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Physical and chemical characterization and bioavailability evaluation in vivo of amaranth protein concentrate

Sidorova, Yuliya S., Petrov, Nikita A., Perova, Irina B., Kolobanov, Alexey I., Zorin, Sergey N.·2023·Foods
DOI 10.3390/foods12081728PMC PMC10137383
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Abstract

Special attention is being paid to the study of amaranth proteins. They are characterized by a high biological value that significantly exceeds those of grain crops. The production of protein concentrate from amaranth flour includes preliminary enzymatic hydrolysis, extraction of the resulting mixture, protein precipitation, microfiltration, and freeze-drying. In our study, the obtained amaranth protein concentrate was limited by valine, with an amino acid score of 74%. The true digestibility of the amaranth protein concentrate determined in vivo was 97.6 ± 0.3%, which was significantly lower than that of casein (99.3 ± 0.2%). The protein digestibility-corrected amino acid score value of the concentrate was 72.2%. The obtained concentrate was a rich source of selenium, copper, magnesium, manganese, and iron. Ferulic acid was the only polyphenolic compound found in the amaranth protein concentrate, but its content was significantly greater compared to the original flour. Saponins were not removed completely during the process of obtaining the amaranth protein concentrate. We identified 15 saponins in the concentrate, mainly of the bidesmoside type, the sapogenins of which are related derivatives of oleanolic acid. Thus, the developed amaranth protein concentrate can be used as an ingredient in functional food products, with a high biological value.

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  • In less purified seed extracts, native amaranthine is commonly described as a legumin-type hexamer (300-390 kDa), whereas flour extracts exhibit additional high-molecular-mass peaks attributed to loosely associated aggregates.

    “In less purified seed extracts, native amaranthine is commonly described as a legumin-type hexamer (300-390 kDa), whereas flour extracts exhibit additional high-molecular-mass peaks attributed to loosely associated aggregates”

    From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Sidorova et al., 2023

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Authors
Sidorova, Y. S., Petrov, N. A., Perova, I. B., Kolobanov, A. I., & Zorin, S. N.
Affiliations
Federal Research Centre of Nutrition and Biotechnology, 109240 Moscow, Russia
ORCID
Sidorova, Yuliya S.
Venue
Foods
Publisher
MDPI AG
Published
2023-04-21
Volume
12
Issue
8
Pages
1728
ISSN
2304-8158
DOI
10.3390/foods12081728
PMC
PMC10137383
Cited by
18
References
0
Language
en
Licence
creativecommons.org/licenses/by/4.0/ (vor)
Funders
Russian Science Foundation (21-76-10049)

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