Tannase
The enzyme tannase (EC 3.1.1.20) catalyzes the following reaction:
It is a key enzyme in the degradation of gallotannins and ellagicitannins, two types of hydrolysable tannins. Specifically, tannase catalyzes the hydrolysis of ester and depside bonds of hydrolysable tannins to release glucose and gallic or ellagic acid.
Tannase belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is tannin acylhydrolase. Other names in common use include tannase S, and tannin acetylhydrolase.
This enzyme has two known domains and one known active site. Tannase can be found in plants, bacteria, and fungi and has different purposes depending on the organism it is found in. Tannase also has many purposes for human use. The production of gallic acid is important in the pharmaceutical industry as it's needed to create trimethoprim, an antibacterial drug. Tannase also has many applications in the food and beverage industry. Specifically, its used to make food and drinks taste better, either by removing turbidity from juices or wines, or removing the bitter taste of tannins in some food and drinks, such as acorn wine. Additionally, because tannase can break ester bonds of glucose with various acids (chebulinic, gallic, and hexahydrophenic), it can be used in the process of fruit ripening.