Research output: Contribution to journal › Article › peer-review
Mechanically activated hydrolysis of plant-derived proteins in food industry. / Gavrilova, Karina V.; Bychkov, Aleksey L.; Bychkova, Elena S. et al.
In: Foods and Raw Materials, Vol. 7, No. 2, 01.01.2019, p. 255-263.Research output: Contribution to journal › Article › peer-review
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TY - JOUR
T1 - Mechanically activated hydrolysis of plant-derived proteins in food industry
AU - Gavrilova, Karina V.
AU - Bychkov, Aleksey L.
AU - Bychkova, Elena S.
AU - Akimenko, Zoya A.
AU - Chernonosov, Aleksandr A.
AU - Kalambet, Yurii A.
AU - Lomovskii, Oleg I.
N1 - Publisher Copyright: © 2019, Gavrilova et al.
PY - 2019/1/1
Y1 - 2019/1/1
N2 - 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 a diameter of 5-20 μm.
AB - 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 a diameter of 5-20 μm.
KW - Amino acids
KW - Destruction of protein molecules
KW - Enzymatic hydrolysis
KW - Mechanochemical activation
KW - Mechanochemistry
KW - Mechanocomposite
KW - Plant materials
KW - Polypeptides
KW - Spray-drying
KW - LIGNOCELLULOSIC BIOMASS
KW - plant materials
KW - amino acids
KW - destruction of protein molecules
KW - mechanocomposite
KW - enzymatic hydrolysis
KW - PEA
KW - polypeptides
KW - FUNCTIONAL-PROPERTIES
KW - EXTRACTION
KW - mechanochemical activation
KW - spray-drying
UR - http://www.scopus.com/inward/record.url?scp=85072988568&partnerID=8YFLogxK
U2 - 10.21603/2308-4057-2019-2-255-263
DO - 10.21603/2308-4057-2019-2-255-263
M3 - Article
AN - SCOPUS:85072988568
VL - 7
SP - 255
EP - 263
JO - Foods and Raw Materials
JF - Foods and Raw Materials
SN - 2308-4057
IS - 2
ER -
ID: 21861963