Name: Nataša Božić

Affiliation: The University of Belgrade, Institute of Chemistry, Technology and Metallurgy, National Institute of the Republic of Serbia (ICTM)

Address: Studentski trg 12-16, 11000 Belgrade

ORCID: 0000-0001-8735-5506

Scopus: 25225074400

Short biography:

She received her PhD in Biochemistry in 2007 from the University of Belgrade, Faculty of Chemistry. In 2009, she completed postdoctoral research in fermentation technology at the Department of Chemical Engineering, Autonomous University of Barcelona, supported by a fellowship from the Ministry of Science and Technological Development of the Republic of Serbia. She continued advanced training at the same institution in molecular biotechnology through several research stays, including a Federation of European Biochemical Societies (FEBS) fellowship in 2010 and additional visits within a bilateral project in 2011 and 2012.

Her expertise spans upstream and downstream processing of glycoside hydrolases and oxidoreductases, encompassing enzyme discovery and development, microbial strain screening, enzyme engineering, and fermentation technologies. She has extensive experience in enzyme immobilization and continuous biotransformations, has authored over 40 peer-reviewed publications and has coordinated several national and international research projects. Dr. Božić has a strong record of mentoring doctoral students and leading interdisciplinary research, with a particular focus in developing robust and sustainable biocatalysts for industrial and biotechnological applications.

University/Company description:

The University of Belgrade, Institute of Chemistry, Technology and Metallurgy, National Institute of the Republic of Serbia (ICTM) is a National Institute of the Republic of Serbia and one of eight national research institutes in the country. Founded in 1961, ICTM employs 270 full-time researchers and staff and conducts both fundamental and applied research primarily in chemistry and related technologies. Its activities are organized through six scientific departments, two Centers of Excellence, and an ISO/IEC 17025–accredited Laboratory for Instrumental Analysis.

ICTM has extensive expertise across the full spectrum of chemistry and chemical engineering, including synthetic organic, inorganic, medicinal, computational, analytical, and biochemistry, as well as biotechnology, polymers, electrochemistry, catalysis, advanced materials, technological device development, and environmental protection. The Institute has a strong track record in applied research, knowledge transfer, and collaboration with industry, supporting the development of innovative technologies, solutions, and products with national and international impact.

Facilities, infrastructure & equipment:

• Bioprocessing and microbiology: microbiology shakers, incubators, a Biostat B plus laboratory fermenter, centrifuges, homogenizer, sonicator.
• Protein production and purification: various electrophoresis systems, gel imager, PCR thermocyclers, FPLC and ÄKTA systems,
• Microscopy and imaging: fluorescent and light microscopes.
• Analytics: Dionex HPLC with Diode Array (DAD) and Refractive Index (RI) detectors, spectrophotometer, fluorimeter, access to IC, GC, GC-MS, HPLC-MS, FTIR and NMR.

Relevant publications and/or research/innovation products:

1. V. Kosić, N. Božić, B. Dojnov, P. Banković, N. Jović-Jovičić, Z. Knežević-Jugović, A. Milutinović-Nikolić. Significantly improved stabilization of glycoside hydrolase important in food industry by immobilization onto appropriately modified beidellite, Applied Clay Science, 2024, 250, 107289. 10.1016/j.clay.2024.107289
2. M. Šokarda Slavić, A. Margetić, B. Dojnov, M. Vujčić, M. Mišić, N. Božić, Z. Vujčić. Modified simultaneous saccharification and fermentation for the production of bioethanol from highly concentrated raw corn starch. Fuel, 2023, 338, 127363. 10.1016/j.fuel.2022.127363
3. M. Šokarda Slavić, M. Kojić, A. Margetić, N. Stanisavljević, L. Gardijan, N. Božić, Z. Vujčić. Highly stable and versatile α-amylase from Anoxybacillus vranjensis ST4 suitable for various applications. International Journal of Biological Macromolecules, 2023, 249, 126055. 10.1016/j.ijbiomac.2023.126055
4. N. Božić, H. Rozeboom, N. Lončar, M. Šokarda Slavić, D. Janssen, Z. Vujčić. Characterization of the starch surface binding site on Bacillus paralicheniformis α-amylase, International Journal of Biological Macromolecules, 2020, 165, 1529-1539. 10.1016/j.ijbiomac.2020.10.025
5. S. Simić, S. Jeremić, L. Đokić, N. Božić, Z. Vujčić, N. Lončar, R. Senthamaraikannan, R. Babu, I. Opsenica, J. Nikodinovic-Runic. Development of an efficient biocatalytic system based on bacterial laccase for the oxidation of selected 1,4-dihydropyridines, Enzyme and Microbial Technology, 2020, 132, 109411. 10.1016/j.enzmictec.2019.109411