Characterization of novel glycosyl hydrolases with application in the food industry

In industrial processes, enzymes are considered as a green alternative to traditional chemical catalysis as they are biodegradable, reusable and they do not produce waste products in excess. Enzymes have been applied to food products since early times of civilization, for instance in the production of bread, wine or milk curd. More recently, glycosidases, a family of enzymes catalysing the hydrolysis of glycosidic bonds in complex sugars, are becoming key tools within the food industry because of their ability to hydrolyse very stable glycosidic bonds in a clean and efficient way. However, many glycolytic processes in the food industry involve the use of harsh conditions (low pH, high concentrations of ethanol, high temperatures) that can lead to enzyme inactivation. A very promising approach to address this issue is the substitution of mesophilic organisms by extremophilic organisms as source of enzymes; as they thrive in extreme environments, their enzymes are generally performing better than their mesophilic counterparts. In this sense, two novel extremo-adapted β-glycosidases (family 1) have been selected and characterized, and their performance tested under different environmental conditions (glucose, fructose, organic co-solvents and arrange of pHs and temperatures) that could be generally found in food industrial processes (Chapter 4). In a second stage, the hydrolytic capacity of these enzymes towards 2 wine glucosides (Chapter 5) and towards glucovanillin and soybean isoflavones (Chapter 6) have been assessed with excellent prospects for their application in those food processes