Moringa oleifera leaf protein fractions and its emulsifying properties at different pHs

Teti Estiasih; Lailatul Isnaini; Fithri Choirun Nisa; Sugeng Heri Suseno; Lily Arsanti Lestari; Kgs Ahmadi; Ambar Fidyasari

doi:10.1016/j.afres.2026.102048

Moringa oleifera leaf protein fractions and its emulsifying properties at different pHs

Teti Estiasih^*
, Lailatul Isnaini
, Fithri Choirun Nisa
, Sugeng Heri Suseno
, Lily Arsanti Lestari
, Kgs Ahmadi
, Ambar Fidyasari

^*Corresponding author for this work

Faculty of Agricultural Technology

Research output: Contribution to journal › Article › peer-review

Abstract

Moringa oleifera (MO) leaf powder (MOLP) is one of the vegetable protein sources and its uses in food formulations are affected by the protein properties. This study aimed to evaluate the characteristics of MOLP protein and its function to stabilize emulsion at different pH of 4, 5, 6, 7, 8, and 9. The results showed that the MOLP protein fractions consisted of albumin (11.67%), globulin (0.83%), prolamin (2.05%) and glutelin (5.1%) with molecular weight (MW) ranging from 25 to 245 kDa. Increasing pH increased emulsifying activity index (EAI), emulsion stability index (ESI), and surface load of MOLP protein extract. Not all proteins were adsorbed at oil globule interface, the adsorbed proteins were dominated by low MW probably due to the dissociation of proteins caused by ionization at different pH. Changes in protein composition at the oil–water interface also influenced the emulsifying properties.

Original language	English
Article number	102048
Journal	Applied Food Research
Volume	6
Issue number	1
DOIs	https://doi.org/10.1016/j.afres.2026.102048
Publication status	Published - Jun 2026

Keywords

Adsorbed protein
Electrophoretic protein profile
Oil globule interface
Protein solubility

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10.1016/j.afres.2026.102048

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title = "Moringa oleifera leaf protein fractions and its emulsifying properties at different pHs",

abstract = "Moringa oleifera (MO) leaf powder (MOLP) is one of the vegetable protein sources and its uses in food formulations are affected by the protein properties. This study aimed to evaluate the characteristics of MOLP protein and its function to stabilize emulsion at different pH of 4, 5, 6, 7, 8, and 9. The results showed that the MOLP protein fractions consisted of albumin (11.67\%), globulin (0.83\%), prolamin (2.05\%) and glutelin (5.1\%) with molecular weight (MW) ranging from 25 to 245 kDa. Increasing pH increased emulsifying activity index (EAI), emulsion stability index (ESI), and surface load of MOLP protein extract. Not all proteins were adsorbed at oil globule interface, the adsorbed proteins were dominated by low MW probably due to the dissociation of proteins caused by ionization at different pH. Changes in protein composition at the oil–water interface also influenced the emulsifying properties.",

keywords = "Adsorbed protein, Electrophoretic protein profile, Oil globule interface, Protein solubility",

author = "Teti Estiasih and Lailatul Isnaini and Nisa, \{Fithri Choirun\} and Suseno, \{Sugeng Heri\} and Lestari, \{Lily Arsanti\} and Kgs Ahmadi and Ambar Fidyasari",

note = "Publisher Copyright: {\textcopyright} 2026 The Authors.",

year = "2026",

month = jun,

doi = "10.1016/j.afres.2026.102048",

language = "English",

volume = "6",

journal = "Applied Food Research",

issn = "2772-5022",

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TY - JOUR

T1 - Moringa oleifera leaf protein fractions and its emulsifying properties at different pHs

AU - Estiasih, Teti

AU - Isnaini, Lailatul

AU - Nisa, Fithri Choirun

AU - Suseno, Sugeng Heri

AU - Lestari, Lily Arsanti

AU - Ahmadi, Kgs

AU - Fidyasari, Ambar

PY - 2026/6

Y1 - 2026/6

N2 - Moringa oleifera (MO) leaf powder (MOLP) is one of the vegetable protein sources and its uses in food formulations are affected by the protein properties. This study aimed to evaluate the characteristics of MOLP protein and its function to stabilize emulsion at different pH of 4, 5, 6, 7, 8, and 9. The results showed that the MOLP protein fractions consisted of albumin (11.67%), globulin (0.83%), prolamin (2.05%) and glutelin (5.1%) with molecular weight (MW) ranging from 25 to 245 kDa. Increasing pH increased emulsifying activity index (EAI), emulsion stability index (ESI), and surface load of MOLP protein extract. Not all proteins were adsorbed at oil globule interface, the adsorbed proteins were dominated by low MW probably due to the dissociation of proteins caused by ionization at different pH. Changes in protein composition at the oil–water interface also influenced the emulsifying properties.

AB - Moringa oleifera (MO) leaf powder (MOLP) is one of the vegetable protein sources and its uses in food formulations are affected by the protein properties. This study aimed to evaluate the characteristics of MOLP protein and its function to stabilize emulsion at different pH of 4, 5, 6, 7, 8, and 9. The results showed that the MOLP protein fractions consisted of albumin (11.67%), globulin (0.83%), prolamin (2.05%) and glutelin (5.1%) with molecular weight (MW) ranging from 25 to 245 kDa. Increasing pH increased emulsifying activity index (EAI), emulsion stability index (ESI), and surface load of MOLP protein extract. Not all proteins were adsorbed at oil globule interface, the adsorbed proteins were dominated by low MW probably due to the dissociation of proteins caused by ionization at different pH. Changes in protein composition at the oil–water interface also influenced the emulsifying properties.

KW - Adsorbed protein

KW - Electrophoretic protein profile

KW - Oil globule interface

KW - Protein solubility

UR - https://www.scopus.com/pages/publications/105037468507

U2 - 10.1016/j.afres.2026.102048

DO - 10.1016/j.afres.2026.102048

M3 - Article

AN - SCOPUS:105037468507

SN - 2772-5022

VL - 6

JO - Applied Food Research

JF - Applied Food Research

IS - 1

M1 - 102048

ER -

Moringa oleifera leaf protein fractions and its emulsifying properties at different pHs

Abstract

Keywords

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