@conference{
author = "Pavlović, Marija and Kojić, Milan and Ristović, Marina and Stojanović, Sanja and Margetić, Aleksandra and Vujčić, Zoran and Šokarda Slavić, Marinela",
year = "2024",
abstract = "This research deals with the characterization of a thermostable endo-1,4-beta-xylanase enzyme from Anoxybacillus vranjensis ST4, a thermophilic bacterium isolated from Vranjska Banja hot spring, Serbia. The enzyme shows a high degree of identity with the same type of enzyme from other species of the genera Anoxybacillus (97%), Geobacillus (74%) and Paenibacillus (65%). The gene for endo-1,4-beta-xylanase from the thermophilic strain ST4 was cloned into the pQE_Ek expression vector and successfully expressed and purified from the Escherichia coli M15[pREP4]. The study encompasses recombinant production, purification, and the comprehensive characterization of the enzymatic properties of endo-1,4-beta-xylanase. This is the first successful overexpression, purification and characterization of a recombinant thermostable endo-1,4-beta-xylanase enzyme from Anoxybacillus. With a monomeric structure of 38.7 kDa, the enzyme demonstrates peak activity at 70°C and pH 6.5. Notably, it exhibits remarkable stability across a wide pH range and at high temperatures, rendering it suitable for diverse industrial applications. Investigation into the enzyme’s kinetic parameters, substrate specificity, and its ability to degrade xylan into high-energy value products further enhances understanding of its biotechnological potential. These findings underscore the significance of thermophilic bacteria and their thermostable enzymes in various industrial processes.",
publisher = "Serbian Society for Microbiology",
journal = "XIII Congress of microbiologists of Serbia, Book of abstracts, April 4-6, 2024, Belgrade, Serbia",
title = "Cloning, overexpression and characterization of a thermostable endo-1,4-beta-xylanase from Anoxybacillus vranjensis ST4",
pages = "31-31",
url = "https://hdl.handle.net/21.15107/rcub_intor_936"
}