Ultrasound-assisted assembly of β-lactoglobulin and chlorogenic acid for non covalent nanocomplex: fabrication, characterization and potential biological function
“…In that study, the protein–polyphenol covalent complexes could be effectively prepared by the redox method, resulting in the band position of complexes moving into positions with higher molecular mass on SDS-PAGE than that of LF. The band position of the group H was also slightly shifted, which indirectly proved our previous hypothesis that ultrasonication could also generate hydroxyl radicals that attacked the nucleophilic group of LG and bind to CA with covalent bonds [34] . Fig.…”
“…In that study, the protein–polyphenol covalent complexes could be effectively prepared by the redox method, resulting in the band position of complexes moving into positions with higher molecular mass on SDS-PAGE than that of LF. The band position of the group H was also slightly shifted, which indirectly proved our previous hypothesis that ultrasonication could also generate hydroxyl radicals that attacked the nucleophilic group of LG and bind to CA with covalent bonds [34] . Fig.…”
“…DSC is an efficient thermal analytic tool for examining changes in the thermal stability of PC and phlorotannin binding ( 42 ). Denaturation peak temperatures (Td) commonly indicate the thermal stability of a protein.…”
Section: Resultsmentioning
confidence: 99%
“…This result might be consistent with the XRD results described above. Liu et al found that the sample of β-lactoglobulin and chlorogenic acid also changed from a complete sheet structure to fragments by SEM observation after ultrasound ( 42 ). In line with the experimental findings, PC and phlorotannin likewise underwent a full sheet structure to fragmentation shift.…”
Section: Resultsmentioning
confidence: 99%
“…The increased thermal stability of UPP might be due to the formation of hydrogen bonds,electrostatic and hydrophobic interactions, which was verified in the FTIR results. Following the conjugation of chlorogenic acid-lactoferrin-dextran, Liu et al discovered that the thermal denaturation temperature of lactoferrin increased [42]. Various methodologies and ligands for polyphenols or polysaccharides could cause the changed protein to exhibit unique thermal behavior (43).…”
IntroductionPhycocyanin offers advantageous biological effects, including immune-regulatory, anticancer, antioxidant, and anti-inflammation capabilities. While PC, as a natural pigment molecule, is different from synthetic pigment, it can be easily degradable under high temperature and light conditions.MethodsIn this work, the impact of ultrasound treatment on the complex of PC and phlorotannin structural and functional characteristics was carefully investigated. The interaction between PC and phlorotannin after ultrasound treatment was studied by UV–Vis, fluorescence spectroscopy, circular dichroism (CD) spectroscopy, fourier transform infrared (FTIR) spectroscopy. Additionally, the antioxidant potential and in vitro digestibility of the complexes were assessed.ResultsThe result was manifested as the UV–Vis spectrum reduction effect, fluorescence quenching effect and weak conformational change of the CD spectrum of PC. PC was identified as amorphous based on the X-ray diffraction (XRD) data and that phlorotannin was embedded into the PC matrix. The differential scanning calorimetry (DSC) results showed that ultrasound treatment and the addition of phlorotannin could improve the denaturation peak temperatures (Td) of PC to 78.7°C. In vitro digestion and free radical scavenging experiments showed that appropriate ultrasound treatment and the addition of phlorotannin were more resistant to simulated gastrointestinal conditions and could improve DPPH and ABTS+ free radical scavenging performance.DiscussionUltrasound treatment and the addition of phlorotannin changed the structural and functional properties of PC. These results demonstrated the feasibility of ultrasound-assisted phlorotannin from A. nodosum in improving the functional properties of PC and provided a possibility for the application of PC-polyphenol complexes as functional food ingredients or as bioactive materials.
“…), thus being more favorable for the formation of covalent bond. Research on physical techniques to enhance polyphenol modifications has emerged; however, it mainly focuses on animal proteins, with less research relating to plant proteins [ 10 , 11 ]. Whether or not the covalent binding of plant proteins to dietary polyphenols could be promoted by ultrasound-assisted means deserves our further study.…”
It is essential to understand the mechanism of action of ultrasound synergistic free radical oxidation to promote covalent reactions between proteins and polyphenols. (−)-epigallo-catechin 3-gallate (EGCG) with rich bioactivity could be used to increase the functional properties of cereal protein—gliadin (GL). This study systematically explored the role of ultrasound treatment (US) on the binding mechanisms of GL and EGCG. Electrophoresis and high-performance liquid chromatography (HPLC) confirmed the greater molecular mass of the covalent complexes in the ultrasound environment. Quantitative analysis by the phenol content revealed that the ultrasound environment increased the EGCG content in the covalent complex by 15.08 mg/g of protein. The changes in the spatial structure of the proteins were indicated by Fourier infrared and ultraviolet spectroscopy. Additionally, scanning electron microscopy (SEM) and atomic force microscopy (AFM) found that US disrupted the aggregation of GL and the clustered structure of the covalent complexes. The results demonstrated that the water solubility of ultrasonic conjugates was significantly increased by 8.8–64.19%, the digestion rate was more efficient, and the radical scavenging capacity was twice that of GL. This research contributes to the theoretical basis for broadening the application of polyphenols in modifying protein.
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