TY - JOUR
T1 - Comparison of the physicochemical and functional properties of flour and protein isolate from moringa (Moringa oleifera Lam.) leaves
AU - Bocarando-Guzmán, M. D.
AU - Luna-Suárez, Silvia
AU - Hernández-Cázares, Aleida S.
AU - Herrera-Corredor, J. Andrés
AU - Hidalgo-Contreras, J. Valente
AU - Ríos-Corripio, M. A.
N1 - Publisher Copyright:
© 2022 M. D. Bocarando-Guzmán, Silvia Luna-Suárez, Aleida S. Hernández-Cázares, J. Andrés Herrera-Corredor, J. Valente Hidalgo-Contreras and M. A. Ríos-Corripio. Published with license by Taylor & Francis Group, LLC. © 2022, Published with license by Taylor & Francis Group, LLC. © 2022 M. D. Bocarando-Guzmán, Silvia Luna-Suárez, Aleida S. Hernández-Cázares, J. Andrés Herrera-Corredor, J. Valente Hidalgo-Contreras and M. A. Ríos-Corripio.
PY - 2022
Y1 - 2022
N2 - The physicochemical and functional properties of flour (MF) and a protein isolate (MPI) obtained from moring leaves were evaluated and compared. These properties were evaluated and compared with a commercial soybean protein isolate (SPI). MPI was obtained by alkaline solubilization at pH 11.5 and isoelectric precipitation at pH 4.5. The protein content of MPI was 75.8%, with a yield of 6.5% when obtained by lyophilization. Electrophoresis analysis confirmed the presence of proteins between 8 and 120 kDa, and FTIR analysis confirmed the yield of MPI and the decrease of non-protein constituents, such as carbohydrates. The MF showed good gelation properties [5 mL (100%) at 14% (w/v) flour]. MPI showed even better gelling properties (10% to 78%) than SPI and similar water and oil absorption capacities (WAC and OAC) (3 g g-1 and 1.5 g g-1 respectively) as SPI. The pH had a significant influence on these properties. It can be concluded that MPI is an important protein source and may be a viable alternative as a functional food ingredient comparable to SPI in some properties such as WAC, OAC, and emulsion stability at low pH.
AB - The physicochemical and functional properties of flour (MF) and a protein isolate (MPI) obtained from moring leaves were evaluated and compared. These properties were evaluated and compared with a commercial soybean protein isolate (SPI). MPI was obtained by alkaline solubilization at pH 11.5 and isoelectric precipitation at pH 4.5. The protein content of MPI was 75.8%, with a yield of 6.5% when obtained by lyophilization. Electrophoresis analysis confirmed the presence of proteins between 8 and 120 kDa, and FTIR analysis confirmed the yield of MPI and the decrease of non-protein constituents, such as carbohydrates. The MF showed good gelation properties [5 mL (100%) at 14% (w/v) flour]. MPI showed even better gelling properties (10% to 78%) than SPI and similar water and oil absorption capacities (WAC and OAC) (3 g g-1 and 1.5 g g-1 respectively) as SPI. The pH had a significant influence on these properties. It can be concluded that MPI is an important protein source and may be a viable alternative as a functional food ingredient comparable to SPI in some properties such as WAC, OAC, and emulsion stability at low pH.
KW - Moringa leaves
KW - alkaline solubilization and isoelectric precipitation
KW - functional properties
KW - protein isolate
UR - http://www.scopus.com/inward/record.url?scp=85128320421&partnerID=8YFLogxK
U2 - 10.1080/10942912.2022.2058533
DO - 10.1080/10942912.2022.2058533
M3 - Artículo
AN - SCOPUS:85128320421
SN - 1094-2912
VL - 25
SP - 733
EP - 747
JO - International Journal of Food Properties
JF - International Journal of Food Properties
IS - 1
ER -