Some characteristics and functional properties of rapeseed protein prepared by ultrasonication, ultrafiltration and isoelectric precipitation

Dong, Xuyan; Guo, Lulu; Wei, Fang; Li, Jufang; Jiang, Mulan; Guangming, Li; Zhao, Yong; Chen, Hong

doi:10.1002/jsfa.4339

Cited by 81 publications

(46 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The decrease of particle size after ultrasonic pretreatments might be attributed to the cavitation and micro-streaming forces resulting from the ultrasound, which could disrupt noncovalent bonds between SPI molecules Hu et al (2013c). It also might be probably ascribed to the dissociation of macromolecular protein by ultrasound during heating (Dong et al 2011). This was in accord with the results of Jambrak et al (2009) who had already reported that ultrasonic pretreatments could change the particle size of proteins.…”

Section: Particle Sizesupporting

confidence: 79%

Effect of ultrasonic pretreatment on physicochemical characteristics and rheological properties of soy protein/sugar Maillard reaction products

et al. 2016

View full text Add to dashboard Cite

Maillard reaction products (MRPs) of soybean protein isolate (SPI) and sugars (glucose and maltose) were prepared by heating in the aqueous dispersion at 95°C for 15 min with ultrasonic pretreatment (ultrasonic power of 200 W) for 20 min. Effect of ultrasonic pretreatment on physicochemical characteristics and rheological properties of SPI/sugar MRPs was investigated. SPI/sugar MRPs prepared with ultrasonic pretreatment had higher degree of glycation (DG), lower browning and less compact tertiary conformation than that with non-ultrasonic pretreatment. Surface hydrophobicity (H 0 ), particle size and rheological properties were measured by fluorescence spectrophotometry, laser particle size analysis and dynamic oscillatory rheometry, respectively. Glycation reduced H 0 and particle size as well as weaken the gel network formed by the acidification of GDL. However, ultrasound increased H 0 and decreased particle size. This is desirable for the formation of acid-induced gel structure. The ultrasonic pretreatments reduced/eliminate the weakening effect of glycation on the gel network of SPI/sugar MRPs, and even improved the gel properties.

show abstract

Section: Particle Sizesupporting

confidence: 79%

Effect of ultrasonic pretreatment on physicochemical characteristics and rheological properties of soy protein/sugar Maillard reaction products

et al. 2016

View full text Add to dashboard Cite

show abstract

“…Studies of the hydrophilicity of rapeseed protein with a mixture of albumine and globuline have shown a great hydrophilicity compared to isolated albumine or globuline fraction [43]. Ultrafiltrated rapeseed protein has a better solubility than the protein which is acid-precipited [44]. This is supported by another examination of rapeseed protein, in which the isolates show a low solubility of 26 % at pH 9, in contrast to ultrafiltrated protein, which exhibit a solubility of 90 %.…”

Section: Protein Solubilitymentioning

confidence: 92%

“…Besides, the FC of the sample depends directly on its soluble protein fraction and the presence of other components (e.g., fiber). They also play a useful role by improving the surface viscosity and promoting the formation of a stable foam [44]. The FC and FS of the RPC-A show a different behavior in comparison to the unmodified protein samples since their FC is the highest of all protein samples, but their FS is the lowest.…”

Section: Foaming Capacitymentioning

confidence: 99%

See 1 more Smart Citation

Rapeseed Proteins for Paperboard Coating

Oviedo

Metz

Schulz

et al. 2014

Chemie Ingenieur Technik

View full text Add to dashboard Cite

Protein samples of rapeseed were prepared with different compositions as protein isolate, protein concentrate and acetylated protein concentrate. They showed functional properties which are consolidated in the coating. The manufactured protein samples were tested in a pilot-scale paperboard coating plant. The results indicated that the use of rapeseed proteins in the coating preparation is technically feasible and that the color and roughness of the coated paperboard show no negative effect on the quality. Industry printing experiments with this coated paperboard achieved the standard quality.

show abstract

“…Cruciferin and napin constitute roughly 70 % and 30 % of the total protein, respectively [10][11][12]. Cruciferin (12 S; molecular mass~240-300 kDa) is a saltsoluble globulin with a isoelectric point (pI) of~7.2 [13], and is comprised of high level of β-sheets (~50 %) and low level of α-helices (~10 %) [14].…”

Section: Introductionmentioning

confidence: 99%

Effect of pH and NaCl on the Emulsifying Properties of a Napin Protein Isolate

2014

View full text Add to dashboard Cite

The physicochemical and emulsifying properties of a napin protein isolate (NPI) were examined as a function of pH (3.0, 5.0 and 7.0) and NaCl content (0, 50 and 100 mM). Specifically, surface charge and hydrophobicity, interfacial tension (IT), solubility, and the emulsifying activity (EAI) and stability (ESI) indices were studied. Surface charge in the absence of NaCl ranged between~+10 mV to~−5 mV depending on the pH, becoming electrically neutral at pH 6.6. Overall, surface hydrophobicity decreased as the pH increased, whereas it increased as NaCl levels were raised. Solubility was high (~93-100 %) regardless of the conditions. NPI's ability to reduce IT was enhanced at higher pHs, however the effect of NaCl was pH dependent with the addition of NaCl enhancing and decreasing NPI's ability to reduce IT at pH 3.0 and 7.0, respectively. Overall, EAI values were similar in magnitude at pH 3.0 and 5.0, and lower at pH 7.0. The effect of NaCl on EAI was similar at pH 3.0 and 7.0, where EAI at the 0 mM and 100 mM NaCl level were similar in magnitude, but increased significantly at the addition of 50 mM NaCl. However, the EAI values at pH 5.0 decreased as the level of NaCl increased. Overall, the stability of NPIstabilized emulsions degraded rapidly and the addition of salt induced faster emulsion instability.

show abstract

Some characteristics and functional properties of rapeseed protein prepared by ultrasonication, ultrafiltration and isoelectric precipitation

Cited by 81 publications

References 27 publications

Effect of ultrasonic pretreatment on physicochemical characteristics and rheological properties of soy protein/sugar Maillard reaction products

Effect of ultrasonic pretreatment on physicochemical characteristics and rheological properties of soy protein/sugar Maillard reaction products

Rapeseed Proteins for Paperboard Coating

Effect of pH and NaCl on the Emulsifying Properties of a Napin Protein Isolate

Contact Info

Product

Resources

About