Biocatalytic conversion of milk proteins into low molecular peptides
https://doi.org/10.29235/1561-8331-2025-61-3-227-236
Abstract
A comparative analysis of the efficiency of milk protein hydrolysis by trypsin and neutral protease using different methods of their addition was conducted. It was found that proteolysis by trypsin (enzyme-substrate ratio 1 : 40) at a temperature 37 °C and pH 8.0 leads to the formation of 81.2 ± 5.5 % of peptides with molecular mass less than 3.0 kDa, while protein hydrolysis by neutral protease (enzyme-substrate ratio 1 : 20) under the same conditions produces 86.6 ± 4.7 % of low molecular weight peptide fractions. It was shown that sequential application of trypsin and neutral protease allows obtaining, on average, 94.9 % of short peptides in comparison with the joint addition (91.3 ± 1.1 % of low molecular weight peptides). The application of the single enzyme provides the production of partial hydrolysates that can be used in the formulation of functional foods with reduced allergenicity, while the sequential and joint addition of trypsin and neutral protease generates extensive hydrolysates, which are considered optimal ingredients in the creation of hypoallergenic food products.
About the Authors
V. N. Leontiev
Belarusian State Technological University
Belarus
Belarus
Leontiev Viktor N. – Ph. D. (Chemistry), Associate Professor, Head of the Department
13a, Sverdlov Str., 220006, Minsk
O. I. Lazovskaya
Belarusian State Technological University
Belarus
Belarus
Lazovskaya Olesya I. – M. Sc. (Chemistry), Research Assistant
13a, Sverdlov Str., 220006, Minsk
A. R. Popenya
Belarusian State Technological University
Belarus
Belarus
Popenya Anna R. – Student
13a, Sverdlov Str., 220006, Minsk
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