Highly stable and versatile α-amylase from Anoxybacillus vranjensis ST4 suitable for various applications
Samo za registrovane korisnike
2023
Autori
Šokarda Slavić, MarinelaKojić, Milan
Margetić, Aleksandra
Stanisavljević, Nemanja
Gardijan, Lazar
Božić, Nataša
Vujčić, Zoran
Članak u časopisu (Objavljena verzija)
Metapodaci
Prikaz svih podataka o dokumentuApstrakt
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.
Ključne reči:
α-Amylase / Anoxybacillus vranjensis / pMALc5HisEk expression vector / StarchIzvor:
International Journal of Biological Macromolecules, 2023, 249, 126055-Izdavač:
- Elsevier
Finansiranje / projekti:
- Ministarstvo nauke, tehnološkog razvoja i inovacija Republike Srbije, institucionalno finansiranje - 200026 (Univerzitet u Beogradu, Institut za hemiju, tehnologiju i metalurgiju - IHTM) (RS-MESTD-inst-2020-200026)
- Ministarstvo nauke, tehnološkog razvoja i inovacija Republike Srbije, institucionalno finansiranje - 200168 (Univerzitet u Beogradu, Hemijski fakultet) (RS-MESTD-inst-2020-200168)
- Ministarstvo nauke, tehnološkog razvoja i inovacija Republike Srbije, institucionalno finansiranje - 200042 (Univerzitet u Beogradu, Institut za molekularnu genetiku i genetičko inženjerstvo) (RS-MESTD-inst-2020-200042)
- Ministarstvo nauke, tehnološkog razvoja i inovacija Republike Srbije, institucionalno finansiranje - 200177 (Centar za imunološka istraživanja 'Branislav Janković' Torlak, Beograd) (RS-MESTD-inst-2020-200177)
Institucija/grupa
TorlakTY - JOUR AU - Šokarda Slavić, Marinela AU - Kojić, Milan AU - Margetić, Aleksandra AU - Stanisavljević, Nemanja AU - Gardijan, Lazar AU - Božić, Nataša AU - Vujčić, Zoran PY - 2023 UR - http://intor.torlakinstitut.com/handle/123456789/634 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. PB - Elsevier 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 = "Šokarda Slavić, Marinela 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.", publisher = "Elsevier", 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" }
Šokarda Slavić, M., 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 Elsevier., 249, 126055. https://doi.org/10.1016/j.ijbiomac.2023.126055
Šokarda Slavić M, 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 .
Šokarda Slavić, Marinela, 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 . .