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Ultrasound-assisted glycosylation of ovalbumin and dextran conjugate carrier for anthocyanins and their stability evaluation  ( SCI-EXPANDED收录 EI收录)   被引量:12

文献类型:期刊文献

英文题名:Ultrasound-assisted glycosylation of ovalbumin and dextran conjugate carrier for anthocyanins and their stability evaluation

作者:Chen, Boyu[1];Chen, Lei[1];Li, Chen[1];Huang, Wanhuan[1];Zhao, Yanan[1];Ai, Chao[1];Teng, Hui[1]

机构:[1]Guangdong Ocean Univ, Coll Food Sci & Technol, Guangdong Prov Key Lab Aquat Prod Proc & Safety, Guangdong Prov Engn Lab Marine Biol Prod, Zhanjiang 524088, Peoples R China

年份:2024

卷号:109

外文期刊名:ULTRASONICS SONOCHEMISTRY

收录:SCI-EXPANDED(收录号:WOS:001296917500001)、、EI(收录号:20243316884317)、Scopus(收录号:2-s2.0-85201151110)、WOS

基金:This work is supported by the National Natural Science Foundation of China (NSFC, Grant No. 32272315, 32372335) , the Natural Science Foundation of Guangdong Province (2022A1515010694) , the Key Field Special Project of High Education of Guangdong Province (2023ZDZX2026)

语种:英文

外文关键词:Anthocyanins; Glycosylation; Stability; Ultrasound

外文摘要:Anthocyanins (AC) are vulnerable to degradation when affected by external factors. The present study employed ultrasound-assisted glycosylation of ovalbumin (OVA) and dextran (Dex) to generate conjugate carrier for AC to improve its stability. The results showed that sonication significantly improved the progression of Maillard reaction to OVA. Compared to traditional glycosylation, ultrasound treatment showed a higher degree of grafting, a lower number of free-SH, and smaller particle size and uniform distribution. The SDS-PAGE results indicated covalent interaction. Intrinsic fluorescence (INF), Fourier transform infrared spectroscopy (FTIR), and Circular dichroism (CD) analysis results suggested that ultrasound-assisted glycosylation altered the OVA structure. The scanning electron microscope (SEM) and X-ray diffractometer (XRD) observed that the ultrasound-assisted complex had a more compact and smoother structure and protein unfolding were better. The protein solubility increased significantly after glycosylation. Thermal gravimetric analysis (TGA) and Differential scanning calorimetry (DSC) indicated that the glycosylated conjugates can significantly improve the thermal stability of AC In addition, the AC showed an improved processing and storage stability when conjugated with glycosylated carrier. The glycosylated protein-anthocyanins complex may help provide new ideas and scientific basis for the development of naturally sourced anthocyanins-relevant products in pharmaceutical and food industry applications.

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