@conference{
author = "Nenadović, Marija and Tomić, Nevena and Nikolić, Stefan and Vujčić, Zoran and Šokarda Slavić, Marinela",
year = "2021",
abstract = "Zein is produced in large quantities as a byproduct of corn starch manufacturing since it
constitutes a majority of the total protein of maize seed (44–70%). Enzymatic treatment of
zein significantly improves its aqueous solubility and provides peptides that are used as
animal feed, functional food, or biologically active carriers for other bioactive molecules.
Moreover, zein-derived peptides exhibit antioxidant, anti-inflammatory, antihypertensive,
anticancer, and antimicrobial activities in human organisms 1. Few attempts up to this day
have been made to screen for microorganisms that are capable of zein degradation.
Available protocols for proteases identification almost exclusively rely on screening on
casein, skim milk, and gelatin agar in limited experimental conditions. We have screened
different Bacillus sp strains isolated from across Serbia for zein-degrading proteases. To
do so we developed an inexpensive, simple, and reproducible way of high throughput
functional screening of zein-degrading proteases on zein-containing gels. Besides detecting
proteases with specificity towards zein, a developed diffusion assay was designed to
support screening for naturally occurring robust proteases with high potential for industrial
application. By using classical methods of protein purification, we isolated an alkaline
thermostable protease from Bacillus amyloliquefaciens strain 12B that is resistant to the
presence of detergents, organic solvents, and high salt concentrations.",
publisher = "University of Belgrade - Faculty of Chemistry, Serbian Biochemical Society",
journal = "Proceedings - X Conference of Serbian Biochemical Society with international participation, “Biochemical Insights into Molecular Mechanisms”, 24.09.2021. Kragujevac, Serbia",
title = "A search for nature’s robust proteases with zein as a substrate",
pages = "158-158",
url = "https://hdl.handle.net/21.15107/rcub_cer_6456"
}