Xingfa Ma, Mehdi Habibi, Jasper Landman, Leonard M.C. Sagis, Penghui Shen
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Subsequently, the oil-water interfacial properties, including the adsorption and rheological behavior in both small and large dilatational and shear deformations, and the emulsion stabilization properties of Rubisco were investigated. We found that acid precipitation-alkaline redispersion produced a Rubisco extract (RA) with extensive structural reassembling, compared to the one produced by ultrafiltration (RU), for which nativity was mostly retained. RA had two-fold higher surface hydrophobicity than RU, and this caused RA to adsorb faster to the oil-water interface and developed a stiffer solid-like interface (G<sub>i</sub>’ = 26 ± 3 mN/m) than RU (G<sub>i</sub>’ = 15 ± 2 mN/m), which was also more resistant to density changes in large dilatational deformations. Consequently, RA displayed higher emulsifying activity and emulsion stability to coalescence during bulk shear and storage. Additionally, structural reassembly resulted in a higher value of the zeta potential of RA, which made the emulsion more stable against flocculation, compared to RU. Our study demonstrates that structural reassembly might be a useful strategy to improve the behavior of plant proteins in oil-water interface and emulsion stabilization, and may stimulate the development of new plant protein-stabilized emulsion-based products.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"160 ","pages":"Article 110820"},"PeriodicalIF":11.0000,"publicationDate":"2024-11-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Rubisco at interfaces II: Structural reassembly enhances oil-water interface and emulsion stabilization\",\"authors\":\"Xingfa Ma, Mehdi Habibi, Jasper Landman, Leonard M.C. Sagis, Penghui Shen\",\"doi\":\"10.1016/j.foodhyd.2024.110820\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><div>Rubisco is the most abundant protein on earth and has gained extensive attentions as a novel food ingredient, such as an emulsifier. Extraction methods can significantly affect its molecular structures and consequently influence its oil-water interface and emulsion stabilization properties. This work aims to elucidate the role of the Rubisco molecular structure in stabilizing the oil-water interface and the multiphase system of emulsions. Ultrafiltration (mild) and acid precipitation-alkaline redispersion (extensive) were used to extract Rubisco from spinach leaves. Protein molecular properties were characterized by size exclusion chromatography (SEC), circular dichroism (CD), and fluorescence spectrometry. Subsequently, the oil-water interfacial properties, including the adsorption and rheological behavior in both small and large dilatational and shear deformations, and the emulsion stabilization properties of Rubisco were investigated. We found that acid precipitation-alkaline redispersion produced a Rubisco extract (RA) with extensive structural reassembling, compared to the one produced by ultrafiltration (RU), for which nativity was mostly retained. RA had two-fold higher surface hydrophobicity than RU, and this caused RA to adsorb faster to the oil-water interface and developed a stiffer solid-like interface (G<sub>i</sub>’ = 26 ± 3 mN/m) than RU (G<sub>i</sub>’ = 15 ± 2 mN/m), which was also more resistant to density changes in large dilatational deformations. Consequently, RA displayed higher emulsifying activity and emulsion stability to coalescence during bulk shear and storage. Additionally, structural reassembly resulted in a higher value of the zeta potential of RA, which made the emulsion more stable against flocculation, compared to RU. 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Rubisco at interfaces II: Structural reassembly enhances oil-water interface and emulsion stabilization
Rubisco is the most abundant protein on earth and has gained extensive attentions as a novel food ingredient, such as an emulsifier. Extraction methods can significantly affect its molecular structures and consequently influence its oil-water interface and emulsion stabilization properties. This work aims to elucidate the role of the Rubisco molecular structure in stabilizing the oil-water interface and the multiphase system of emulsions. Ultrafiltration (mild) and acid precipitation-alkaline redispersion (extensive) were used to extract Rubisco from spinach leaves. Protein molecular properties were characterized by size exclusion chromatography (SEC), circular dichroism (CD), and fluorescence spectrometry. Subsequently, the oil-water interfacial properties, including the adsorption and rheological behavior in both small and large dilatational and shear deformations, and the emulsion stabilization properties of Rubisco were investigated. We found that acid precipitation-alkaline redispersion produced a Rubisco extract (RA) with extensive structural reassembling, compared to the one produced by ultrafiltration (RU), for which nativity was mostly retained. RA had two-fold higher surface hydrophobicity than RU, and this caused RA to adsorb faster to the oil-water interface and developed a stiffer solid-like interface (Gi’ = 26 ± 3 mN/m) than RU (Gi’ = 15 ± 2 mN/m), which was also more resistant to density changes in large dilatational deformations. Consequently, RA displayed higher emulsifying activity and emulsion stability to coalescence during bulk shear and storage. Additionally, structural reassembly resulted in a higher value of the zeta potential of RA, which made the emulsion more stable against flocculation, compared to RU. Our study demonstrates that structural reassembly might be a useful strategy to improve the behavior of plant proteins in oil-water interface and emulsion stabilization, and may stimulate the development of new plant protein-stabilized emulsion-based products.
期刊介绍：
Food Hydrocolloids publishes original and innovative research focused on the characterization, functional properties, and applications of hydrocolloid materials used in food products. These hydrocolloids, defined as polysaccharides and proteins of commercial importance, are added to control aspects such as texture, stability, rheology, and sensory properties. The research's primary emphasis should be on the hydrocolloids themselves, with thorough descriptions of their source, nature, and physicochemical characteristics. Manuscripts are expected to clearly outline specific aims and objectives, include a fundamental discussion of research findings at the molecular level, and address the significance of the results. Studies on hydrocolloids in complex formulations should concentrate on their overall properties and mechanisms of action, while simple formulation development studies may not be considered for publication.
The main areas of interest are:
-Chemical and physicochemical characterisation
Thermal properties including glass transitions and conformational changes-
Rheological properties including viscosity, viscoelastic properties and gelation behaviour-
The influence on organoleptic properties-
Interfacial properties including stabilisation of dispersions, emulsions and foams-
Film forming properties with application to edible films and active packaging-
Encapsulation and controlled release of active compounds-
The influence on health including their role as dietary fibre-
Manipulation of hydrocolloid structure and functionality through chemical, biochemical and physical processes-
New hydrocolloids and hydrocolloid sources of commercial potential.
The Journal also publishes Review articles that provide an overview of the latest developments in topics of specific interest to researchers in this field of activity.
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