Flavonoid esters synthesis using novel biocatalytic systems - CAL B immobilized onto LifeTech (TM) ECR supports
Само за регистроване кориснике
2020
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
In order to enhance productivity and cost-effectiveness of current lipase-catalyzed processes of flavonoid esters synthesis, different LifeTech (TM) ECR carriers varying in functional groups, polarity and porosity were hereby screened as immobilization supports for free lipase B from Candida antarctica. The most prospective ones were examined in esterification of three flavonoid glycoside representatives - phloridzin, naringin and esculin using different acyl donors. Highly active preparations were obtained by using hydrophobic C18 (ECR 8806M), epoxy/butyl (ECR 8285F) and primary amino (ECR 8409F) functionalized resins. Interestingly, lipase immobilized via hydrophobic interactions and covalent bonds exhibited high catalytic activity in esterification reactions using oleic acid as well as natural oils as acyl donors, yielding more than 70 % and 50 % conversion degree, respectively. On the other hand, lipase immobilized onto amino-support by electrostatic interactions, which demonstrate...d the highest hydrolytic activity, showed poor efficiency in ester syntheses. Operational stability study proved exceptionally high potential of lipases immobilized on epoxy-support or hydrophobic support for reproducible and cost-effective industrial application, since 90 % of initial activity was preserved after six consecutive reaction cycles of oleyl ester synthesis, while within following nine reuses, only moderate activity loss occurred. Moreover, besides very good esterifying activity, lipase immobilized via hydrophobic interactions showed outstanding operational stability during ten reuses in reaction of phloridzin transesterification with coconut oil.
Кључне речи:
Candida antarctica lipase B / Immobilization / LifeTech (TM) ECR carriers / Flavonoid / EsterificationИзвор:
Biochemical Engineering Journal, 2020, 163, 107748-Издавач:
- Elsevier B.V.
Финансирање / пројекти:
- Министарство науке, технолошког развоја и иновација Републике Србије, институционално финансирање - 200287 (Иновациони центар Технолошко-металуршког факултета у Београду доо) (RS-200287)
- Министарство науке, технолошког развоја и иновација Републике Србије, институционално финансирање - 200135 (Универзитет у Београду, Технолошко-металуршки факултет) (RS-200135)
DOI: 10.1016/j.bej.2020.107748
ISSN: 1369-703X
WoS: 000577158600011
Scopus: 2-s2.0-85089149493
Колекције
Институција/група
Tehnološko-metalurški fakultetTY - JOUR AU - Milivojević, Ana AU - Ćorović, Marija AU - Simović, Milica AU - Banjanac, Katarina AU - Bezbradica, Dejan PY - 2020 UR - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/4370 AB - In order to enhance productivity and cost-effectiveness of current lipase-catalyzed processes of flavonoid esters synthesis, different LifeTech (TM) ECR carriers varying in functional groups, polarity and porosity were hereby screened as immobilization supports for free lipase B from Candida antarctica. The most prospective ones were examined in esterification of three flavonoid glycoside representatives - phloridzin, naringin and esculin using different acyl donors. Highly active preparations were obtained by using hydrophobic C18 (ECR 8806M), epoxy/butyl (ECR 8285F) and primary amino (ECR 8409F) functionalized resins. Interestingly, lipase immobilized via hydrophobic interactions and covalent bonds exhibited high catalytic activity in esterification reactions using oleic acid as well as natural oils as acyl donors, yielding more than 70 % and 50 % conversion degree, respectively. On the other hand, lipase immobilized onto amino-support by electrostatic interactions, which demonstrated the highest hydrolytic activity, showed poor efficiency in ester syntheses. Operational stability study proved exceptionally high potential of lipases immobilized on epoxy-support or hydrophobic support for reproducible and cost-effective industrial application, since 90 % of initial activity was preserved after six consecutive reaction cycles of oleyl ester synthesis, while within following nine reuses, only moderate activity loss occurred. Moreover, besides very good esterifying activity, lipase immobilized via hydrophobic interactions showed outstanding operational stability during ten reuses in reaction of phloridzin transesterification with coconut oil. PB - Elsevier B.V. T2 - Biochemical Engineering Journal T1 - Flavonoid esters synthesis using novel biocatalytic systems - CAL B immobilized onto LifeTech (TM) ECR supports SP - 107748 VL - 163 DO - 10.1016/j.bej.2020.107748 ER -
@article{ author = "Milivojević, Ana and Ćorović, Marija and Simović, Milica and Banjanac, Katarina and Bezbradica, Dejan", year = "2020", abstract = "In order to enhance productivity and cost-effectiveness of current lipase-catalyzed processes of flavonoid esters synthesis, different LifeTech (TM) ECR carriers varying in functional groups, polarity and porosity were hereby screened as immobilization supports for free lipase B from Candida antarctica. The most prospective ones were examined in esterification of three flavonoid glycoside representatives - phloridzin, naringin and esculin using different acyl donors. Highly active preparations were obtained by using hydrophobic C18 (ECR 8806M), epoxy/butyl (ECR 8285F) and primary amino (ECR 8409F) functionalized resins. Interestingly, lipase immobilized via hydrophobic interactions and covalent bonds exhibited high catalytic activity in esterification reactions using oleic acid as well as natural oils as acyl donors, yielding more than 70 % and 50 % conversion degree, respectively. On the other hand, lipase immobilized onto amino-support by electrostatic interactions, which demonstrated the highest hydrolytic activity, showed poor efficiency in ester syntheses. Operational stability study proved exceptionally high potential of lipases immobilized on epoxy-support or hydrophobic support for reproducible and cost-effective industrial application, since 90 % of initial activity was preserved after six consecutive reaction cycles of oleyl ester synthesis, while within following nine reuses, only moderate activity loss occurred. Moreover, besides very good esterifying activity, lipase immobilized via hydrophobic interactions showed outstanding operational stability during ten reuses in reaction of phloridzin transesterification with coconut oil.", publisher = "Elsevier B.V.", journal = "Biochemical Engineering Journal", title = "Flavonoid esters synthesis using novel biocatalytic systems - CAL B immobilized onto LifeTech (TM) ECR supports", pages = "107748", volume = "163", doi = "10.1016/j.bej.2020.107748" }
Milivojević, A., Ćorović, M., Simović, M., Banjanac, K.,& Bezbradica, D.. (2020). Flavonoid esters synthesis using novel biocatalytic systems - CAL B immobilized onto LifeTech (TM) ECR supports. in Biochemical Engineering Journal Elsevier B.V.., 163, 107748. https://doi.org/10.1016/j.bej.2020.107748
Milivojević A, Ćorović M, Simović M, Banjanac K, Bezbradica D. Flavonoid esters synthesis using novel biocatalytic systems - CAL B immobilized onto LifeTech (TM) ECR supports. in Biochemical Engineering Journal. 2020;163:107748. doi:10.1016/j.bej.2020.107748 .
Milivojević, Ana, Ćorović, Marija, Simović, Milica, Banjanac, Katarina, Bezbradica, Dejan, "Flavonoid esters synthesis using novel biocatalytic systems - CAL B immobilized onto LifeTech (TM) ECR supports" in Biochemical Engineering Journal, 163 (2020):107748, https://doi.org/10.1016/j.bej.2020.107748 . .