Abstract
Rambutan seed protein untreated (No-US) and treated (US) with high intensity ultrasonication (~ 320 W 20 min) had been characterized. LC-MS/MS analysis revealed that molecular sizes of proteins identified in rambutan seed protein were in a range of 4.1 to 318.9 kDa. US protein had higher fractions of small molecular weight proteins than No-US protein, suggesting US disrupted polypeptide structures into smaller units. No-US protein and US protein displayed similar band patterns on SDS PAGE gels. The surface hydrophobicity, the denaturation temperature, and the enthalpy of heat denaturation of No-US protein and US protein were not significantly different. The applied ultrasonication was suggested to not have a strong effect on the protein tertiary conformation. Rambutan seed protein had a relatively high amount of hydrophobic amino acids of 40.2% promoted strong intra-hydrophobic interaction. Emulsions prepared by US protein had lesser bridging flocculation and higher creaming stability than prepared by No-US protein.
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Acknowledgements
This research project was financial supported by Agricultural Research Development Agency (Public Organization) of Thailand or “ARDA” (CRP6405030700). Rambutan seeds in this study were kindly donated by Malee Group Public Company Limited and Universal Food Public Company Limited. Soy protein isolate was kindly donated by Rama Production Co. Ltd. (Bangkok, Thailand). Chemical analysis and some experimental work were performed at Central Instrument Facility (Faculty of Science, Mahidol University, Bangkok), Scientific and Technological Research Equipment Centre Chulalongkorn University (Bangkok), Proteomics Services Center (Faculty of Medical Technology, Mahidol University, Bangkok), National Metal and Materials Technology Center (National Science and Technology Center, Pathum Thani), Department of Science Service (Division of Engineering Materials, Bangkok), and Office of Scientific Instrument and Testing (Prince of Songkla University, Songkhla). The author would like to thank Associate Professor Dr. Kanitha Tananuwong for the valuable discussion on the LC-MS/MS technique.
Funding
This study was funded by Agricultural Research Development Agency (Public Organization) of Thailand or “ARDA” (CRP6405030700).
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Suwimon Ariyaprakai: Conceptualization, Methodology, Formal analysis, Investigation, Writing-Original Draft, Writing – Review & Editing, Project administration, Funding acquisition.
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Supplementary Material 1
The LC-MS/MS analysis data showing names, molecular weight, and relative amounts of all proteins identified in US rambutan seed protein and in No-US rambutan seed protein. (DOCX 28.9 KB)
Supplementary Material 2
The image of SDS PAGE gel from Fig. 2 labled by SpotID. The corresponding table showing molecular weight band, band intensity, and band volume at each SpotID area of US rambutan seed protein and No-US rambutan seed protein. (DOCX 182 KB)
Supplementary Material 3
The DSC thermogram of (a) US rambutan seed protein and (b) No-US rambutan seed protein obtained by a heating rate of 5 °C/min. The graphs within the heating range of 70 °C to 100 °C were shown.(DOCX 35.3 KB)
Supplementary Material 4
The drawing pictures showing (a) emulsions stabilized by US rambutan seed protiens without bridging flocculaiton and (b) emulsions stabilized by No-US rambutan seed protiens with bridging flocculaiton.(DOCX 1.45 MB)
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Ariyaprakai, S. Effects of High Intensity Ultrasonication on Molecular Characteristics and Emulsifying Properties of Rambutan Seed Protein. Food Biophysics 19, 230–242 (2024). https://doi.org/10.1007/s11483-023-09815-5
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DOI: https://doi.org/10.1007/s11483-023-09815-5