Structure and functional characteristics of rapeseed protein isolate-dextran conjugates

Qu, Wenjuan; Zhang, Xinxin; Han, Xiao; Wang, Zhiping; He, Ronghai; Ma, Haile

doi:10.1016/j.foodhyd.2018.03.039

Cited by 138 publications

(43 citation statements)

References 43 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This might be attributed to the unfolding of protein structure by the high level of acylation that led to the exposure of reactive amino acids. It was worth noting that the change of the spatial structure of protein likely resulted in the exposure of other buried amino acids, 15 which was conrmed by the increased content of Asp, Tyr and Phe shown in Table 1 in the RPI3 with high level of acylation degree.…”

Section: Amino Acid Composition Analysismentioning

confidence: 99%

Effects of acylation and glycation treatments on physicochemical and gelation properties of rapeseed protein isolate

Wang

Zhang

et al. 2018

RSC Adv.

View full text Add to dashboard Cite

show abstract

Section: Amino Acid Composition Analysismentioning

confidence: 99%

Effects of acylation and glycation treatments on physicochemical and gelation properties of rapeseed protein isolate

Wang

Zhang

et al. 2018

RSC Adv.

View full text Add to dashboard Cite

show abstract

“…In recent years, research (He et al, ; Partanen et al, ; Qu et al, ) about RPI mainly focusing on the physicochemical properties, functional qualities, and bioactive properties have been carried out. For example, the bioactive peptide obtained by enzymatic hydrolysis from RPI is a kind of processed product, however, large amounts of polypeptides are wasted during the separation and purification processes.…”

Section: Introductionmentioning

confidence: 99%

Effects of Succinylation on the Physicochemical Properties and Structural Characteristics of Edible Rapeseed Protein Isolate Films

Dai

et al. 2019

J Americ Oil Chem Soc

View full text Add to dashboard Cite

This study described the manufacture and characterization of different levels of succinic anhydride (0-15%, w/w) on rapeseed protein isolate (RPI) films. Mechanical, barrier, optical, surface, microstructure, and thermal properties were investigated. Results showed that 5% succinylated rapeseed protein isolate (SRPI) film revealed the overall optimal properties. The mechanical and barrier properties of 5% SRPI film were enhanced significantly compared to the RPI film. The water vapor permeability values of RPI and 5% SRPI films were 0.77 and 0.32 g mm/[hour m 2 kPa], respectively. Succinylation improved the color of RPI. The contact angle of 5% SRPI film was 108.68 and was the most hydrophobic combination. Moreover, scanning electron microscopy images revealed that 5% SRPI showed a dense, homogenous, and smooth microstructure. Thermogravimetric analysis results verified a low level of succinylation strengthened the thermal resistance of SRPI films. The content of β-sheet was almost half of all secondary structures after succinylation, which was supported by analyses of Fourier transform infrared spectroscopy. Results demonstrated that succinylation could be employed to improve the properties of rapeseed protein and SRPI films have great potential to be used as edible films.

show abstract

“…CD is considered to be a sensitive indicator of protein conformational changes at the molecular level and it can reflect the peptide conformation of the protein backbone (Qu et al., 2018). A negative peak near 208 nm usually reflects a change in the α‐helical structure, and a change in the β‐sheet structure is usually reflected at 217 nm (Shi et al., 2010).…”

Section: Resultsmentioning

confidence: 99%

Effect of reaction temperature on the protein structure and the ability to encapsulate β‐carotene of WPI‐dextran conjugates

Chu

Kang

Zhao

et al. 2020

Journal of Food Science

View full text Add to dashboard Cite

In this paper, we studied the effect of glycosylation reaction on the molecular structure and functional properties of whey protein isolate (WPI), and studied the effect of reaction temperature (50 to 90 °C) on the molecular structure and functional properties of WPI–dextran conjugates (WPI‐D). The results of the extent of glycation (EG) and sodium dodecyl sulfate–polyacrylamide gel electrophoresis confirmed the formation of WPI‐D. Circular dichroism (CD), Fourier transform infrared spectrum, and fluorescence spectroscopy indicated that the molecular structure of WPI was changed after glycosylation—the β‐sheet content was decreased and the tryptophan content was increased. The emulsifying properties and the ability to encapsulate β‐carotene of WPI‐D were improved compared with WPI (P < 0.05). When the reaction temperature was 70 and 80 °C, the EG and the ability to encapsulate β‐carotene of WPI‐D were better (P < 0.05), which was related to protein unfolding. However, due to the polymerization between the WPI molecules, the emulsion activity index of WPI‐D and the ability to encapsulate β‐carotene were lowered at 90 °C (P < 0.05). Therefore, the glycosylation reaction can change the molecular structure and functional properties of WPI; the emulsifying properties and the ability to encapsulate β‐carotene of WPI‐D can be changed by controlling the reaction temperature of glycosylation. Practical Application The glycosylation reaction can change the molecular structure and functional properties of Whey protein isolate; the emulsifying properties and the ability to encapsulate β‐carotene of WPI‐dextran conjugates can be changed by controlling the reaction temperature of glycosylation.

show abstract

Structure and functional characteristics of rapeseed protein isolate-dextran conjugates

Cited by 138 publications

References 43 publications

Effects of acylation and glycation treatments on physicochemical and gelation properties of rapeseed protein isolate

Effects of acylation and glycation treatments on physicochemical and gelation properties of rapeseed protein isolate

Effects of Succinylation on the Physicochemical Properties and Structural Characteristics of Edible Rapeseed Protein Isolate Films

Effect of reaction temperature on the protein structure and the ability to encapsulate β‐carotene of WPI‐dextran conjugates

Contact Info

Product

Resources

About