FOOD CHEMISTRY
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2022
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IF 9.231
Na Xia,Chunqing Wang,Siming Zhu
In this study, ovalbumin (OVA) formed a complex with neohesperidin (NH) via a pH-shifting method. The NH-OVA complex self-assembled into NH-OVA nano-particles, which were then characterized and whose binding mechanism was evaluated by using multi-spectroscopic, thermodynamics, and molecular docking simulation methods. Fluorescence intensity decreased after OVA was complexed with NH. The binding constant of the OVA-NH complex was in the order of 6.32 × 10 5 M −1 suggesting that the complex is stable. Circular dichroism (CD) analysis showed that α -helix content increased, β-folding, β -turning, and irregular crimp content decreased after OVA and NH binding. Isothermal titration calorimetry results showed that hydrophobic interactions and hydrogen bonds made an important impact in the complex formation. The molecular docking results revealed that Van der Waals forces and hydrogen bonds contributed to the free binding energy of the complex. There were multiple possible surface binding sites between OVA with NH. The obtained results provide new insights into the interaction mechanism of OVA and NH, and as a vehicle for NH, the OVA has shown promising applications in functional foods.
研究领域:
食品科学
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生物化学
✓ 已验证
DOI
PubMed
高影响因子
JOURNAL OF FOOD ENGINEERING
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2025
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IF 5.8
Xuanyi Zhang,Xiaojun Lin,Jingwen Wang,Xiaoyu Luo,Baojun Xu
This study focused on enhancing the stability and bioaccessibility of pterostilbene (PTS) by encapsulating it with hydroxypropyl-β-cyclodextrin (HP-β-CD) using high-pressure homogenization (HPH) and pH-shift methods. The encapsulation process was performed at pressures of 50, 100, and 150 MPa along with three different treatments, achieving a maximum encapsulation efficiency of 94.34% and a loading capacity of 14.82% at 150 MPa. The SEM, XRD, and FTIR analyses confirmed encapsulation by revealing significant morphological changes, crystal structure modifications, and host-guest interactions. PTS-HP-β-CD complexes retained 82.22% of PTS at 4°C (28 days) and 76% under UVB (120 min), compared to 56.03% and 21% for free PTS, respectively. Additionally, these complexes exhibited enhanced DPPH scavenging rates (44.95% at 0.02 mg/mL), nearly twice that of free PTS. In the release studies, the complexes’ release behavior aligned with the Higuchi model. Encapsulated PTS revealed lower digestion rates in in-vitro gastric (32.24% vs. 49.88%) and intestinal phases (63.98% vs. 91.01%). Additionally, there was no observable toxicity for PTS-HP-β-CD to human epidermal keratinocytes, supporting its potential use in cosmetics, food, and pharmaceuticals. These results demonstrated that HPH combined with pH-shift methods effectively improved the stability and bioaccessibility of PTS, offering a promising strategy for its formulation.
研究领域:
食品科学
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药剂学
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生物学
✓ 已验证
产品关联
DOI
高影响因子
LWT-FOOD SCIENCE AND TECHNOLOGY
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2024
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IF 6
Lingyuan Wang,Diandian Huang,Keting Li,Yan Dai,Angxin Song,Laping He,Xingyi Chen,Lei Wang
Previous studies have shown that the organic solvent-free method has considerable potential for delivery systems in food applications. In this study, Nanocomplex of zein and pectin from apple (AP) or citrus (CP) was systemically fabricated and characterized by adjusting pectin pH (2.0–11.0) and mass ratios of zein:pectin (1:0, 1:0.5, 1:1, 1:2 and 1:3) via one-step pH-shifted process. Results showed that the size of zein/pectin nanocomplex remarkably decreased from >500 nm to ∼150 nm with the increasing pH level of pectin solution and proportion of pectin addition. Spherical shape was observed for nanocomplex formed by AP and CP in transmission electron microscopy images. Compared with zein/AP nanocomplex , zein/CP nanocomplex exhibited the smaller size, smoother surface and lower surface hydrophobicity, prompting us to conclude that CP, as compared to AP, had better performance. To further explore the mechanism, the behavior difference could be interpreted by the altered hydrophobic interaction between zein and pectin as revealed by fluorescence spectroscopy and Fourier transform infrared spectroscopy (FTIR). Findings in this study would facilitate the understanding of interaction between zein and pectin and provide new perspectives of pH-shift induced zein nanocomplex.
研究领域:
食品科学
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材料科学
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生物化学
✓ 已验证
产品关联
DOI
高影响因子
ULTRASONICS SONOCHEMISTRY
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2024
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IF 8.7
Xipeng Wang,Cunfang Wang,Mengjia Ma,Zhenghao Li,Xiaoning Zhang,Hua Jiang,Cunzhong Yuan
Mulberry leaf protein (MLP) is a nutrient-rich protein, but its applicability is limited because of its poor solubility. To address this issue, this study combines MLP with whey protein isolates (WPI), known for the high nutritional value, and subsequently forms composite protein nanoparticles using the ultrasound-assisted pH shifting method. Microscopic observation and SDS-PAGE confirmed the binding between these two proteins. Fluorescence spectra and Fourier Transform infrared spectroscopy (FTIR) analysis supported the involvement of electrostatic interactions, hydrophobic attractions, and hydrogen bonding in the formation of stable complex nanoparticles. The interactions between the proteins became stronger after ultrasound-assisted pH-shifting treatment. Solubility, emulsification capacity, foaming, and antioxidant activity, among other indicators, demonstrate that the prepared composite nanoparticles exhibit favorable functional properties. The study successfully illustrates the creation of protein-based complex nanoparticles through the ultrasound-assisted pH shifting method, with potential applications in the delivery of bioactive compounds.
研究领域:
食品科学
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生物化学
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营养学
✓ 已验证
产品关联
DOI
PubMed
高影响因子
JOURNAL OF DAIRY SCIENCE
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2023
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IF 3.5
Ru Zhao,Wenfei Fu,Dan Li,Chao Dong,Zhaoxue Bao,Cuina Wang
ABSTRACT Three modifications (pH-shift, ultrasound, combined pH-shift/ultrasound) induced alterations in pure whey protein (WPI), pea protein (PPI), and mixed whey/pea protein (WPI/PPI) were investigated. The processing effect was related to the protein type and technique utilized. Solubility of WPI remained unchanged by various treatments. Particle size was enlarged by pH-shift while reduced by ultrasound and combined approach. All methods exposed more surface hydrophobic groups on WPI, while pH-shift and joint processing was detrimental to its emulsifying activity. PPI and mixture exhibited similar responses toward the modifications. Solubility of PPI and the blend enhanced in the sequence of pH-shift/ultrasound > ultrasound > pH-shift. Individual approach expanded while co-handling diminished the particle diameter. Treatments also caused more disclosure of hydrophobic regions in PPI and WPI/PPI and emulsifying activity was ameliorated in the order of pH-shift/ultrasound > ultrasound > pH-shift.
研究领域:
食品科学
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蛋白质化学
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超声波技术
✓ 已验证
产品关联
DOI
PubMed
高影响因子
JOURNAL OF DAIRY SCIENCE
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2023
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IF 3.5
X.P. Wang,C.F. Wang,X.Q. Zhao,M.J. Ma,Z.H. Li,H. Jiang,X.N. Zhang,C.Z. Yuan
ABSTRACT Milk proteins can be used as encapsulation walls to increase the bioavailability of active compounds because they can bind hydrophobic, hydrophilic, and charged compounds. The objective of this study was to investigate the effects of astaxanthin (ASTA) encapsulation and the functional properties of milk protein and ASTA nanocomposites by ultrasound-assisted pH-shifting treatment of different milk proteins, including milk protein concentrate (MPC), micellar casein (MCC), and whey protein isolate (WPI). The ultrasound-assisted pH shifting treatment of milk protein helped to improve the encapsulation rate of ASTA. Therein, MCC showed the great improvement on encapsulating ASTA after co-treatment with the raised encapsulated rate of 5.11%, followed by WPI and MPC. Furthermore, the nanocomposites of ASTA with milk protein exhibit improved bioavailability, antioxidant capacity, and storage stability. By comparison, MCC-encapsulated ASTA has the best storage stability, followed by MPC, and WPI-encapsulated ASTA has the least stability over a 28-d storage period. The results of intrinsic fluorescence and surface hydrophobicity showed that milk protein underwent fluorescence quenching after binding to ASTA, which was due to the hydrophobic sites of the protein being occupied by ASTA. In general, the nanocomposites of milk protein and ASTA fabricated by using ultrasound-assisted pH-shifting treatment have the potential to be better nano-delivery systems for ASTA in functional foods, especially MCC showed the excellent performance in encapsulation after treatment technique.
研究领域:
食品科学
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营养学
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生物技术
✓ 已验证
产品关联
DOI
PubMed
高影响因子
FOOD CHEMISTRY
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2018
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IF 4.946
Weijun Chen,Wenjun Wang,Xiaobin Ma,Ruiling Lv,Ritesh Balaso Watharkar,Tian Ding,Xingqian Ye,Donghong Liu
Effect of pH-shifting on structural and functional properties of whey protein isolate and its interaction with (−)-epigallocatechin-3-gallate were investigated. Circular dichroism spectra showed that pH-shifting induced the decrease in α-helix content by 12.18% and β-sheet content by 3.24%, but β-turn and random coil content increased by 4.26% and 5.91%, respectively. Increase of fluorescence intensity and red-shift of maximum emission wavelength indicated the structural unfolding and exposure of tyrosine. The treatment also significantly increased the surface hydrophobicity, disulfide bonds content, solubility, emulsifying activity and emulsion stability of whey protein isolate at P < 0.05 level. Fluorescence quenching analysis revealed that treated whey protein isolate have a stronger binding affinity to (−)-epigallocatechin-3-gallate, resulting a better protection against the degradation of (−)-epigallocatechin-3-gallate and its antioxidant activity. This study confirmed that pH-shifting treatment can improve functional properties of whey protein isolate and its potential as a protective carrier for polyphones.
研究领域:
食品科学
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蛋白质化学
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营养学
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生物物理学
✓ 已验证
产品关联
DOI
PubMed
高影响因子
危险品化学品经营许可证（带存储）