Dissecting the Disulfide Linkage of the N-Terminal Domain of HMW 1Dx5 and Its Contributions to Dough Functionality

Wang, Jing Jing; Liu, Guang; Huang, Yanbo; Qing-jun, Zeng; Hou, Yi; Li, Lin; Ou, Shiyi; Zhang, Min; Hu, Song-Qing

doi:10.1021/acs.jafc.7b02449

Cited by 22 publications

(14 citation statements)

References 39 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Similarly, as was found for the LMW-GS in the present study, the crosslinking sites of the HMW-GS have been reported to be located in hydrophilic regions of the proteins [79,80]. Moreover, recent investigations have indicted surface hydrophobicity in the N-terminal domains of HMW-GS as an important factor for interdisulfide bond formation [81].…”

Section: Discussionsupporting

confidence: 88%

Glutenin and Gliadin, a Piece in the Puzzle of their Structural Properties in the Cell Described through Monte Carlo Simulations

et al. 2020

View full text Add to dashboard Cite

Gluten protein crosslinking is a predetermined process where specific intra- and intermolecular disulfide bonds differ depending on the protein and cysteine motif. In this article, all-atom Monte Carlo simulations were used to understand the formation of disulfide bonds in gliadins and low molecular weight glutenin subunits (LMW-GS). The two intrinsically disordered proteins appeared to contain mostly turns and loops and showed “self-avoiding walk” behavior in water. Cysteine residues involved in intramolecular disulfide bonds were located next to hydrophobic peptide sections in the primary sequence. Hydrophobicity of neighboring peptide sections, synthesis chronology, and amino acid chain flexibility were identified as important factors in securing the specificity of intramolecular disulfide bonds formed directly after synthesis. The two LMW-GS cysteine residues that form intermolecular disulfide bonds were positioned next to peptide sections of lower hydrophobicity, and these cysteine residues are more exposed to the cytosolic conditions, which influence the crosslinking behavior. In addition, coarse-grained Monte Carlo simulations revealed that the protein folding is independent of ionic strength. The potential molecular behavior associated with disulfide bonds, as reported here, increases the biological understanding of seed storage protein function and provides opportunities to tailor their functional properties for different applications.

show abstract

Section: Discussionsupporting

confidence: 88%

Glutenin and Gliadin, a Piece in the Puzzle of their Structural Properties in the Cell Described through Monte Carlo Simulations

et al. 2020

View full text Add to dashboard Cite

show abstract

“…The high β ‐sheet conformation indicated stronger interactions of peptide molecules . Moreover, the higher content of ordered structures (>75%) maintained the conformation stability of the target peptides …”

Section: Resultsmentioning

confidence: 99%

Recovery and identification bioactive peptides from protein isolate of Spirulina platensis and their in vitro effectiveness against oxidative stress‐induced erythrocyte hemolysis

et al. 2020

Self Cite

View full text Add to dashboard Cite

BACKGROUND Spirulina platensis is recognized as one of the most nutritious foods, containing a high protein content of up to 70%. Meanwhile, he interest in using natural protein resources to develop bioactive peptides is steadily increasing. Therefore, this study released the bioactive peptides from S. platensis by enzymatic hydrolysis using pepsin (1:3000 U g−1), and their amino acid sequences were determined by de novo sequencing. On this basis, the antioxidant activities of synthesized bioactive peptides were comprehensively evaluated by 2,2′‐azinobis‐3‐ethylbenzothiazolin‐6‐sulfonic acid assay, 1,1‐diphenyl‐2‐picryhydrazyl assay, and cell hemolysis assay induced by 2,2′‐azobis‐(2‐amidino‐propane) dihydrochloride (AAPH). RESULTS The degree of hydrolysis and recovery percentage of pepsin hydrolysis were 172 and 825 g kg–1 respectively, and FFEFF (P1: m/z 736.4, 8%), EYFDALA (P2: m/z 828.4, relative intensity 18.5%), and VTAPAASVAL (P3: m/z 899.5, relative intensity 17.3%) were purified and identified. P2 possessed an excellent radical scavenging activity compared with P1, P3, and vitamin C, which was contributed to by its high β‐sheet conformation and specific amino acid compositions. Moreover, P2 significantly attenuated AAPH‐induced oxidative hemolysis of erythrocytes and protected the erythrocytes, because it reduced the formation of malondialdehyde and increased the enzyme activities of superoxide dismutase, catalase, and glutathione peroxidase in erythrocytes. CONCLUSION This study provided insights into the potential antioxidant function of the synthesized peptides originated from the bioactive peptides of S. platensis proteins, which would contribute to the development of natural antioxidant from new protein resources. © 2020 Society of Chemical Industry

show abstract

“…An especially significant decrease was observed at 70 °C, which was consistent with the results of Francesco et al [ 22 ]. The increase in α-helix meant the formation of ordered and compact protein spatial structure [ 23 ] by enhancing protein folding [ 24 ]. The increase in intermolecular β-sheets further demonstrated that protein polymerized during heating of wheat flour.…”

Section: Discussionmentioning

confidence: 99%

Investigation on the Molecular and Physicochemical Changes of Protein and Starch of Wheat Flour during Heating

Tao

Wang

Zhou

et al. 2021

Foods

View full text Add to dashboard Cite

The behaviors of starch and protein in wheat flour during heating were investigated, and the molecular changes of starch and protein and their effects on the textural characteristics were assessed. The results showed that with the increased temperature, soluble protein aggregated to insoluble high-molecular-weight protein polymers when the heating temperature exceeded 70 °C, and the aggregation of protein was mainly caused by covalent bonds of disulfide (SS) bonds. Hydrophobic interaction was the main noncovalent bond that participated in the formation of protein aggregates. The major change in the secondary structure during heating was a pronounced transition towards β-sheet-like structures. Considerable disruption of ordered structures of starch occurred at 70 °C, and starch was fully gelatinized at 80 °C. Typical starch pasting profiles of cooked flour were observed when the temperature was below 70 °C, and heat treatment decreased the pasting viscosity of the cooked flour from control to 80 °C, whereas the viscosity of the wheat flour increased in heating treatment at 90, 95 and 100 °C. The intense protein-starch interaction during heating affected the textural characteristic of flour gelation, which showed higher strength at 90, 95 and 100 °C. This study may provide a basis for improving wheat flour processing conditions and could lead to the production of new wheat products.

show abstract

Dissecting the Disulfide Linkage of the N-Terminal Domain of HMW 1Dx5 and Its Contributions to Dough Functionality

Cited by 22 publications

References 39 publications

Glutenin and Gliadin, a Piece in the Puzzle of their Structural Properties in the Cell Described through Monte Carlo Simulations

Glutenin and Gliadin, a Piece in the Puzzle of their Structural Properties in the Cell Described through Monte Carlo Simulations

Recovery and identification bioactive peptides from protein isolate of Spirulina platensis and their in vitro effectiveness against oxidative stress‐induced erythrocyte hemolysis

Investigation on the Molecular and Physicochemical Changes of Protein and Starch of Wheat Flour during Heating

Contact Info

Product

Resources

About