{"title":"Effects of High Intensity Ultrasonication on Molecular Characteristics and Emulsifying Properties of Rambutan Seed Protein","authors":"Suwimon Ariyaprakai","doi":"10.1007/s11483-023-09815-5","DOIUrl":null,"url":null,"abstract":"<div><p>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.</p></div>","PeriodicalId":564,"journal":{"name":"Food Biophysics","volume":"19 1","pages":"230 - 242"},"PeriodicalIF":2.8000,"publicationDate":"2023-12-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Biophysics","FirstCategoryId":"97","ListUrlMain":"https://link.springer.com/article/10.1007/s11483-023-09815-5","RegionNum":4,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"FOOD SCIENCE & TECHNOLOGY","Score":null,"Total":0}
引用次数: 0
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.
期刊介绍:
Biophysical studies of foods and agricultural products involve research at the interface of chemistry, biology, and engineering, as well as the new interdisciplinary areas of materials science and nanotechnology. Such studies include but are certainly not limited to research in the following areas: the structure of food molecules, biopolymers, and biomaterials on the molecular, microscopic, and mesoscopic scales; the molecular basis of structure generation and maintenance in specific foods, feeds, food processing operations, and agricultural products; the mechanisms of microbial growth, death and antimicrobial action; structure/function relationships in food and agricultural biopolymers; novel biophysical techniques (spectroscopic, microscopic, thermal, rheological, etc.) for structural and dynamical characterization of food and agricultural materials and products; the properties of amorphous biomaterials and their influence on chemical reaction rate, microbial growth, or sensory properties; and molecular mechanisms of taste and smell.
A hallmark of such research is a dependence on various methods of instrumental analysis that provide information on the molecular level, on various physical and chemical theories used to understand the interrelations among biological molecules, and an attempt to relate macroscopic chemical and physical properties and biological functions to the molecular structure and microscopic organization of the biological material.