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163 results on '"Niu, Fuge"'

16. Does arginine aggregate formation in aqueous solutions follow a two-step mechanism?

Author

Niu, Fuge, Hu, Xinyu, Ritzoulis, Christos, Tu, Weiwei, Zhao, Xurui, Xia, Yuanzhi, Lu, Yinghua, Yin, Junfeng, and Pan, Weichun

Abstract

The formation of aggregates was studied in arginine aqueous solutions using light scattering. The main driving force for aggregate formation is hydrogen bonding between the arginine (Arg) amino acids, which is partially verified using density functional theory calculations. The measurement of energy loss during this process, coupled with Cryo-EM morphology data, indicates that these aggregates are in the solid state. The aggregation occurs in two steps, with a liquid intermediate stage. The investigation of the effect of pH and solute concentration on aggregate formation for other amino acid aqueous solutions verifies that aggregate formation is amino-acid specific, while small-sized clusters formed by weak interactions lead to large-sized aggregation. The water structure around amino acid molecules sheds light on the prediction of their aggregate formation. Homochirality is observed in the aggregates; its existence sheds light on the origin of protein homochirality. [ABSTRACT FROM AUTHOR]

Published
2024
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32. Fabrication and stability of W/O/W emulsions stabilized by gum arabic and polyglycerol polyricinoleate.

Author

Niu, Fuge, Zhao, Mengdi, Tu, Weiwei, Li, Zhe, Gao, Yi, Du, Yixuan, and Pan, Weichun

Subjects
*GUM arabic, *EMULSIONS, *OIL-water interfaces, *VITAMIN B12, *ADSORPTION capacity, *CHEMICAL industry
Abstract

BACKGROUND: In order to study the effect of adsorption of surfactant at the two interfacial layers on emulsion stability, the kinetically stable water‐in‐oil‐in‐water (W/O/W) emulsion carriers were prepared using polyglycerol polyricinoleate (PGPR) and gum arabic (GA) as emulsifiers. The relationship between the adsorption of the surfactant and the stability mechanism of the emulsions was elucidated. RESULTS: When the contents of PGPR and GA were low, the interfaces between oil and the inner and outer water phases, respectively, could not be completely covered. However, when the concentration of PGPR was higher than 60 g kg−1, the excess PGPR was adsorbed on the interface between the oil phase and the outer water phase. When the concentration of GA reached 80 g kg−1, more GA was adsorbed to the oil‐in‐water interface. Moreover, the presence of PGPR on the interface could reduce the adsorption capacity of GA. Two types of kinetically stable emulsions were obtained by optimizing the interface composition (60 g kg−1 GA/80 g kg−1 PGPR and 60 g kg−1 PGPR/80 g kg−1 GA). The kinetically stable W/O/W emulsions prepared in this study were successfully used to encapsulate a hydrophilic vitamin (vitamin B12) with an encapsulation efficiency (EE) of 80% and release efficiency (RE) of 95%. The interfacial adsorption GA can accelerate the hydrolysis of fat. CONCLUSION: Overall, this study provides a new strategy for the preparation of W/O/W emulsions, which might be beneficial for application in food, cosmetic, chemical, and pharmaceutical industries. © 2023 Society of Chemical Industry. [ABSTRACT FROM AUTHOR]

Published
2024
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36. The influence of KCl concentration on the gelation of myofibrillar protein giant squid (Dosidicus gigas) due to molecular conformation change

Author

Niu, Fuge, Ma, Shuang, Zhang, Xiuzhen, Ritzoulis, Christos, Chen, Yueyue, and Pan, Weichun

Subjects
Nutrition and Dietetics, Endocrinology, Diabetes and Metabolism, Food Science
Abstract

IntroductionProtein gelation process is of importance in food industry. The objective of this study is to investigate the influence of salt concentration variation, which induced protein conformation change, on protein’s intermolecular interactions and its gelation process.MethodsParamyosin has been separated and purified from myofibrillar protein extracted from giant squid. Then Giant squid’s paramyosin molecular mass and intermolecular interactions were quantified by means of light scattering techniques. Finally, the micro-rheology study via diffusing wave spectroscopy (DWS) technique revealed that this conformation change dramatically affected myofibrillar protein gelation process.ResultsThe obtained apparent molecular weight (ca 2 × 105 g/mol) suggested that protein molecules existed as dimers, while the second virial coefficient A2 significantly reduced from −3.98456 × 10−5 to −5.07575 × 10−4 ml mol/g2 when KCl concentrated from 0.15 to 1 mol/L. Light scattering data also suggest that paramyosin dimers are stiff, with a persistence length of 120 nm, almost the length of a molecule and independent of salt concentration. Mean-square displacement (MSD) of tracer particles at 5 temperatures with 4 salt concentrations displayed that this conformation change had dramatic effect. Therefore, G’ and G” were remarkably altered with at least one order of magnitude difference owing to this event occurrence.ConclusionsParamyosin conformation change due to KCl concentrated enhances attractive interactions with apparent molecular mass increase, which resulted in majority paramyosin molecules (> 99%) in dimeric form and promoted aggregates formation. DWS technique revealed that the conformation change dramatic affected this process characterized by the correlation functions, MSD, and G’ and G”. This study brings forward data on understanding the effect of a major salt supplement, KCl, on the chemical physics of a major muscle protein.

Published
2023
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