@conference{
author = "Mijalković, Jelena and Stefanović, Andrea and Pavlović, Neda and Šekuljica, Nataša and Jakovetić Tanasković, Sonja and Gazikalović, Ivana and Knežević-Jugović, Zorica",
year = "2023",
abstract = "Soybean, a protein-rich leguminous oilseed, is often unacceptable due to its taste,
appearance, and smell. Enzymatic technologies offer an alternative to conventional chemical
procedures for protein modification, allowing for accurate oversight and adjustment of reaction
flow to desired nutritional and bioactive properties due to the high sensitivity of protease under
mild reaction conditions.
Herein, the feasibility of implementing a one- or two-step biotechnological process,
triggered by commercial endo- and exo-peptidases, to enhance the nutritional and bioactive
characteristics of soy protein concentrates (SPC), was investigated. Two nutritionally valuable
fractions, the hydrolysate (liquid stream-fraction) and the ocara (solid stream-fraction), have been
separated. The hydrolysates were characterized by examining the crude protein content, protein
recovery, and free amino group content. The antioxidant activity was quantified by measuring
superoxide radical inhibition, and metal-ion chelation.
Commercial peptidases led to different reaction kinetics and protein recovery, resulting in
different peptide profiles determined by dead-end ultrafiltration (3, 10, and 30 kDa) and
subsequent gel-filtration chromatography using the Toyopearl HW40F resin. Enzymatic
hydrolysis seemed to enhance the hydrolyzate's protein content while decreasing the ocara's
protein content. The percentage of soluble protein recovered from SPC ranged between 68 and
82%, revealing that Flavourzyme was most suitable to solubilize SPC. The highest yield of
hydrolyzed peptide bonds, correlated with higher antioxidant activity, was shown by Alcalase-
Flavourzyme (~20%) as well as Neutrase-Flavourzyme (~21.5%), with a tendency to favor
Neutrase due to more sensory-acceptable product. Each produced hydrolysate's amino acid
content, sulfhydryl groups, and surface hydrophobicity have been examined, and substantial
correlations with antioxidant activity have been found. Because the quantity of phytic acid and
trypsin inhibitor, the principal anti-nutritional components of SPC, was greatly reduced by
enzymatic hydrolysis, the ocara were classified as value-added byproducts. Neutrase-
Flavourzyme hydrolyzate's antioxidant activity was attributed to its large proportion of peptide
fractions below 3 kDa.",
publisher = "Belgrade : University, Faculty of Technology and Metallurgy",
journal = "Book of Abstracts / International Conference Biochemical Engineering and Biotechnology for Young Scientists, Belgrade, 2023",
title = "ENHANCEMENT OF THE BIOACTIVE AND NUTRITIONAL PROPERTIES OF SOY PROTEIN CONCENTRATE THROUGH THE USE OF ENZYME TECHNOLOGY",
pages = "79",
url = "https://hdl.handle.net/21.15107/rcub_technorep_7018"
}