Transglutine is a term derived from the combination of the prefix "trans-" meaning across or through, and "glutine," taken from the Latin word "gluten," referring to a protein complex found in grains such as wheat, barley, and rye. In the field of biochemistry and molecular biology, transglutine refers to an enzyme known as transglutaminase.
Transglutaminase is a naturally occurring enzyme that catalyzes biochemical reactions, specifically the covalent bonding of proteins. This process, known as transamidation or protein crosslinking, occurs when the enzyme forms a bridge between amino acids within the protein structure, leading to the creation of new connections. This enzyme plays a crucial role in various biological processes, including blood clotting, tissue healing, and the formation of the extracellular matrix.
In the context of food science and the culinary industry, transglutine is often used as a food additive due to its unique ability to bind and modify proteins. It is utilized to improve the texture, binding capacity, and stability of food products, particularly those made with gluten-containing grains. By crosslinking the gluten proteins, transglutine enhances the elasticity of the dough, improving the texture of baked goods like bread, pasta, and pastries.
Furthermore, transglutine is employed to create meat analogues or "mock" meats, where it helps in binding and texturizing plant-based proteins, making them more similar to traditional meat products. It offers a valuable tool for food manufacturers seeking to develop gluten-free or meat alternatives with improved sensory properties.
