ABSTRACT
L-Glutaminases are enzymes that catalyze the cleavage of the gamma-amido bond of L-glutamine residues, producing ammonia and L-glutamate. These enzymes have several applications in food and pharmaceutical industries. However, the L-glutaminases that hydrolyze free L-glutamine (L-glutamine glutaminases, EC 3.5.1.2) have different structures and properties with respect to the L-glutaminases that hydrolyze the same amino acid covalently bound in peptides (peptidyl glutaminases, EC 3.5.1.43) and proteins (protein-glutamine glutaminase, EC 3.5.1.44). In the food industry, L-glutamine glutaminases are applied to enhance the flavor of foods, whereas protein glutaminases are useful to improve the functional properties of proteins. This review will focus on structural backgrounds and differences between these enzymes, the methodology available to measure the activity as well as strengths and limitations. Production methods, applications, and challenges in the food industry will be also discussed. This review will provide useful information to search and identify the suitable L-glutaminase that best fits to the intended application.