Comparison of functional properties and secondary structures of defatted wheat germ proteins separated by reverse micelles and alkaline extraction and isoelectric precipitation

Zhu, Ke‐Xue; Sun, Xiaohong; Chen, Zhicheng; Peng, Wei; Qian, Haifeng; Zhou, Hui‐Ming

doi:10.1016/j.foodchem.2010.05.081

Cited by 94 publications

(69 citation statements)

References 30 publications

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“…Moreover, the differences in WAC between Isolate-A and Isolate-B can be attributed to the denatured proteins which can bind more water through exposure of hydrophilic groups (Davis et al 2007). WAC value of DWF (3.57 gg −1 ) was higher than 3.55 gg −1 of commercial soy protein isolate (SPI) reported by Ke-Xue Zhu et al (2010). High WAC of DWF makes it a potential ingredient in meat, bread, and cakes industries.…”

Section: Resultsmentioning

confidence: 69%

Chemical composition, molecular weight distribution, secondary structure and effect of NaCl on functional properties of walnut (Juglans regia L) protein isolates and concentrates

Mao

Hua

2012

J Food Sci Technol

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Chemical composition, molecular weight distribution, secondary structure and effect of sodium chloride concentration on functional properties of walnut protein isolates, concentrates and defatted walnut flour were study. Compared with walnut protein concentrates (75.6%) and defatted walnut flour (52.5%), walnut protein isolates contain a relatively high amount of protein (90.5%). The yield of walnut protein isolates and concentrates was 43.2% and 76.6%, respectively. In molecular weight distribution study, Walnut protein isolates showed one peak with molecular weight of 106.33 KDa (100%) and walnut protein concentrates showed four peaks with molecular weight of 16,725 KDa (0.8%),104.943 KDa(63.9%), 7.3 KDa (11.4%), 2.6 KDa (23.9%). The secondary structure of walnut protein isolates was similar to that of walnut protein concentrates, but was differ from that of defatted walnut flour. The addition of sodium chloride (0~1 M) could improve the functionality of walnut protein concentrates, isolates and defatted walnut flour. The maximum solubility, water absorption capacity, emulsifying properties and foaming properties of walnut protein isolates, concentrates and defatted walnut flour were at sodium chloride solutions of 1.0 M, 0.6 M, 0.4 M, 0.6 M, respectively. The solubility of walnut protein concentrates (32.5%) in distilled water with 0 M sodium chloride was lower than that of walnut protein isolates (35.2%). The maximum solubility of walnut protein isolates, concentrates and defatted walnut flour in solution were 36.8%, 33.7% and 9.6% at 1.0 M sodium chloride solutions, respectively. As compared with other vegetable proteins, walnut protein isolates and concentrates exhibited better emulsifying properties and foam stability.

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Section: Resultsmentioning

confidence: 69%

Chemical composition, molecular weight distribution, secondary structure and effect of NaCl on functional properties of walnut (Juglans regia L) protein isolates and concentrates

Mao

Hua

2012

J Food Sci Technol

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“…The results were in agreement with Agboola et al (2005), who found that low foam capacity for rice glutelins can be directly linked to poor solubility and lack of flexibility due to the high content of disulphide bonds. The foam stability values of REP and RDP were markedly higher than that of egg white protein (<60%) (Zhu et al, 2010) at 20 min, without any significant differences in foam stability between REP and RDP (p > 0.05).…”

Section: Foam Capacity and Foam Stabilitymentioning

confidence: 75%

“…REP and RDP had foam capacity values of 115.9% and 118.8%, respectively. No significant differences in foam capacities among REP, RDP and egg white protein (at 117% (Zhu et al, 2010) and used as a standard for foaming comparisons among proteins) were observed (p > 0.05). RDP having a higher foam capacity than that of REP (p > 0.05) was consistent with protein solubility at pH 7.0, as an important prerequisite for foam formation; that is those proteins should solubilize in the aqueous phase and rapidly unfold to form a cohesive layer of protein around gas/air droplets (Tang et al, 2003).…”

Section: Foam Capacity and Foam Stabilitymentioning

confidence: 91%

“…Our preliminary experiment indicated that the solubility of rice dreg protein was superior to the native rice endosperm protein in water at a neutral condition. The functionalities of protein are essentially determined by their physicochemical and conformational properties (Zhu et al, 2010). However, little information is available on the changes of functional properties and secondary structures of longgrain indica rice endosperm proteins before and after food processing.…”

Section: Introductionmentioning

confidence: 99%

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Comparison of functional and structural properties of native and industrial process-modified proteins from long-grain indica rice

Zhao

Selomulya

Xiong

et al. 2012

Journal of Cereal Science

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“…La CAA de API (0,8 mL/g) estuvo por debajo de lo reportado para el aislado comercial de soya, el cual presenta un valor más de cuatro veces mayor (3,55 mL/g) (Zhu et al, 2010).…”

Section: Capacidad De Absorción De Aceite Y Aguaunclassified

Propiedades tecnofuncionales y biológicas de harina, aislado y fracciones proteicas mayoritarias de semillas deInga paterno

Sánchez-Mendoza

Ruíz-Ruíz

Dávila-Ortíz

et al. 2017

CyTA - Journal of Food

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RESUMENSe evaluaron las propiedades tecnofuncionales y biológicas de harina, aislado proteico, albúminas y globulinas de semillas de Inga paterno, incluyendo solubilidad proteica, capacidad de absorción de agua y aceite, capacidad espumante y emulsionante, poder reductor de hierro (FRAP) y capacidad inhibitoria de la Enzima Convertidora de Angiotensina (ECA-I). Los resultados muestran que las globulinas presentan mayor solubilidad proteica, capacidad emulsionante y de absorción de aceite; mientras que las albúminas mejor capacidad de absorción de agua, mientras que el aislado proteico mostro mejor capacidad espumante. Estas propiedades fueron dependientes del pH. El FRAP fue de entre 3 y 30% de (0,1-0,3 mg proteína/mL) en todas las muestras, mientras que la actividad de inhibitoria de la ECA-I (0,3 mg proteína/mL) se presentó en harina y aislado proteico, existiendo diferencia estadísticamente significativa (p < 0,05) debido al tratamiento en ambos ensayos. La incorporación de proteínas de semillas de Inga paterno a formulaciones alimenticias podría mejorar sus propiedades tecnofuncionales y su actividad biológica.Techno-functional and biological properties of flour, isolated and majority protein fractions from seeds of Inga paterno ABSTRACT Inga paterno seeds techno-functional and biological properties of flour, protein isolate, albumins and globulins were evaluated. Protein solubility, water and oil absorption capacity, foaming and emulsifying capacity and stability, FRAP and inhibitory capacity ACE-I were including. Globulins had the highest protein solubility, emulsifying capacity and fat absorption capacity; while albumins showed better water absorption capacity. Protein isolate had higher values at foaming capacity. Techno-functional properties were pH dependent. The tested samples showed values between 3 and 30% of FRAP (0.1-0.3 mg protein/mL). Furthermore, flour and protein isolate showed inhibitory activity of ACE-I (0.3 mg protein/mL). Incorporation of Inga paterno proteins seed to food formulations could improve its techno-functional properties and biological activity. ARTICLE HISTORY

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Comparison of functional properties and secondary structures of defatted wheat germ proteins separated by reverse micelles and alkaline extraction and isoelectric precipitation

Cited by 94 publications

References 30 publications

Chemical composition, molecular weight distribution, secondary structure and effect of NaCl on functional properties of walnut (Juglans regia L) protein isolates and concentrates

Chemical composition, molecular weight distribution, secondary structure and effect of NaCl on functional properties of walnut (Juglans regia L) protein isolates and concentrates

Comparison of functional and structural properties of native and industrial process-modified proteins from long-grain indica rice

Propiedades tecnofuncionales y biológicas de harina, aislado y fracciones proteicas mayoritarias de semillas deInga paterno

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