Related Experiment Video
Updated: Jun 9, 2025
10:01
Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro
Published on: April 8, 2020
5.8K
Lentil protein and trehalose conjugates: Structural interactions and mechanisms for improving multi-level structure
Mohammad Alrosan1,2,3, Sofyan Maghaydah4,5, Ali Al-Qaisi6
1Department of Food Science and Nutrition, Faculty of Agricultur, Jerash University, Jerash, Jordan.
Journal of Food Science
|October 22, 2024
Summary
Trehalose conjugation significantly improved lentil proteins
Area of Science:
- Food Science and Technology
- Protein Chemistry
- Bioconjugation
Background:
- Lentil proteins (LPs) possess high nutritional value but suffer from poor water solubility and digestibility, limiting their food applications.
- Current uses of LPs are primarily for nutritional benefits, not functional properties, hindering their competitiveness against other plant-based proteins.
- Expanding LP applications requires enhancing their functional characteristics, particularly water solubility.
Purpose of the Study:
- To improve the functionality and nutritional value of lentil proteins (LPs).
- To address the limitations of low water solubility and digestibility in LPs.
- To explore the potential of trehalose conjugation for modifying LP properties.
Main Methods:
- Investigated lentil protein structure using spectroscopic techniques (fluorescence, UV-Vis, FTIR) at varying trehalose concentrations.
- Analyzed changes in surface charge and hydrophobicity of trehalose-conjugated LPs (T-LPs).
- Quantified improvements in digestibility and water solubility of T-LPs compared to native LPs.
Main Results:
- Trehalose conjugation significantly altered LP structure and conformation (p < 0.05).
- Surface charge shifted from -22.7 to -31.4, and hydrophobicity decreased from 753 to 543 a.u. in T-LPs.
- T-LPs exhibited enhanced digestibility (75% to 81.8%) and solubility (60% to 66%).
Conclusions:
- Trehalose conjugation is an effective method to improve the quality and functionality of lentil proteins.
- Enhanced solubility and digestibility of T-LPs expand their potential use in various food products, including beverages.
- This approach positions LPs as a more competitive and versatile plant-based protein source.
Related Concept Videos
01:22Protein Folding
117.5K
Overview
117.5K
02:15Protein and Protein Structure
78.7K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
A protein's shape is critical to its function. For example, an enzyme...
78.7K
01:24Protein Organization
6.3K
Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence....
The primary structure of a protein is its amino acid sequence....
6.3K
00:49Ligand Binding and Linkage
4.8K
Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked. In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
4.8K
02:04Protein-protein Interfaces
12.5K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
12.5K
01:56Structural Protein Function
27.5K
Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to...
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to...
27.5K