The role of cysteine in the formation of domain structures of papain and legumin in peas, involved in limited proteolysis
https://doi.org/10.21285/2227-2925-2021-11-4-642-650
Abstract
The limited use of plant proteins for food is explained by their low bioavailability and poor digestibility by enzymes of the gastrointestinal tract. Partially reproduced enzymatic processes of limited proteolysis that occur during seed germination are used to modify and improve the edibility characteristics of seed proteins. The present work discusses the possibility of reducing the duration of seed germination processes by optimising the conditions and parameters of limited proteolysis. To optimise manufacturing high-quality final product, enzymes (additional to the natural enzymes in the seed) and proteolysis conditions (in this case, temperature), as well as added substances (hydrolysis activators), were selected. The influence of cysteine on the formation of domain structures of proteins (enzymes and globulins) was evaluated. The proposed expressions can be used to determine those fragments of protein molecules that form stable domains and become unstructured when exposed to enzymes. Optimal conditions for limited proteolysis were identified based on the physical mechanism of action of papain-like proteolytic enzymes on pea legumin LegA (3KSC, CAA10722). It is shown that the decomposition of protein secondary structures takes 6–8 times longer, since the formed hydrogen bonds limit the access of enzymes to the corresponding amino-acid residues. It is also demonstrated that the decomposition of hydrogen bonds, e.g. by preliminary heat treatment of proteins, will broaden the prospects for limited proteolysis.
Keywords
cysteine,
papain,
pea legumin,
domains,
unstructured region,
denaturation temperature,
limited proteolysis
Supporting agencies: This work was supported by the project 075-00316-20-01 (FZMMM-2020-0013, mnemonic code 0611-2020-013) from the Ministry of Science and Higher Education of the Russian Federation.
About the Authors
Yu. I. Matveev
N. M. Emanuel Institute of Biochemical Physics RAS
Russian Federation
Russian Federation
Yuri I. Matveev, Cand. Sci. (Physics and Mathematics), Senior Scientist
4, Kosygin St., Moscow, 117997
E. V. Averyanova
Biysk Technological Institute (branch) of the Altay State Technical University
Russian Federation
Russian Federation
Elena V. Averyanova, Cand. Sci. (Chemistry), Associate Professor, Department of Biotechnology
7, Hero of the Soviet Union Trofimov St., Biysk, 659305
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Review
For citations:
Matveev Yu.I., Averyanova E.V. The role of cysteine in the formation of domain structures of papain and legumin in peas, involved in limited proteolysis. Proceedings of Universities. Applied Chemistry and Biotechnology. 2021;11(4):642-650. (In Russ.) https://doi.org/10.21285/2227-2925-2021-11-4-642-650
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