Cyanuric chloride functionalized silica nanoparticles for covalent immobilization of lipase
Само за регистроване кориснике
2016
Аутори
Banjanac, KatarinaMihailović, Mladen
Prlainović, Nevena
Stojanović, Marija
Simović, Milica
Marinković, Aleksandar
Bezbradica, Dejan
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
BACKGROUNDIn this work, fumed nano-silica (FNS) was chemically modified to amino (AFNS) and subsequently to cyanuric chloride (CCAFNS) modified silica and tested for the immobilization of lipase from Candida rugosa (CRL). The effects of the initial enzyme concentration, immobilization time and buffer ionic strength on immobilization were investigated in order to optimize utilization of the support and determine the mechanism of immobilization. The most active preparations were used to examine thermal and operational stability. RESULTSThe amount of immobilized enzyme increased with increasing enzyme concentration, achieving loadings of 121.3, 104.8 and 61.2mg per g of FNS, CCAFNS and AFNS, respectively. Lipase immobilized on CCAFNS carrier in 0.1molL(-1) buffer expressed the highest lipolytic activity (1320 IU g(-1) support), while more stable preparations were obtained in 1molL(-1) buffer. CONCLUSIONSuccessful modification of silica was confirmed with Fourier transform infrared spectro...scopy and thermogravimetric analysis. Activity results showed that, depending on the support, immobilization was governed by different interactions. On FNS and AFNS immobilization was exclusively by adsorption, while on CCAFNS after the initial adsorption lipase molecules reoriented and amino groups of the enzyme formed a covalent bond with the chlorine atom of the modified carrier. Improved thermal and operational stability of lipase immobilized on CCAFNS in 1molL(-1) buffer led to the conclusion that electrostatic interactions have a great role in the immobilization.
Кључне речи:
silica nanoparticles / modification / APTMS / cyanuric chloride / lipase / enzyme immobilizationИзвор:
Journal of Chemical Technology and Biotechnology, 2016, 91, 2, 439-448Издавач:
- Wiley-Blackwell, Hoboken
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)
- Синтеза, развој технологија добијања и примена наноструктурних мултифункционалних материјала дефинисаних својстава (RS-MESTD-Integrated and Interdisciplinary Research (IIR or III)-45019)
DOI: 10.1002/jctb.4595
ISSN: 0268-2575
WoS: 000367951200019
Scopus: 2-s2.0-84953839970
Колекције
Институција/група
Tehnološko-metalurški fakultetTY - JOUR AU - Banjanac, Katarina AU - Mihailović, Mladen AU - Prlainović, Nevena AU - Stojanović, Marija AU - Simović, Milica AU - Marinković, Aleksandar AU - Bezbradica, Dejan PY - 2016 UR - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/3372 AB - BACKGROUNDIn this work, fumed nano-silica (FNS) was chemically modified to amino (AFNS) and subsequently to cyanuric chloride (CCAFNS) modified silica and tested for the immobilization of lipase from Candida rugosa (CRL). The effects of the initial enzyme concentration, immobilization time and buffer ionic strength on immobilization were investigated in order to optimize utilization of the support and determine the mechanism of immobilization. The most active preparations were used to examine thermal and operational stability. RESULTSThe amount of immobilized enzyme increased with increasing enzyme concentration, achieving loadings of 121.3, 104.8 and 61.2mg per g of FNS, CCAFNS and AFNS, respectively. Lipase immobilized on CCAFNS carrier in 0.1molL(-1) buffer expressed the highest lipolytic activity (1320 IU g(-1) support), while more stable preparations were obtained in 1molL(-1) buffer. CONCLUSIONSuccessful modification of silica was confirmed with Fourier transform infrared spectroscopy and thermogravimetric analysis. Activity results showed that, depending on the support, immobilization was governed by different interactions. On FNS and AFNS immobilization was exclusively by adsorption, while on CCAFNS after the initial adsorption lipase molecules reoriented and amino groups of the enzyme formed a covalent bond with the chlorine atom of the modified carrier. Improved thermal and operational stability of lipase immobilized on CCAFNS in 1molL(-1) buffer led to the conclusion that electrostatic interactions have a great role in the immobilization. PB - Wiley-Blackwell, Hoboken T2 - Journal of Chemical Technology and Biotechnology T1 - Cyanuric chloride functionalized silica nanoparticles for covalent immobilization of lipase EP - 448 IS - 2 SP - 439 VL - 91 DO - 10.1002/jctb.4595 ER -
@article{ author = "Banjanac, Katarina and Mihailović, Mladen and Prlainović, Nevena and Stojanović, Marija and Simović, Milica and Marinković, Aleksandar and Bezbradica, Dejan", year = "2016", abstract = "BACKGROUNDIn this work, fumed nano-silica (FNS) was chemically modified to amino (AFNS) and subsequently to cyanuric chloride (CCAFNS) modified silica and tested for the immobilization of lipase from Candida rugosa (CRL). The effects of the initial enzyme concentration, immobilization time and buffer ionic strength on immobilization were investigated in order to optimize utilization of the support and determine the mechanism of immobilization. The most active preparations were used to examine thermal and operational stability. RESULTSThe amount of immobilized enzyme increased with increasing enzyme concentration, achieving loadings of 121.3, 104.8 and 61.2mg per g of FNS, CCAFNS and AFNS, respectively. Lipase immobilized on CCAFNS carrier in 0.1molL(-1) buffer expressed the highest lipolytic activity (1320 IU g(-1) support), while more stable preparations were obtained in 1molL(-1) buffer. CONCLUSIONSuccessful modification of silica was confirmed with Fourier transform infrared spectroscopy and thermogravimetric analysis. Activity results showed that, depending on the support, immobilization was governed by different interactions. On FNS and AFNS immobilization was exclusively by adsorption, while on CCAFNS after the initial adsorption lipase molecules reoriented and amino groups of the enzyme formed a covalent bond with the chlorine atom of the modified carrier. Improved thermal and operational stability of lipase immobilized on CCAFNS in 1molL(-1) buffer led to the conclusion that electrostatic interactions have a great role in the immobilization.", publisher = "Wiley-Blackwell, Hoboken", journal = "Journal of Chemical Technology and Biotechnology", title = "Cyanuric chloride functionalized silica nanoparticles for covalent immobilization of lipase", pages = "448-439", number = "2", volume = "91", doi = "10.1002/jctb.4595" }
Banjanac, K., Mihailović, M., Prlainović, N., Stojanović, M., Simović, M., Marinković, A.,& Bezbradica, D.. (2016). Cyanuric chloride functionalized silica nanoparticles for covalent immobilization of lipase. in Journal of Chemical Technology and Biotechnology Wiley-Blackwell, Hoboken., 91(2), 439-448. https://doi.org/10.1002/jctb.4595
Banjanac K, Mihailović M, Prlainović N, Stojanović M, Simović M, Marinković A, Bezbradica D. Cyanuric chloride functionalized silica nanoparticles for covalent immobilization of lipase. in Journal of Chemical Technology and Biotechnology. 2016;91(2):439-448. doi:10.1002/jctb.4595 .
Banjanac, Katarina, Mihailović, Mladen, Prlainović, Nevena, Stojanović, Marija, Simović, Milica, Marinković, Aleksandar, Bezbradica, Dejan, "Cyanuric chloride functionalized silica nanoparticles for covalent immobilization of lipase" in Journal of Chemical Technology and Biotechnology, 91, no. 2 (2016):439-448, https://doi.org/10.1002/jctb.4595 . .