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Hub AI
Tannase AI simulator
(@Tannase_simulator)
Hub AI
Tannase AI simulator
(@Tannase_simulator)
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.
In addition to catalyzing the hydrolysis of the central ester bond between the two aromatic rings of digallate (depsidase activity), tannase may also have an esterase activity (hydrolysis of terminal ester functional groups that are attached to only one of the two aromatic rings).
Digallate is the conjugate base of digallic acid, but are often used synonymously. Similarly, gallate and gallic acid are used interchangeably. Both digallic and gallic acid are organic acids that are seen in gallotannins and are usually esterified to a glucose molecule. In other words, tannins (which contain digallate/digallic acid) are the natural substrate of tannase. When tannins, specifically gallotannins, are broken down by tannase through the hydrolysis of ester bonds, gallic acid and glucose are formed.
The crystal structure of tannase varies slightly depending on the strain being observed, in this case we are looking at the tannase SN35N strain produced in Lactobacillus plantarum. On average, its molecular weight is in the range of 50-320 kDa.
Tannase from Lactobacillus plantarum has 489 amino acid residues and two domains. The two domains of tannase are called the α/β-hydrolase domain and the lid domain. The α/β-hydrolase domain consists of residues 4-204 and 396-469, and is composed of two nine-stranded β-sheets surrounded by four α-helices on one side and two α-helices on the other side. Conversely, the lid domain consists of residues 205–395 and is composed of seven α-helices and two β-sheets.
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.
In addition to catalyzing the hydrolysis of the central ester bond between the two aromatic rings of digallate (depsidase activity), tannase may also have an esterase activity (hydrolysis of terminal ester functional groups that are attached to only one of the two aromatic rings).
Digallate is the conjugate base of digallic acid, but are often used synonymously. Similarly, gallate and gallic acid are used interchangeably. Both digallic and gallic acid are organic acids that are seen in gallotannins and are usually esterified to a glucose molecule. In other words, tannins (which contain digallate/digallic acid) are the natural substrate of tannase. When tannins, specifically gallotannins, are broken down by tannase through the hydrolysis of ester bonds, gallic acid and glucose are formed.
The crystal structure of tannase varies slightly depending on the strain being observed, in this case we are looking at the tannase SN35N strain produced in Lactobacillus plantarum. On average, its molecular weight is in the range of 50-320 kDa.
Tannase from Lactobacillus plantarum has 489 amino acid residues and two domains. The two domains of tannase are called the α/β-hydrolase domain and the lid domain. The α/β-hydrolase domain consists of residues 4-204 and 396-469, and is composed of two nine-stranded β-sheets surrounded by four α-helices on one side and two α-helices on the other side. Conversely, the lid domain consists of residues 205–395 and is composed of seven α-helices and two β-sheets.