Immobilization of α-amylase from bacillus paralicheniformis on bentonites
Аутори
Kosić, VišnjaPavlović, Stefan
Božić, Nataša
Dojnov, Biljana
Stevanović, Gordana
Knežević-Jugović, Zorica
Milutinović Nikolić, Aleksandra
Конференцијски прилог (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
α-Amylase from Bacillus paralicheniformis (BliAmy) is a highly efficient raw starch digesting enzyme. Starch is an inexpensive source of many food industrial products. Naturally occurring clay are non-toxic, environmentally friendly and inexpensive. Therefore, immobilization of BliAmy by adsorption on three differently modified bentonites was studied. Modifications included common Na-exchange procedure, acid activation, and alkali activation. The modified clays were characterized by X-ray powder diffraction, mercury intrusion porosimetry and the points of zero charge were determined. The adsorption of the enzyme was significantly influenced by the type of modification of bentonite, being the highest for the acid-activated bentonite with the highest porosity. On the other hand, the highest enzyme activity for immobilized α-amylase was obtained with alkali-modified bentonite (98 U/g), suggesting it as a good candidate for immobilization of α-amylase for application in the food industry.
Кључне речи:
α-Amylase / Bacillus paralicheniformis / raw starch / immobilization / modified bentonitesИзвор:
Proceedings - 16th International Conference on Fundamental and Applied Aspects of Physical Chemistry, Physical Chemistry 2022, September, 26-30, 2022, Belgrade, Serbia, 2022, 161-164Издавач:
- The Society of Physical Chemists of Serbia
Финансирање / пројекти:
- Министарство науке, технолошког развоја и иновација Републике Србије, институционално финансирање - 200026 (Универзитет у Београду, Институт за хемију, технологију и металургију - ИХТМ) (RS-MESTD-inst-2020-200026)
Институција/група
IHTMTY - CONF AU - Kosić, Višnja AU - Pavlović, Stefan AU - Božić, Nataša AU - Dojnov, Biljana AU - Stevanović, Gordana AU - Knežević-Jugović, Zorica AU - Milutinović Nikolić, Aleksandra PY - 2022 UR - https://cer.ihtm.bg.ac.rs/handle/123456789/5925 AB - α-Amylase from Bacillus paralicheniformis (BliAmy) is a highly efficient raw starch digesting enzyme. Starch is an inexpensive source of many food industrial products. Naturally occurring clay are non-toxic, environmentally friendly and inexpensive. Therefore, immobilization of BliAmy by adsorption on three differently modified bentonites was studied. Modifications included common Na-exchange procedure, acid activation, and alkali activation. The modified clays were characterized by X-ray powder diffraction, mercury intrusion porosimetry and the points of zero charge were determined. The adsorption of the enzyme was significantly influenced by the type of modification of bentonite, being the highest for the acid-activated bentonite with the highest porosity. On the other hand, the highest enzyme activity for immobilized α-amylase was obtained with alkali-modified bentonite (98 U/g), suggesting it as a good candidate for immobilization of α-amylase for application in the food industry. PB - The Society of Physical Chemists of Serbia C3 - Proceedings - 16th International Conference on Fundamental and Applied Aspects of Physical Chemistry, Physical Chemistry 2022, September, 26-30, 2022, Belgrade, Serbia T1 - Immobilization of α-amylase from bacillus paralicheniformis on bentonites SP - 161 EP - 164 UR - https://hdl.handle.net/21.15107/rcub_cer_5925 ER -
@conference{ author = "Kosić, Višnja and Pavlović, Stefan and Božić, Nataša and Dojnov, Biljana and Stevanović, Gordana and Knežević-Jugović, Zorica and Milutinović Nikolić, Aleksandra", year = "2022", abstract = "α-Amylase from Bacillus paralicheniformis (BliAmy) is a highly efficient raw starch digesting enzyme. Starch is an inexpensive source of many food industrial products. Naturally occurring clay are non-toxic, environmentally friendly and inexpensive. Therefore, immobilization of BliAmy by adsorption on three differently modified bentonites was studied. Modifications included common Na-exchange procedure, acid activation, and alkali activation. The modified clays were characterized by X-ray powder diffraction, mercury intrusion porosimetry and the points of zero charge were determined. The adsorption of the enzyme was significantly influenced by the type of modification of bentonite, being the highest for the acid-activated bentonite with the highest porosity. On the other hand, the highest enzyme activity for immobilized α-amylase was obtained with alkali-modified bentonite (98 U/g), suggesting it as a good candidate for immobilization of α-amylase for application in the food industry.", publisher = "The Society of Physical Chemists of Serbia", journal = "Proceedings - 16th International Conference on Fundamental and Applied Aspects of Physical Chemistry, Physical Chemistry 2022, September, 26-30, 2022, Belgrade, Serbia", title = "Immobilization of α-amylase from bacillus paralicheniformis on bentonites", pages = "161-164", url = "https://hdl.handle.net/21.15107/rcub_cer_5925" }
Kosić, V., Pavlović, S., Božić, N., Dojnov, B., Stevanović, G., Knežević-Jugović, Z.,& Milutinović Nikolić, A.. (2022). Immobilization of α-amylase from bacillus paralicheniformis on bentonites. in Proceedings - 16th International Conference on Fundamental and Applied Aspects of Physical Chemistry, Physical Chemistry 2022, September, 26-30, 2022, Belgrade, Serbia The Society of Physical Chemists of Serbia., 161-164. https://hdl.handle.net/21.15107/rcub_cer_5925
Kosić V, Pavlović S, Božić N, Dojnov B, Stevanović G, Knežević-Jugović Z, Milutinović Nikolić A. Immobilization of α-amylase from bacillus paralicheniformis on bentonites. in Proceedings - 16th International Conference on Fundamental and Applied Aspects of Physical Chemistry, Physical Chemistry 2022, September, 26-30, 2022, Belgrade, Serbia. 2022;:161-164. https://hdl.handle.net/21.15107/rcub_cer_5925 .
Kosić, Višnja, Pavlović, Stefan, Božić, Nataša, Dojnov, Biljana, Stevanović, Gordana, Knežević-Jugović, Zorica, Milutinović Nikolić, Aleksandra, "Immobilization of α-amylase from bacillus paralicheniformis on bentonites" in Proceedings - 16th International Conference on Fundamental and Applied Aspects of Physical Chemistry, Physical Chemistry 2022, September, 26-30, 2022, Belgrade, Serbia (2022):161-164, https://hdl.handle.net/21.15107/rcub_cer_5925 .