Solubilization of proteins in extracted oil bodies by SDS: A simple and efficient protein sample preparation method for Tricine–SDS–PAGE

Ying, Yusang; Zhao, Luping; Kong, Lingzhi; Kong, Xiangzhen; Hua, Yufei; Chen, Yeming

doi:10.1016/j.foodchem.2015.02.088

Cited by 31 publications

(20 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…As shown in Figure , the extraction rate of CFP was lower at pH 5.0, however, it was higher at pH 3.0 and 11.0. pH 11.0 was used for the preparation of CFP, using the isoelectric precipitation method described by Ying et al (). The protein power contained 77.89% ± 0.23% of protein, 3.68% ± 0.09% of sugar, 3.89% ± 0.12% of lipid, 7.66% ± 0.38% of ash, and 5.38% ± 0.06% of moisture.…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Identification and analysis of bioactive peptides from scallops (Chlamys farreri ) protein by simulated gastrointestinal digestion

et al. 2018

J Food Process Preserv

View full text Add to dashboard Cite

In this study, the hydrolysates of scallops (Chlamys farreri) protein were prepared by in vitro simulated gastrointestinal digestion. Antioxidant peptides, VPSIDDQEELM, DAQEKLE, EELDNALN, VPSIDDQEELM, DAQEKLE, EELDNALN, VPSIDDQEELM and VPSIDDQEELM, were identified by ultra performance liquid chromatography system coupled to a Synapt Mass Quadrupole Time‐of‐Flight Mass Spectrometer (UPLC‐Q‐TOF‐MS). The antioxidant activities of the CFP hydrolysates, i.e., reducing powers, linoleic acid peroxidation inhibition activity and 2, 2‐dipheny l‐1‐picrylhydrazyl (DPPH) free radical scavenging activities, were tested. The antioxidant activities (54.44% ± 0.02%), reducing power (0.250 ± 0.02) and DPPH free radical scavenging activities of the hydrolysates shows higher than the same concentration of protein solution. This research provided a theoretical and practical data for the application of the bioactive peptides form CFP. Practical applications In this research, what we focused on is the qualitative of peptides from the digestive solutions. It makes more sense to discuss about the information of the special analogues, sequence and activity of peptides from hydrolysis fragment after simulated gastrointestinal digestion of CFP. These peptides which have hydrophobic residues at the C‐termini contribute to the antioxidant activity of the peptides. Comparing the antioxidant activities of the same concentration of CFP solution and in vitro gastric and gastro duodenal digestion hydrolysates, the hydrolysates of the digestion had higher reducing powers, linoleic acid peroxidation inhibition activity, and DPPH free radical scavenging activities. It could be speculated that both the peptides at approximately low‐molecular‐mass peptides (10–15 kDa) were contributing to the antioxidant activities of the hydrolysates. After the target peptides were determined, the quantitative of peptides may be more meaningful. Quantitative calculation of the digestion will be clarified in future work.

show abstract

Section: Resultsmentioning

confidence: 99%

“…After fixing, gel was stained with 0.025% (w/v) Coomassie Blue G‐250 in 10% (v/v) acetic acid for 2 hr, and destained by 10% (v/v) acetic acid. The band intensities on gel were analyzed by Bio‐Rad Image Lab Software (Ying, Zhao, & Kong, ).…”

Section: Methodsmentioning

confidence: 99%

Identification and analysis of bioactive peptides from scallops (Chlamys farreri ) protein by simulated gastrointestinal digestion

et al. 2018

J Food Process Preserv

View full text Add to dashboard Cite

show abstract

“…A simple and efficient protein sample preparation method was used in electrophoresis (Ying et al., 2015). OB suspension treated by different inorganic salts was blended for 2 min with SDS buffer at an SDS/protein mass ratio of 1.52:1.…”

Section: Methodsmentioning

confidence: 99%

Combination of Alcalase 2.4 L and CaCl₂ for aqueous extraction of peanut oil

Zhou

Chen

Liu

et al. 2020

Journal of Food Science

View full text Add to dashboard Cite

The combined application of CaCl2 and Alcalase 2.4 L to the aqueous extraction process of peanuts was evaluated as a method to destabilize the oil body (OB) emulsion and improve the oil yield. After adding 5 mM CaCl2, the oil yield was reached to 92.0% which was similar with that obtained using Alcalase 2.4 L alone, and the required enzyme loading was decreased by approximately 60 times. In addition, the demulsification mechanism during aqueous extraction process was also investigated. Particle size and zeta‐potential measurements indicated that the stability of the peanut OB emulsion dramatically decreased when CaCl2 was added. Under these conditions, the demulsification of Alcalase 2.4 L performed was more efficiently. SDS–PAGE results showed that adding CaCl2 changed the subunit structure of the peanut OB interface proteins and promoted the cross‐linking among the arachin Ara h3 isoforms, resulting in unstable emulsions.

show abstract

“…HCl 12 M at 110 for 22 h in a hydrolysis tube. The amino acid content was determined according to Ying and others using High-performance liquid chromatography Waters 2695, with Waters amino acid analysis package, Waters, America 16 . Further, the overall amino acid content was utilized to estimate protein concentrations in each sample.…”

Section: Determination Of Protein Concentrations Through Ami-mentioning

confidence: 99%

Effect of Physiochemical Factors and Peanut Varieties on the Charge Stability of Oil Bodies Extracted by Aqueous Method

2019

View full text Add to dashboard Cite

Solubilization of proteins in extracted oil bodies by SDS: A simple and efficient protein sample preparation method for Tricine–SDS–PAGE

Cited by 31 publications

References 29 publications

Identification and analysis of bioactive peptides from scallops (Chlamys farreri ) protein by simulated gastrointestinal digestion

Identification and analysis of bioactive peptides from scallops (Chlamys farreri ) protein by simulated gastrointestinal digestion

Combination of Alcalase 2.4 L and CaCl₂ for aqueous extraction of peanut oil

Effect of Physiochemical Factors and Peanut Varieties on the Charge Stability of Oil Bodies Extracted by Aqueous Method

Contact Info

Product

Resources

About

Solubilization of proteins in extracted oil bodies by SDS: A simple and efficient protein sample preparation method for Tricine–SDS–PAGE

Cited by 31 publications

References 29 publications

Identification and analysis of bioactive peptides from scallops (Chlamys farreri ) protein by simulated gastrointestinal digestion

Identification and analysis of bioactive peptides from scallops (Chlamys farreri ) protein by simulated gastrointestinal digestion

Combination of Alcalase 2.4 L and CaCl2 for aqueous extraction of peanut oil

Effect of Physiochemical Factors and Peanut Varieties on the Charge Stability of Oil Bodies Extracted by Aqueous Method

Contact Info

Product

Resources

About

Combination of Alcalase 2.4 L and CaCl₂ for aqueous extraction of peanut oil