Studies on the interactional characterization of preheated silkworm pupae protein (SPP) with anthocyanins (C3G) and their effect on anthocyanin stability

Attaribo, Thomas; Jiang, Xizhi; Huang, Gaiqun; Zhang, Bei; Xin, Xiangdong; Zhang, Yueyue; Zhang, Ning; Gui, Zhongzheng

doi:10.1016/j.foodchem.2020.126904

Cited by 61 publications

(28 citation statements)

References 48 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The increased stability is often reported to be related to the affinity, even though further work is still needed to verify the protective mechanism. Several studies tested also the effect of preheating for the formation of the complexes (Attaribo et al., 2020; Chen et al., 2019; Chung, Rojanasasithara, Mutilangi, & McClements, 2015; He et al., 2016; Shpigelman et al., 2010), in some cases showing that preheating enhances interactions (Shpigelman et al., 2010) and can improve stability (beyond the effect of the nonpreheated protein), yet an optimal preheating temperature was also reported to exist (Attaribo et al., 2020). Although noncovalent polyphenol–protein interactions are well known to be polyphenol structure dependent, less is known on how the protein structure and amino acid sequence affect the stability (except for the improved interaction of preheated proteins), yet a difference between the impact of different proteins was reported (Wang & Zhao, 2016).…”

Section: Effects Of Polyphenol–protein Interaction On the Stabilitymentioning

confidence: 99%

Available technologies on improving the stability of polyphenols in food processing

et al. 2021

View full text Add to dashboard Cite

Polyphenols are the most important phytochemicals in our diets and have received great attention due to their broad benefits for human health by suppressing oxidative stress and playing a protective role in preventing different pathologies such as cardiovascular disease, cancer, diabetes, and obesity. The stability of polyphenols depends on their environments of processing and storage, such as pH and temperature. A wide range of technologies has been developed to stabilize polyphenols during processing. This review will provide an overview of the stability of polyphenols in relation to their structure, the factors impacting the stability of polyphenols, the new products deriving from unstable polyphenols, and the effect of a series of technologies for the stabilization of polyphenols, such as chemical modification, nanotechnology, lyophilization, encapsulation, cold plasma treatment, polyphenol–protein interaction, and emulsion as a means of improving stability. Finally, the effects of cooking and storage on the stability of polyphenols were discussed.

show abstract

Section: Effects Of Polyphenol–protein Interaction On the Stabilitymentioning

confidence: 99%

Available technologies on improving the stability of polyphenols in food processing

et al. 2021

View full text Add to dashboard Cite

show abstract

“… Ren et al (2019) inferred that hydrophobic forces play a role in the binding of C3G to soybean 7S and 11S globulins by isothermal titration thermal analysis. It has also been reported that preheated silkworm pupae protein (SPP) improved on the stability of C3G during food processing, which is due to the hydrophobic interaction between C3G and preheated SPP complexes ( Attaribo et al, 2020 ). Thus, hydrophobic interactions play an important role in the protection of the stability of soybean 7S and 11S globulins during simulated digestion.…”

Section: Resultsmentioning

confidence: 99%

Effects and interaction mechanism of soybean 7S and 11S globulins on anthocyanin stability and antioxidant activity during in vitro simulated digestion

Zheng

Zhao

et al. 2021

Current Research in Food Science

View full text Add to dashboard Cite

The objective of this study was to investigate the effects of soybean 7S and 11S globulins on the stability and antioxidant capacity of cyanidin-3-O-glucoside (C3G) in the simulated gastrointestinal environment, and further to elucidate their interaction mechanism. The stability and total content of anthocyanins (ACNs) before and after simulated digestion were determined by Ultraviolet–visible (UV–Vis) spectroscopic and pH differential methods, respectively, and free radical scavenging activity of C3G after simulated digestion were measured using ABTS and DPPH assays. The interaction mechanism was further investigated using molecular docking and molecular dynamics simulation. The analysis results showed that soybean 7S and 11S globulins had a protective effect on the stability of C3G during simulated digestion and improved the antioxidant capacity of C3G after simulated digestion. Soybean 11S globulin had a better effect than soybean 7S globulin in protecting the stability and antioxidant capacity of C3G against simulated gastrointestinal environment. In silico results showed that the binding interactions between C3G and 7S and 11S globulins were mainly hydrogen bonds and van der Waals forces, followed by hydrophobic interactions. Among them, ASN69 and THR101 are the key amino acid residues for 7S–C3G binding, and THR82 and PRO86 are the key amino acid residues for 11S–C3G binding. The results suggested that it may be helpful to use soybean 7S and 11S globulins as carriers to improve the stability and antioxidant activity of ACNs.

show abstract

“…Samples were scanned by Fourier infrared spectrometer (TENSOR II High‐sensitivity Measurement Research Grade Fourier Transform Infrared Spectrometer, Bruker, Germany). The scanning range is 4000–400 cm −1 , and the number of scanning is 32 times (Attaribo et al, 2020).…”

Section: Methodsmentioning

confidence: 99%

Microencapsulation of roselle anthocyanins with β‐cyclodextrin and proteins enhances the thermal stability of anthocyanins

Yana

Wang

et al. 2022

Food Processing Preservation

View full text Add to dashboard Cite

A Roselle extract was used in spray‐drying encapsulation with three different wall materials (soy protein isolate, gelatin, and β‐cyclodextrin) and combinations of those. The encapsulation efficiency, thermal stability, and microstructural evaluation of the encapsulated powder were further analyzed. The results showed that the encapsulation efficiency of gelatin, β‐cyclodextrin, and soy protein isolate for purified roselle anthocyanins was 73.99 ± 2.66%, 89.75 ± 0.14%, and 98.51 ± 0.45%. The encapsulation efficiency of anthocyanins by the composite wall materials (β‐cyclodextrin+gelatin, β‐cyclodextrin + soy protein isolate, and soy protein isolate+gelatin) could reach above 99%. The microcapsules with β‐cyclodextrin and soy protein isolate exhibited the smoothest curves of Fourier transform infrared spectroscopy within the characteristic peak of anthocyanins. The microcapsules containing gelatin have a surface structure with the least obvious holes or gaps and showed optimum thermal behavior. Novelty impact statement The pairwise combination of soy protein isolate, gelatin, and β‐cyclodextrin as carriers of purified roselle anthocyanins yielded high encapsulation efficiency of over 99% The addition of β‐cyclodextrin prevented the self‐aggregation of proteins, making the encapsulation efficiency of composite wall materials higher than that of single‐wall materials. The β‐turn of the heated protein was enhanced during the formation of the microcapsules. This change made the wall material combine more tightly.

show abstract

Studies on the interactional characterization of preheated silkworm pupae protein (SPP) with anthocyanins (C3G) and their effect on anthocyanin stability

Cited by 61 publications

References 48 publications

Available technologies on improving the stability of polyphenols in food processing

Available technologies on improving the stability of polyphenols in food processing

Effects and interaction mechanism of soybean 7S and 11S globulins on anthocyanin stability and antioxidant activity during in vitro simulated digestion

Microencapsulation of roselle anthocyanins with β‐cyclodextrin and proteins enhances the thermal stability of anthocyanins

Contact Info

Product

Resources

About