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Conformational changes in lentil protein structure resulting from the application of moderate electric fields

Grant number: 19/18704-0
Support type:Scholarships abroad - Research Internship - Master's degree
Effective date (Start): September 15, 2019
Effective date (End): November 14, 2019
Field of knowledge:Agronomical Sciences - Food Science and Technology - Food Engineering
Principal researcher:Ana Carla Kawazoe Sato
Grantee:Cristiane Grella Miranda
Supervisor abroad: Antonio Augusto Vicente
Home Institution: Faculdade de Engenharia de Alimentos (FEA). Universidade Estadual de Campinas (UNICAMP). Campinas , SP, Brazil
Research place: Universidade do Minho (UMinho), Portugal  
Associated to the scholarship:18/16456-7 - Complex coacervation using lentil protein obtained by different methods of extraction, BP.MS

Abstract

The growing tendency towards a diet free or reduced of animal products has aroused interest for vegetable protein sources. Thus, pulse proteins such as lentils, chickpeas and beans, due to their high protein content, have become viable options. However, proteins obtained by the traditional alkaline extraction method may show impaired functionality when considering their commercial application. Therefore, strategies to improve the functionality of these proteins have been increasingly studied. The application of moderate electric fields is a technique that promotes modification of the protein structure by the passage of a current, which may or may not generate heat. Studies with milk and soy proteins indicate that this technology is capable of modifying the protein structure due to the opening of its chains and exposure of hydrophobic and thiols groups. However, as it is an emerging technology, studies on structural modification of pulse proteins are still scarce. Thus, the objective of this work is to evaluate the possible modifications caused by the application of the moderate electric fields to the lentil proteins obtained by the alkaline extraction method. The project aims to evaluate the hydrophobicity properties, accessibility of sulfhydryl groups and changes in the secondary structure of the protein. Furthermore, we intend to evaluate how these possible modifications can affect the complex coacervation process of this protein with pectin. (AU)

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