Novel β-galactosidase nanobiocatalyst systems for application in the synthesis of bioactive galactosides
2016
Аутори
Banjanac, KatarinaSimović, Milica
Ćorović, Marija
Milivojević, Ana
Prlainović, Nevena
Marinković, Aleksandar
Bezbradica, Dejan
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
In this study, unmodified, amino modified and cyanuric chloride functionalized amino modified nonporous fumed nano-silica particles (FNS, AFNS and CCAFNS, respectively) were used for the development of efficient nanobiocatalysts for application in the biosynthesis of bioactive galactosides, galacto-oligosaccharides (GOS). Hence, in an attempt to elucidate the mechanism of immobilization, based on available enzyme conformation, the effects of immobilization parameters (initial enzyme concentration, immobilization time and pH) were analyzed. Among all three used nano-sized supports, the one with amino groups (AFNS) exhibited the best beta-galactosidase binding capacity of 220 mg g(-1) support with the efficiency of similar to 90% at pH 4.5 and immobilization time 3 h. The highest hydrolytic activity of similar to 2200 IU g(-1) was achieved, which is far higher than previously reported. Meanwhile, beta-galactosidases covalently immobilized on CCAFNS and adsorbed on FNS nanoparticles were ...found to have similar trends with respect to immobilization efficiency (58-71%) and hydrolytic activity (similar to 600 IU g(-1)). Furthermore, thermal stability at 60 degrees C was increased by beta-galactosidases immobilized on AFNS and CCAFNS (4 and 1.4-fold, respectively) due to the protective effect of interactions formed between enzyme molecules and the surfaces of nanoparticles. Since b-galactosidase immobilized on AFNS was the nanobiocatalyst with the highest activity and stability, it was applied in GOS production. With AFNS- beta-galactosidase GOS production of 90 g L-1 h(-1) was achieved as compared to 30 g L-1 h(-1) by free beta-beta-galactosidase, meaning that AFNS enhanced the selectivity of b-galactosidase for transgalactosylation, which is a crucial advantage for its application in GOS production.
Извор:
RSC Advances, 2016, 6, 99, 97216-97225Издавач:
- Royal Society of Chemistry
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-46010)
- Проучавање синтезе, структуре и активности органских једињења природног и синтетског порекла (RS-172013)
- Синтеза, развој технологија добијања и примена наноструктурних мултифункционалних материјала дефинисаних својстава (RS-45019)
DOI: 10.1039/c6ra20409k
ISSN: 2046-2069
WoS: 000386242500095
Scopus: 2-s2.0-84991730114
Колекције
Институција/група
Tehnološko-metalurški fakultetTY - JOUR AU - Banjanac, Katarina AU - Simović, Milica AU - Ćorović, Marija AU - Milivojević, Ana AU - Prlainović, Nevena AU - Marinković, Aleksandar AU - Bezbradica, Dejan PY - 2016 UR - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/3298 AB - In this study, unmodified, amino modified and cyanuric chloride functionalized amino modified nonporous fumed nano-silica particles (FNS, AFNS and CCAFNS, respectively) were used for the development of efficient nanobiocatalysts for application in the biosynthesis of bioactive galactosides, galacto-oligosaccharides (GOS). Hence, in an attempt to elucidate the mechanism of immobilization, based on available enzyme conformation, the effects of immobilization parameters (initial enzyme concentration, immobilization time and pH) were analyzed. Among all three used nano-sized supports, the one with amino groups (AFNS) exhibited the best beta-galactosidase binding capacity of 220 mg g(-1) support with the efficiency of similar to 90% at pH 4.5 and immobilization time 3 h. The highest hydrolytic activity of similar to 2200 IU g(-1) was achieved, which is far higher than previously reported. Meanwhile, beta-galactosidases covalently immobilized on CCAFNS and adsorbed on FNS nanoparticles were found to have similar trends with respect to immobilization efficiency (58-71%) and hydrolytic activity (similar to 600 IU g(-1)). Furthermore, thermal stability at 60 degrees C was increased by beta-galactosidases immobilized on AFNS and CCAFNS (4 and 1.4-fold, respectively) due to the protective effect of interactions formed between enzyme molecules and the surfaces of nanoparticles. Since b-galactosidase immobilized on AFNS was the nanobiocatalyst with the highest activity and stability, it was applied in GOS production. With AFNS- beta-galactosidase GOS production of 90 g L-1 h(-1) was achieved as compared to 30 g L-1 h(-1) by free beta-beta-galactosidase, meaning that AFNS enhanced the selectivity of b-galactosidase for transgalactosylation, which is a crucial advantage for its application in GOS production. PB - Royal Society of Chemistry T2 - RSC Advances T1 - Novel β-galactosidase nanobiocatalyst systems for application in the synthesis of bioactive galactosides EP - 97225 IS - 99 SP - 97216 VL - 6 DO - 10.1039/c6ra20409k ER -
@article{ author = "Banjanac, Katarina and Simović, Milica and Ćorović, Marija and Milivojević, Ana and Prlainović, Nevena and Marinković, Aleksandar and Bezbradica, Dejan", year = "2016", abstract = "In this study, unmodified, amino modified and cyanuric chloride functionalized amino modified nonporous fumed nano-silica particles (FNS, AFNS and CCAFNS, respectively) were used for the development of efficient nanobiocatalysts for application in the biosynthesis of bioactive galactosides, galacto-oligosaccharides (GOS). Hence, in an attempt to elucidate the mechanism of immobilization, based on available enzyme conformation, the effects of immobilization parameters (initial enzyme concentration, immobilization time and pH) were analyzed. Among all three used nano-sized supports, the one with amino groups (AFNS) exhibited the best beta-galactosidase binding capacity of 220 mg g(-1) support with the efficiency of similar to 90% at pH 4.5 and immobilization time 3 h. The highest hydrolytic activity of similar to 2200 IU g(-1) was achieved, which is far higher than previously reported. Meanwhile, beta-galactosidases covalently immobilized on CCAFNS and adsorbed on FNS nanoparticles were found to have similar trends with respect to immobilization efficiency (58-71%) and hydrolytic activity (similar to 600 IU g(-1)). Furthermore, thermal stability at 60 degrees C was increased by beta-galactosidases immobilized on AFNS and CCAFNS (4 and 1.4-fold, respectively) due to the protective effect of interactions formed between enzyme molecules and the surfaces of nanoparticles. Since b-galactosidase immobilized on AFNS was the nanobiocatalyst with the highest activity and stability, it was applied in GOS production. With AFNS- beta-galactosidase GOS production of 90 g L-1 h(-1) was achieved as compared to 30 g L-1 h(-1) by free beta-beta-galactosidase, meaning that AFNS enhanced the selectivity of b-galactosidase for transgalactosylation, which is a crucial advantage for its application in GOS production.", publisher = "Royal Society of Chemistry", journal = "RSC Advances", title = "Novel β-galactosidase nanobiocatalyst systems for application in the synthesis of bioactive galactosides", pages = "97225-97216", number = "99", volume = "6", doi = "10.1039/c6ra20409k" }
Banjanac, K., Simović, M., Ćorović, M., Milivojević, A., Prlainović, N., Marinković, A.,& Bezbradica, D.. (2016). Novel β-galactosidase nanobiocatalyst systems for application in the synthesis of bioactive galactosides. in RSC Advances Royal Society of Chemistry., 6(99), 97216-97225. https://doi.org/10.1039/c6ra20409k
Banjanac K, Simović M, Ćorović M, Milivojević A, Prlainović N, Marinković A, Bezbradica D. Novel β-galactosidase nanobiocatalyst systems for application in the synthesis of bioactive galactosides. in RSC Advances. 2016;6(99):97216-97225. doi:10.1039/c6ra20409k .
Banjanac, Katarina, Simović, Milica, Ćorović, Marija, Milivojević, Ana, Prlainović, Nevena, Marinković, Aleksandar, Bezbradica, Dejan, "Novel β-galactosidase nanobiocatalyst systems for application in the synthesis of bioactive galactosides" in RSC Advances, 6, no. 99 (2016):97216-97225, https://doi.org/10.1039/c6ra20409k . .