Affiliation:
1. Institute of Solid State Chemistry and Mechanochemistry, Siberian Branch of the Russian Academy of Sciences
2. Novosibirsk State University
3. Novosibirsk State Technical University
4. Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of the Russian Academy of Sciences
5. OOO ‘Ampersend’
Abstract
A poor consumption of important nutrients triggered a public interest in functional foods that contain easy-to-digest proteins. The present research features fractionation, mechanical activation, and enzymatic hydrolysis of pea protein. According to modern chemical methods, the protein content in the original pea biomass was 24.3% and its molecular weight distribution (MWD) was 5–135 kDa. Fractionation, or protein displacement, resulted in four fractions of biopolymers with different chemical composition, i.e. a different content of protein and carbohydrate molecules. The paper introduces some data on the enzymatic transformations of the substrate. A set of experiments made it possible to define the optimal conditions for the mechanical activation of pea biomass with proteolytic enzymes. The enzymes were obtained from Protosubtilin G3x, a complex enzyme preparation. When the substrate and the enzymes were mechanically activated together, it produced mechanocomposite, an intermediate product with increased reactivity. It increased the specific surface area by 3.2 times and doubled the crystallinity of the substrate. As a result, the rate and yield of the subsequent enzymatic hydrolysis increased from 18% to 61%. The study determined the capacity of the substrate in relation to the enzyme preparation. Under optimal conditions, the pea hydrolysis destroyed protein molecules within two hours. After four hours of hydrolysis, no changes were detected. A polyacrylamide gel electrophoresis revealed non-hydrolysed protein molecules with MW ≈ 20 kDa. Presumably, they corresponded with legumin, which is resistant to neutral and alkaline proteases. The resulting hydrolysates were spray-dried to test their potential use as a food component. The product obtained by spray-drying had a monomodal distribution of particle sizes of spherical shape with adiameter of 5–20 μm.
Publisher
Kemerovo State University
Reference40 articles.
1. European Commission. Horizon 2020: Annual Monitoring Report. Publications Office of the European Union; 2015. DOI: https://doi.org/10.2777/32., European Commission. Horizon 2020: Annual Monitoring Report. Publications Office of the European Union; 2015. DOI: https://doi.org/10.2777/32.
2. Ulberth F, Maragkoudakis P, Czimbalmos A, Wollgast J, Rzychon M, Caldeira S, et al. Tomorrow’s healthy society. Research priorities for foods and diets: final report – Study. Luxemburg: Publications Office of the European Union; 2014. 116 p. DOI: https://doi.org/10.2788/1395., Ulberth F, Maragkoudakis P, Czimbalmos A, Wollgast J, Rzychon M, Caldeira S, et al. Tomorrow’s healthy society. Research priorities for foods and diets: final report – Study. Luxemburg: Publications Office of the European Union; 2014. 116 p. DOI: https://doi.org/10.2788/1395.
3. Bannikova AV, Evdokimov IA. The scientific and practical principles of creating products with increased protein content. Foods and Raw Materials. 2015;3(2):3–12. DOI: https://doi.org/10.12737/13114., Bannikova AV, Evdokimov IA. The scientific and practical principles of creating products with increased protein content. Foods and Raw Materials. 2015;3(2):3–12. DOI: https://doi.org/10.12737/13114.
4. Salvatore S, Vandenplas Y. Hydrolyzed Proteins in Allergy. In: Bhatia J, Shamir R, Vandenplas Y, editors. Protein in Neonatal and Infant Nutrition: Recent Updates. Basel: Nestec; 2016. pp. 11–27. DOI: https://doi.org/10.1159/000442699., Salvatore S, Vandenplas Y. Hydrolyzed Proteins in Allergy. In: Bhatia J, Shamir R, Vandenplas Y, editors. Protein in Neonatal and Infant Nutrition: Recent Updates. Basel: Nestec; 2016. pp. 11–27. DOI: https://doi.org/10.1159/000442699.
5. Barać M, Cabrilo S, Pešić M, Stanojević S, Pavlićević M, Maćej O, et al. Functional properties of pea (Pisum sativum, L.) protein isolates modified with chymosin. International Journal of Molecular Sciences. 2011;12(12):8372–8387. DOI: https://doi.org/10.3390/ijms12128372., Barać M, Cabrilo S, Pešić M, Stanojević S, Pavlićević M, Maćej O, et al. Functional properties of pea (Pisum sativum, L.) protein isolates modified with chymosin. International Journal of Molecular Sciences. 2011;12(12):8372–8387. DOI: https://doi.org/10.3390/ijms12128372.
Cited by
11 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献