiselini, u poređenju sa višim homolozima, oktanskom i dekanskom.Pored broja ugljenikovih atoma, na aktivnost enzima značajno je uticalo prisustvo dvostruke veze u molekulu supstrata i razgranatost supstrata. Naime, lipaza iz C. rugosa ispoljila je mnogo manju aktivnost u reakciji sa izopropanolom nego sa propanolom, dok je pokazala mnogo veći afinitet prema 9-cis-oktadecenskoj kiselini u odnosu ...na njen zasićeni analog, oktadekansku kiselinu.
Кључне речи:
lipase / Candida rugosa / esterification / specificityИзвор:
Journal of the Serbian Chemical Society, 2006, 71, 1, 31-41Издавач:
- Serbian Chemical Society, Belgrade
Институција/група
Tehnološko-metalurški fakultetTY - JOUR AU - Bezbradica, Dejan AU - Karalazić, Ivana AU - Ognjanović, Nevena AU - Mijin, Dušan AU - Šiler-Marinković, Slavica AU - Knežević, Zorica PY - 2006 UR - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/1002 AB - In this study, the feasibility of the synthesis of various flavor esters catalyzed by a commercial lipase from Candida rugosa was investigated and the process parameters were optimized. Lipase from C. rugosa successfully catalyzed the synthesis of 19 esters. The highest yields, of more than 90 % after 20 h, were observed in the synthesis of short-chain esters, pentyl propanoate, isopentyl butanoate, and butyl butanoate. Increasing the number of carbon atoms of both substrates above 8 caused a significant decrease of the initial reaction rates and the final yields. The enzyme showed surprisingly low affinity towards pentanoic acid and hexanoic acid, compared with the higher homologues, octanoic acid and decanoic acid. In addition to the number of carbon atoms, the structure of the substrates had a significant influence on the enzyme activity. Namely, the activity of the enzyme towards isopropanol was significantly lower compared with n-propanol. Additionally, cis-9-octadecenoic acid was a better substrate than octadecanoic acid, its saturated analogue. AB - Cilj ovog rada je bio ispitivanje mogućnosti sinteze različitih estara pomoću lipaze iz Candida rugosa kao i optimizacija procesnih parametara. Pokazano je da se data lipaza može koristiti kao efikasan biokatalizator za dobijanje devetnaest različitih estara. Najveći prinosi, veći od 90%, dobijeni su u slučaju sinteze nižih estara kao što su pentil-propanoat, 2-metilbutil-butanoat i butil-butanoat. Početna brzina sinteze estara i krajnji prinosi bili su znatno niži sa supstratima koji sadrže više od 8 ugljenikovih atoma. Enzim je pokazao iznenađujuće mali afinitet prema pentanskoj i heksanskoj kiselini, u poređenju sa višim homolozima, oktanskom i dekanskom.Pored broja ugljenikovih atoma, na aktivnost enzima značajno je uticalo prisustvo dvostruke veze u molekulu supstrata i razgranatost supstrata. Naime, lipaza iz C. rugosa ispoljila je mnogo manju aktivnost u reakciji sa izopropanolom nego sa propanolom, dok je pokazala mnogo veći afinitet prema 9-cis-oktadecenskoj kiselini u odnosu na njen zasićeni analog, oktadekansku kiselinu. PB - Serbian Chemical Society, Belgrade T2 - Journal of the Serbian Chemical Society T1 - Studies on the specificity of Candida rugosa lipase catalyzed esterification reactions in organic media T1 - Ispitivanje specifičnosti lipaze iz Candida rugosa u reakciji esterifikacije u organskom rastvaraču EP - 41 IS - 1 SP - 31 VL - 71 UR - https://hdl.handle.net/21.15107/rcub_technorep_1002 ER -
@article{ author = "Bezbradica, Dejan and Karalazić, Ivana and Ognjanović, Nevena and Mijin, Dušan and Šiler-Marinković, Slavica and Knežević, Zorica", year = "2006", abstract = "In this study, the feasibility of the synthesis of various flavor esters catalyzed by a commercial lipase from Candida rugosa was investigated and the process parameters were optimized. Lipase from C. rugosa successfully catalyzed the synthesis of 19 esters. The highest yields, of more than 90 % after 20 h, were observed in the synthesis of short-chain esters, pentyl propanoate, isopentyl butanoate, and butyl butanoate. Increasing the number of carbon atoms of both substrates above 8 caused a significant decrease of the initial reaction rates and the final yields. The enzyme showed surprisingly low affinity towards pentanoic acid and hexanoic acid, compared with the higher homologues, octanoic acid and decanoic acid. In addition to the number of carbon atoms, the structure of the substrates had a significant influence on the enzyme activity. Namely, the activity of the enzyme towards isopropanol was significantly lower compared with n-propanol. Additionally, cis-9-octadecenoic acid was a better substrate than octadecanoic acid, its saturated analogue., Cilj ovog rada je bio ispitivanje mogućnosti sinteze različitih estara pomoću lipaze iz Candida rugosa kao i optimizacija procesnih parametara. Pokazano je da se data lipaza može koristiti kao efikasan biokatalizator za dobijanje devetnaest različitih estara. Najveći prinosi, veći od 90%, dobijeni su u slučaju sinteze nižih estara kao što su pentil-propanoat, 2-metilbutil-butanoat i butil-butanoat. Početna brzina sinteze estara i krajnji prinosi bili su znatno niži sa supstratima koji sadrže više od 8 ugljenikovih atoma. Enzim je pokazao iznenađujuće mali afinitet prema pentanskoj i heksanskoj kiselini, u poređenju sa višim homolozima, oktanskom i dekanskom.Pored broja ugljenikovih atoma, na aktivnost enzima značajno je uticalo prisustvo dvostruke veze u molekulu supstrata i razgranatost supstrata. Naime, lipaza iz C. rugosa ispoljila je mnogo manju aktivnost u reakciji sa izopropanolom nego sa propanolom, dok je pokazala mnogo veći afinitet prema 9-cis-oktadecenskoj kiselini u odnosu na njen zasićeni analog, oktadekansku kiselinu.", publisher = "Serbian Chemical Society, Belgrade", journal = "Journal of the Serbian Chemical Society", title = "Studies on the specificity of Candida rugosa lipase catalyzed esterification reactions in organic media, Ispitivanje specifičnosti lipaze iz Candida rugosa u reakciji esterifikacije u organskom rastvaraču", pages = "41-31", number = "1", volume = "71", url = "https://hdl.handle.net/21.15107/rcub_technorep_1002" }
Bezbradica, D., Karalazić, I., Ognjanović, N., Mijin, D., Šiler-Marinković, S.,& Knežević, Z.. (2006). Studies on the specificity of Candida rugosa lipase catalyzed esterification reactions in organic media. in Journal of the Serbian Chemical Society Serbian Chemical Society, Belgrade., 71(1), 31-41. https://hdl.handle.net/21.15107/rcub_technorep_1002
Bezbradica D, Karalazić I, Ognjanović N, Mijin D, Šiler-Marinković S, Knežević Z. Studies on the specificity of Candida rugosa lipase catalyzed esterification reactions in organic media. in Journal of the Serbian Chemical Society. 2006;71(1):31-41. https://hdl.handle.net/21.15107/rcub_technorep_1002 .
Bezbradica, Dejan, Karalazić, Ivana, Ognjanović, Nevena, Mijin, Dušan, Šiler-Marinković, Slavica, Knežević, Zorica, "Studies on the specificity of Candida rugosa lipase catalyzed esterification reactions in organic media" in Journal of the Serbian Chemical Society, 71, no. 1 (2006):31-41, https://hdl.handle.net/21.15107/rcub_technorep_1002 .