Insight into the presence state and stability mechanism of oil in aqueous system during aqueous enzymatic extraction of peanut oil and protein simultaneously

This study aimed to examine the presence state and stability mechanism of oil in aqueous system (AS) during aqueous enzymatic method. The AS comprised oils in three states: free-state oil (FSO), emulsified-state oil (ESO), adsorbed-state oil (ASO). The contents of residual oil were the lowest in AS (9.07%), while those of ESO, ASO, and FSO were 5.88%, 1.62%, and 1.57%, respectively, under the following conditions: crushing pretreatment, 120 s; enzyme concentration, 1.5%; hydrolysis temperature and time, 50 °C and 1.5 h; pH, 7.0. Stability mechanism of oil in AS was elucidated by examining protein interfacial behaviour, secondary and spatial structure, intermolecular interactions. ASO was existed through the exposure of intramolecular hydrophobic groups in specific proteins. Protein aggregates with reduced interfacial tension and attenuated hydrogen bonds stabilised ESO by anchoring at the oil-water interfaces. Protein-induced viscosity modulation in AS maintained colloidal stability of small oil particles, facilitating the formation of FSO. • Oil in AS was lowest when extraction under enzyme 1.5%, 50 °C, 1.5 h, and pH 7.0. • Three state oils (FSO, ESO, ASO) were presented in aqueous phase systems (AS). • Hydrophobic sites of specific protein’s hydrophobic groups adsorbed oil to form ASO. • ESO existed by anchoring at interface of protein with interfacial tension and -H. • FSO existed by AS viscosity modulation induced by proteins.

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Publication Details

Journal
LWT
Published
2025-09-16
DOI
https://doi.org/10.1016/j.lwt.2025.118511
Primary Topic
Proteins in Food Systems
Type
article
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article

Insight into the presence state and stability mechanism of oil in aqueous system during aqueous enzymatic extraction of peanut oil and protein simultaneously

Tingwei Zhu, Fusheng Chen, Haoran Xiong, Xingfeng Guo et al.
LWT
Proteins in Food Systems
article

Insight into the presence state and stability mechanism of oil in aqueous system during aqueous enzymatic extraction of peanut oil and protein simultaneously

Tingwei Zhu, Fusheng Chen, Haoran Xiong, Xingfeng Guo, Zhong-Yi Lu, Qianqian Guo, Xinling Gan
article en

Abstract

This study aimed to examine the presence state and stability mechanism of oil in aqueous system (AS) during aqueous enzymatic method. The AS comprised oils in three states: free-state oil (FSO), emulsified-state oil (ESO), adsorbed-state oil (ASO). The contents of residual oil were the lowest in AS (9.07%), while those of ESO, ASO, and FSO were 5.88%, 1.62%, and 1.57%, respectively, under the following conditions: crushing pretreatment, 120 s; enzyme concentration, 1.5%; hydrolysis temperature and time, 50 °C and 1.5 h; pH, 7.0. Stability mechanism of oil in AS was elucidated by examining protein interfacial behaviour, secondary and spatial structure, intermolecular interactions. ASO was existed through the exposure of intramolecular hydrophobic groups in specific proteins. Protein aggregates with reduced interfacial tension and attenuated hydrogen bonds stabilised ESO by anchoring at the oil-water interfaces. Protein-induced viscosity modulation in AS maintained colloidal stability of small oil particles, facilitating the formation of FSO. • Oil in AS was lowest when extraction under enzyme 1.5%, 50 °C, 1.5 h, and pH 7.0. • Three state oils (FSO, ESO, ASO) were presented in aqueous phase systems (AS). • Hydrophobic sites of specific protein’s hydrophobic groups adsorbed oil to form ASO. • ESO existed by anchoring at interface of protein with interfacial tension and -H. • FSO existed by AS viscosity modulation induced by proteins.

LWTVol. 233
Henan University of Technology (CN), Henan Institute of Education (CN)
Openalex Percentile: Top 70%
Proteins in Food Systems
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Insight into the presence state and stability mechanism of oil in aqueous system during aqueous enzymatic extraction of peanut oil and protein simultaneously — Tingwei Zhu, Fusheng Chen, et al. · LWT (2025) | TGRS Research Map | TGRS