Highly stable and versatile α-amylase from Anoxybacillus vranjensis ST4 suitable for various applications
Само за регистроване кориснике
2023
Аутори
Slavić, Marinela ŠokardaKojić, Milan
Margetić, Aleksandra
Stanisavljević, Nemanja
Gardijan, Lazar
Božić, Nataša
Vujčić, Zoran
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
α-Amylase from the thermophilic bacterial strain Anoxybacillus vranjensis ST4 (AVA) was cloned into the pMALc5HisEk expression vector and successfully expressed and purified from the Escherichia coli ER2523 host strain. AVA belongs to the GH13_5 subfamily of glycoside hydrolases and has 7 conserved sequence regions (CSRs) distributed in three distinct domains (A, B, C). In addition, there is a starch binding domain (SBD) from the CBM20 family of carbohydrate binding modules (CBMs). AVA is a monomer of 66 kDa that achieves maximum activity at 60–80 °C and is active and stable over a wide pH range (4.0–9.0). AVA retained 50 % of its activity after 31 h of incubation at 60 °C and was resistant to a large number of denaturing agents. It hydrolyzed starch granules very efficiently, releasing maltose, maltotriose and maltopentaose as the main products. The hydrolysis rates of raw corn, wheat, horseradish, and potato starch, at a concentration of 10 %, were 87.8, 85.9, 93.0, and 58 %, respect...ively, at pH 8.5 over a 3 h period. This study showed that the high level of expression as well as the properties of this highly stable and versatile enzyme show all the prerequisites for successful application in industry.
Кључне речи:
pMALc5HisEk expression vector / Starch / α-AmylaseИзвор:
International Journal of Biological Macromolecules, 2023, 249, 126055-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)
- Министарство науке, технолошког развоја и иновација Републике Србије, институционално финансирање - 200168 (Универзитет у Београду, Хемијски факултет) (RS-MESTD-inst-2020-200168)
- Министарство науке, технолошког развоја и иновација Републике Србије, институционално финансирање - 200042 (Универзитет у Београду, Институт за молекуларну генетику и генетичко инжењерство) (RS-MESTD-inst-2020-200042)
- Министарство науке, технолошког развоја и иновација Републике Србије, институционално финансирање - 200177 (Центар за имунолошка истраживања 'Бранислав Јанковић' Торлак, Београд) (RS-MESTD-inst-2020-200177)
URI
https://www.sciencedirect.com/science/article/pii/S0141813023029501https://imagine.imgge.bg.ac.rs/handle/123456789/2066
Колекције
Институција/група
Institut za molekularnu genetiku i genetičko inženjerstvoTY - JOUR AU - Slavić, Marinela Šokarda AU - Kojić, Milan AU - Margetić, Aleksandra AU - Stanisavljević, Nemanja AU - Gardijan, Lazar AU - Božić, Nataša AU - Vujčić, Zoran PY - 2023 UR - https://www.sciencedirect.com/science/article/pii/S0141813023029501 UR - https://imagine.imgge.bg.ac.rs/handle/123456789/2066 AB - α-Amylase from the thermophilic bacterial strain Anoxybacillus vranjensis ST4 (AVA) was cloned into the pMALc5HisEk expression vector and successfully expressed and purified from the Escherichia coli ER2523 host strain. AVA belongs to the GH13_5 subfamily of glycoside hydrolases and has 7 conserved sequence regions (CSRs) distributed in three distinct domains (A, B, C). In addition, there is a starch binding domain (SBD) from the CBM20 family of carbohydrate binding modules (CBMs). AVA is a monomer of 66 kDa that achieves maximum activity at 60–80 °C and is active and stable over a wide pH range (4.0–9.0). AVA retained 50 % of its activity after 31 h of incubation at 60 °C and was resistant to a large number of denaturing agents. It hydrolyzed starch granules very efficiently, releasing maltose, maltotriose and maltopentaose as the main products. The hydrolysis rates of raw corn, wheat, horseradish, and potato starch, at a concentration of 10 %, were 87.8, 85.9, 93.0, and 58 %, respectively, at pH 8.5 over a 3 h period. This study showed that the high level of expression as well as the properties of this highly stable and versatile enzyme show all the prerequisites for successful application in industry. T2 - International Journal of Biological Macromolecules T1 - Highly stable and versatile α-amylase from Anoxybacillus vranjensis ST4 suitable for various applications SP - 126055 VL - 249 DO - 10.1016/j.ijbiomac.2023.126055 ER -
@article{ author = "Slavić, Marinela Šokarda and Kojić, Milan and Margetić, Aleksandra and Stanisavljević, Nemanja and Gardijan, Lazar and Božić, Nataša and Vujčić, Zoran", year = "2023", abstract = "α-Amylase from the thermophilic bacterial strain Anoxybacillus vranjensis ST4 (AVA) was cloned into the pMALc5HisEk expression vector and successfully expressed and purified from the Escherichia coli ER2523 host strain. AVA belongs to the GH13_5 subfamily of glycoside hydrolases and has 7 conserved sequence regions (CSRs) distributed in three distinct domains (A, B, C). In addition, there is a starch binding domain (SBD) from the CBM20 family of carbohydrate binding modules (CBMs). AVA is a monomer of 66 kDa that achieves maximum activity at 60–80 °C and is active and stable over a wide pH range (4.0–9.0). AVA retained 50 % of its activity after 31 h of incubation at 60 °C and was resistant to a large number of denaturing agents. It hydrolyzed starch granules very efficiently, releasing maltose, maltotriose and maltopentaose as the main products. The hydrolysis rates of raw corn, wheat, horseradish, and potato starch, at a concentration of 10 %, were 87.8, 85.9, 93.0, and 58 %, respectively, at pH 8.5 over a 3 h period. This study showed that the high level of expression as well as the properties of this highly stable and versatile enzyme show all the prerequisites for successful application in industry.", journal = "International Journal of Biological Macromolecules", title = "Highly stable and versatile α-amylase from Anoxybacillus vranjensis ST4 suitable for various applications", pages = "126055", volume = "249", doi = "10.1016/j.ijbiomac.2023.126055" }
Slavić, M. Š., Kojić, M., Margetić, A., Stanisavljević, N., Gardijan, L., Božić, N.,& Vujčić, Z.. (2023). Highly stable and versatile α-amylase from Anoxybacillus vranjensis ST4 suitable for various applications. in International Journal of Biological Macromolecules, 249, 126055. https://doi.org/10.1016/j.ijbiomac.2023.126055
Slavić MŠ, Kojić M, Margetić A, Stanisavljević N, Gardijan L, Božić N, Vujčić Z. Highly stable and versatile α-amylase from Anoxybacillus vranjensis ST4 suitable for various applications. in International Journal of Biological Macromolecules. 2023;249:126055. doi:10.1016/j.ijbiomac.2023.126055 .
Slavić, Marinela Šokarda, Kojić, Milan, Margetić, Aleksandra, Stanisavljević, Nemanja, Gardijan, Lazar, Božić, Nataša, Vujčić, Zoran, "Highly stable and versatile α-amylase from Anoxybacillus vranjensis ST4 suitable for various applications" in International Journal of Biological Macromolecules, 249 (2023):126055, https://doi.org/10.1016/j.ijbiomac.2023.126055 . .