Immobilization of lipase on epoxy-activated Purolite((R)) A109 and its post-immobilization stabilization
Само за регистроване кориснике
2014
Аутори
Mihailović, MladenStojanović, Marija
Banjanac, Katarina
Carević, Milica
Prlainović, Nevena
Milosavić, Nenad
Bezbradica, Dejan
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
In this study, Purolite (R) A109, polystyrenic macroporous resin, was used as immobilization support due to its good mechanical properties and high particle diameter (400 mu m), which enables efficient application in enzyme reactors due to lower pressure drops. The surface of support had been modified with epichlorhydrine and was tested in lipase immobilization. Optimized procedure for support modification proved to be more efficient than conventional procedure for hydroxy groups (at 22 degrees C for 18 h), since duration of procedure was shortened to 40 min by performing modification at 52 degrees C resulting with almost doubled concentration of epoxy groups (563 mu mol g(-1)). Lipase immobilized on epoxy-modified support showed significantly improved thermal stability comparing to both, free form and commercial immobilized preparation (Novozym (R) 435). The highest activity (47.5 IU g(-1)) and thermal stability (2.5 times higher half-life than at low ionic strength) were obtained wit...h lipase immobilized in high ionic strength. Thermal stability of immobilized lipase was further improved by blocking unreacted epoxy groups on supports surface with amino acids. The most efficient was treatment with phenylalanine, since in such a way blocked immobilized enzyme retained 65% of initial activity after 8 h incubation at 65 degrees C, while non-blocked derivative retained 12%.
Кључне речи:
Lipase / Purolite((R)) A109 / Candida antarctica / Immobilization / Amino acidsИзвор:
Process Biochemistry, 2014, 49, 4, 637-646Издавач:
- Elsevier Sci Ltd, Oxford
Финансирање / пројекти:
- Развој нових инкапсулационих и ензимских технологија за производњу биокатализатора и биолошки активних компонената хране у циљу повећања њене конкурентности, квалитета и безбедности (RS-MESTD-Integrated and Interdisciplinary Research (IIR or III)-46010)
- Проучавање синтезе, структуре и активности органских једињења природног и синтетског порекла (RS-MESTD-Basic Research (BR or ON)-172013)
DOI: 10.1016/j.procbio.2014.01.013
ISSN: 1359-5113
WoS: 000335281800014
Scopus: 2-s2.0-84897913807
Колекције
Институција/група
Tehnološko-metalurški fakultetTY - JOUR AU - Mihailović, Mladen AU - Stojanović, Marija AU - Banjanac, Katarina AU - Carević, Milica AU - Prlainović, Nevena AU - Milosavić, Nenad AU - Bezbradica, Dejan PY - 2014 UR - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/2853 AB - In this study, Purolite (R) A109, polystyrenic macroporous resin, was used as immobilization support due to its good mechanical properties and high particle diameter (400 mu m), which enables efficient application in enzyme reactors due to lower pressure drops. The surface of support had been modified with epichlorhydrine and was tested in lipase immobilization. Optimized procedure for support modification proved to be more efficient than conventional procedure for hydroxy groups (at 22 degrees C for 18 h), since duration of procedure was shortened to 40 min by performing modification at 52 degrees C resulting with almost doubled concentration of epoxy groups (563 mu mol g(-1)). Lipase immobilized on epoxy-modified support showed significantly improved thermal stability comparing to both, free form and commercial immobilized preparation (Novozym (R) 435). The highest activity (47.5 IU g(-1)) and thermal stability (2.5 times higher half-life than at low ionic strength) were obtained with lipase immobilized in high ionic strength. Thermal stability of immobilized lipase was further improved by blocking unreacted epoxy groups on supports surface with amino acids. The most efficient was treatment with phenylalanine, since in such a way blocked immobilized enzyme retained 65% of initial activity after 8 h incubation at 65 degrees C, while non-blocked derivative retained 12%. PB - Elsevier Sci Ltd, Oxford T2 - Process Biochemistry T1 - Immobilization of lipase on epoxy-activated Purolite((R)) A109 and its post-immobilization stabilization EP - 646 IS - 4 SP - 637 VL - 49 DO - 10.1016/j.procbio.2014.01.013 ER -
@article{ author = "Mihailović, Mladen and Stojanović, Marija and Banjanac, Katarina and Carević, Milica and Prlainović, Nevena and Milosavić, Nenad and Bezbradica, Dejan", year = "2014", abstract = "In this study, Purolite (R) A109, polystyrenic macroporous resin, was used as immobilization support due to its good mechanical properties and high particle diameter (400 mu m), which enables efficient application in enzyme reactors due to lower pressure drops. The surface of support had been modified with epichlorhydrine and was tested in lipase immobilization. Optimized procedure for support modification proved to be more efficient than conventional procedure for hydroxy groups (at 22 degrees C for 18 h), since duration of procedure was shortened to 40 min by performing modification at 52 degrees C resulting with almost doubled concentration of epoxy groups (563 mu mol g(-1)). Lipase immobilized on epoxy-modified support showed significantly improved thermal stability comparing to both, free form and commercial immobilized preparation (Novozym (R) 435). The highest activity (47.5 IU g(-1)) and thermal stability (2.5 times higher half-life than at low ionic strength) were obtained with lipase immobilized in high ionic strength. Thermal stability of immobilized lipase was further improved by blocking unreacted epoxy groups on supports surface with amino acids. The most efficient was treatment with phenylalanine, since in such a way blocked immobilized enzyme retained 65% of initial activity after 8 h incubation at 65 degrees C, while non-blocked derivative retained 12%.", publisher = "Elsevier Sci Ltd, Oxford", journal = "Process Biochemistry", title = "Immobilization of lipase on epoxy-activated Purolite((R)) A109 and its post-immobilization stabilization", pages = "646-637", number = "4", volume = "49", doi = "10.1016/j.procbio.2014.01.013" }
Mihailović, M., Stojanović, M., Banjanac, K., Carević, M., Prlainović, N., Milosavić, N.,& Bezbradica, D.. (2014). Immobilization of lipase on epoxy-activated Purolite((R)) A109 and its post-immobilization stabilization. in Process Biochemistry Elsevier Sci Ltd, Oxford., 49(4), 637-646. https://doi.org/10.1016/j.procbio.2014.01.013
Mihailović M, Stojanović M, Banjanac K, Carević M, Prlainović N, Milosavić N, Bezbradica D. Immobilization of lipase on epoxy-activated Purolite((R)) A109 and its post-immobilization stabilization. in Process Biochemistry. 2014;49(4):637-646. doi:10.1016/j.procbio.2014.01.013 .
Mihailović, Mladen, Stojanović, Marija, Banjanac, Katarina, Carević, Milica, Prlainović, Nevena, Milosavić, Nenad, Bezbradica, Dejan, "Immobilization of lipase on epoxy-activated Purolite((R)) A109 and its post-immobilization stabilization" in Process Biochemistry, 49, no. 4 (2014):637-646, https://doi.org/10.1016/j.procbio.2014.01.013 . .