Inulinases

Inulinases are enzymes that catalyze the hydrolysis of inulin, a polysaccharide composed of repeating fructose units. These enzymes belong to the glycoside hydrolase family and are primarily found in bacteria, fungi, and yeasts, as well as in some plants. Inulinases cleave inulin into smaller oligosaccharides, such as inulobiose and inulotriose, and ultimately into its monosaccharide component, fructose.

There are three main types of inulinases based on their catalytic action: exoinulinases, endoinulinases, and inulin fructotransferases. Exoinulinases act on the non-reducing end of the inulin chain, releasing fructosyl units. Endoinulinases act on internal bonds within the inulin chain, producing a mixture of oligosaccharides. Inulin fructotransferases can transfer fructosyl units to other molecules.

These enzymes have significant industrial applications. They are widely used in the food industry to produce high-fructose syrups from inulin-rich sources like chicory and Jerusalem artichokes. This process is an alternative to the enzymatic conversion of glucose to fructose. Inulinases are also employed in the pharmaceutical industry for the production of fructooligosaccharides (FOS), which are prebiotics known for their health benefits. Research is ongoing to explore their potential in bioremediation and biofuel production. The efficiency and specificity of inulinases make them valuable tools in various biotechnological processes.