Tannase

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tannase
Identifiers
EC no. 3.1.1.20
CAS no. 9025-71-2
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The enzyme tannase (EC 3.1.1.20) catalyzes the following reaction: [1]

Contents

digallate + H2O = 2 gallate

It is a key enzyme in the degradation of gallotannins and ellagicitannins, two types of hydrolysable tannins. [2] Specifically, tannase catalyzes the hydrolysis of ester and depside bonds of hydrolysable tannins to release glucose and gallic or ellagic acid. [3] [2]

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. [4]

This enzyme has two known domains and one known active site. [3] Tannase can be found in plants, bacteria, and fungi and has different purposes depending on the organism it is found in. [2] 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. [5] 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. [3] 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. [6]

Mechanism

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). [4]

Digallate is the conjugate base of digallic acid, [7] but are often used synonymously. Similarly, gallate and gallic acid are used interchangeably. [8] Both digallic and gallic acid are organic acids that are seen in gallotannins and are usually esterified to a glucose molecule. [2] 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. [2]

Structure

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. [3]

Domains

Tannase from Lactobacillus plantarum has 489 amino acid residues and two domains. [5] 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. [3]

Active sites

There is one known active site in tannase found in the SN35N strain. The crystal structure shows there is a tunnel formed by two opposing domains that can fit the various substrates needed for tannase to hydrolyze. [3] This active site is referred to as the Ser163 active site and is located in the α/β-hydrolase domain. In this active site Ser163, Asp419, and His451 residues form a catalytic triad. [3] [6] If any one of these residues are mutated in the catalytic triad, tannase activity almost always stops. [9]

Structure and function

One way in which the structure of tannase is tied with its function involves a loop structure, called the flap. The flap connects β8 and β9 sheets and is located under the catalytic triad. As a result of weak electron densities, this structure is very flexible. Due to its flexibility, the flap is better able to guide the substrate in entering the enzyme and helps to strengthen the overall binding of the complex by forming additional interactions with other parts of the substrate. [9]

Function

Plants

Tannase functions differently in the cell depending on the organism being observed. In many plants, tannase is used to produce tannins, which are found in leaves, wood, and bark. [10] The production of tannins in plants is essential for defense against herbivory, as they cause a strong unpalatable flavor. [11] Tannins are considered secondary metabolites in plants. Therefore, their production by tannase plays no direct role in plant primary metabolism.[ citation needed ]

Microorganisms

On the other hand, tannase serves a different purpose in many microorganisms. In the cell, tannase is a key enzyme in the degradation of gallotannins . [12] This is important, because some microorganisms use tannase to breakdown hydrolysable tannins, such as gallotannins, to form glucose and gallic acid. [5] [13] These byproducts are created from the hydroxylation of the aromatic nucleus of the tannin, followed by ring cleavage. Glucose and gallic acid can then be readily converted to metabolites (i.e. pyruvate, succinate, and acetyl coenzyme A) that can be used in the Krebs cycle. Specific microorganisms that utilize tannase in this way include Pseudomonas species. [14]

Species distribution

Tannase is present in a diverse group of microorganisms, including rumen bacteria. [12] Many other bacterial species have been found to produce tannase by being isolated from different types of media such as soil, wastewater, compost, forest litter, feces, beverages, pickles, etc. Bacteria and archaea species with tannase activity have been found in the genera: Achromobacter, Atopobium, Azotobacter, Bacillus, Citrobacter, Corynebacterium, Enterobacter, Enterococcus, Fusobacterium, Gluconoacetobacter, Klebsiella, Lactobacillus, Lonepinella, Methanobrevibacter, Microbacterium, Oenococcus, Pantoea, Pediococcus, Providencia, Pseudomonas, Selenomonad, and Serratia. [15] In addition, some fungal species are dominant tannase producers, such as Aspergilli species. [2]

Related Research Articles

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<span class="mw-page-title-main">Cellulase</span> Class of enzymes

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<span class="mw-page-title-main">Aspartate transaminase</span> Enzyme involved in amino acid metabolism

Aspartate transaminase (AST) or aspartate aminotransferase, also known as AspAT/ASAT/AAT or (serum) glutamic oxaloacetic transaminase, is a pyridoxal phosphate (PLP)-dependent transaminase enzyme that was first described by Arthur Karmen and colleagues in 1954. AST catalyzes the reversible transfer of an α-amino group between aspartate and glutamate and, as such, is an important enzyme in amino acid metabolism. AST is found in the liver, heart, skeletal muscle, kidneys, brain, red blood cells and gall bladder. Serum AST level, serum ALT level, and their ratio are commonly measured clinically as biomarkers for liver health. The tests are part of blood panels.

<span class="mw-page-title-main">DD-transpeptidase</span> Bacterial enzyme

DD-transpeptidase is a bacterial enzyme that catalyzes the transfer of the R-L-αα-D-alanyl moiety of R-L-αα-D-alanyl-D-alanine carbonyl donors to the γ-OH of their active-site serine and from this to a final acceptor. It is involved in bacterial cell wall biosynthesis, namely, the transpeptidation that crosslinks the peptide side chains of peptidoglycan strands.

<span class="mw-page-title-main">Neuraminidase</span> Glycoside hydrolase enzymes that cleave the glycosidic linkages of neuraminic acids

Exo-α-sialidase is a glycoside hydrolase that cleaves the glycosidic linkages of neuraminic acids:

<span class="mw-page-title-main">Glucose 6-phosphatase</span> Enzyme

The enzyme glucose 6-phosphatase (EC 3.1.3.9, G6Pase; systematic name D-glucose-6-phosphate phosphohydrolase) catalyzes the hydrolysis of glucose 6-phosphate, resulting in the creation of a phosphate group and free glucose:

<span class="mw-page-title-main">Glucocerebrosidase</span> Mammalian protein found in humans

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β-Glucosidase Class of enzymes

β-Glucosidase is an enzyme that catalyses the following reaction:

<span class="mw-page-title-main">6-phosphogluconolactonase</span> Cytosolic enzyme

6-Phosphogluconolactonase (EC 3.1.1.31, 6PGL, PGLS, systematic name 6-phospho-D-glucono-1,5-lactone lactonohydrolase) is a cytosolic enzyme found in all organisms that catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconic acid in the oxidative phase of the pentose phosphate pathway:

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<span class="mw-page-title-main">Limonene-1,2-epoxide hydrolase</span>

In enzymology, a limonene-1,2-epoxide hydrolase (EC 3.3.2.8) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Microsomal epoxide hydrolase</span>

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<span class="mw-page-title-main">Digallic acid</span> Chemical compound

Digallic acid is a polyphenolic compound found in Pistacia lentiscus. Digallic acid is also present in the molecule of tannic acid. Digalloyl esters involve either -meta, or -para depside bonds.

A gallotannin is any of a class of molecules belonging to the hydrolysable tannins. Gallotannins are polymers formed when gallic acid, a polyphenol monomer, esterifies and binds with the hydroxyl group of a polyol carbohydrate such as glucose.

A hydrolysable tannin or pyrogallol-type tannin is a type of tannin that, on heating with hydrochloric or sulfuric acids, yields gallic or ellagic acids.

The ellagitannins are a diverse class of hydrolyzable tannins, a type of polyphenol formed primarily from the oxidative linkage of galloyl groups in 1,2,3,4,6-pentagalloyl glucose. Ellagitannins differ from gallotannins, in that their galloyl groups are linked through C-C bonds, whereas the galloyl groups in gallotannins are linked by depside bonds.

<span class="mw-page-title-main">Glucogallin</span> Chemical compound

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N-acetyl-β-d-glucosaminidase(EC 3.2.1.30; EC 3.2.1.52) is a mesophilic hydrolase that specifically hydrolyzes N-acetyl-glucosides. The enzyme is found across a wide variety of marine and terrestrial creatures with the primary function of breaking down oligosaccharides in the presence of water. One of the primary functions of the enzyme is to target and hydrolyze oligosaccharides containing chitin. In this chitinase function, the enzyme contributes to the ability of many organisms to break down chitin-containing molecules and subsequently digest or re-uptake environmental chitin, carbon, or nitrogen. The enzyme's crystal structure varies slightly across organisms, but is characterized by three or four domains with one active site. Across proteins, the active site entails an α-β barrel with either an arginine or tryptophan residues in the barrel pocket to bind incoming substrate.

References

  1. ↑ Dyckerhoff H, Armbruster R (1933). "Zur Kenntnis der Tannase". Hoppe-Seyler's Z. Physiol. Chem. 219 (1–2): 38–56. doi:10.1515/bchm2.1933.219.1-2.38.
  2. 1 2 3 4 5 6 Chandrasekaran, M.; Beena, P.S. (2013), "Tannase: source, biocatalytic characteristics, and bioprocesses for production", Marine Enzymes for Biocatalysis, Elsevier, pp. 259–293, doi:10.1533/9781908818355.3.259, ISBN   9781907568800 , retrieved 2021-10-21
  3. 1 2 3 4 5 6 7 Matoba, Y.; Tanaka, N.; Sugiyama, M. (2013-07-24). "Crystal structure of tannase from Lactobacillus plantarum in the orthorhombic crystal". Proteins: Structure, Function, and Bioinformatics. doi:10.2210/pdb3wa6/pdb . Retrieved 2021-10-03.
  4. 1 2 Haslam E, Stangroom JE (April 1966). "The esterase and depsidase activities of tannase". Biochem. J. 99 (1): 28–31. doi:10.1042/bj0990028. PMC   1264952 . PMID   5965343.
  5. 1 2 3 Yao, J.; Guo, G. S.; Ren, G. H.; Liu, Y. H. (2013). "Production, characterization and applications of tannase". Journal of Molecular Catalysis B: Enzymatic. 101: 137–147. doi:10.1016/j.molcatb.2013.11.018. ISSN   1381-1177 – via Elsevier.
  6. 1 2 Jana, A.; Halder, S. K.; Banerjee, A.; Paul, T.; Pati, B.R.; Mondal, K.C.; Das Mohapatra, P.K. (2014-04-01). "Biosynthesis, structural architecture and biotechnological potential of bacterial tannase: A molecular advancement". Bioresource Technology. 157: 327–340. Bibcode:2014BiTec.157..327J. doi:10.1016/j.biortech.2014.02.017. ISSN   0960-8524. PMID   24613317.
  7. ↑ PubChem. "Digallate". pubchem.ncbi.nlm.nih.gov. Retrieved 2021-10-21.
  8. ↑ PubChem. "Gallic acid". pubchem.ncbi.nlm.nih.gov. Retrieved 2021-10-21.
  9. 1 2 Ren, B.; Wu, M.; Wang, Q.; Peng, X.; Wen, H.; McKinstry, W.J.; Chen, Q. (2013). "Crystal Structure of Tannase from Lactobacillus plantarum". Journal of Molecular Biology. 425 (15): 2737–2751. doi:10.1016/j.jmb.2013.04.032. ISSN   0022-2836. PMID   23648840.
  10. ↑ "Tannins". www.fs.usda.gov. Retrieved 2024-05-02.
  11. ↑ "Medicinal Botany – Active Plant Ingredients". www.fs.fed.us. Retrieved 2021-10-21.
  12. 1 2 Bhat TK, Singh B, Sharma OP (1998). "Microbial degradation of tannins--a current perspective". Biodegradation. 9 (5): 343–57. doi:10.1023/A:1008397506963. PMID   10192896. S2CID   11466481.
  13. ↑ Matoba, Y.; Tanaka, N.; Noda, M.; Higashikawa, F.; Kumagai, T.; Sugiyama, M. (2013-08-23). "Crystallographic and mutational analyses of tannase from Lactobacillus plantarum". Proteins: Structure, Function, and Bioinformatics. 81 (11): 2052–2058. doi:10.1002/prot.24355. ISSN   0887-3585. PMID   23836494. S2CID   34843052.
  14. ↑ Chowdhury, S.P.; Khanna, S.; Verma, S.C.; Tripathi, A.K. (2004). "Molecular diversity of tannic acid degrading bacteria isolated from tannery soil". Journal of Applied Microbiology. 97 (6): 1210–1219. doi:10.1111/j.1365-2672.2004.02426.x. ISSN   1364-5072. PMID   15546412. S2CID   743583.
  15. ↑ de las Rivas, B.; Rodríguez, H.; Anguita, J.; Muñoz, R. (2019). "Bacterial tannases: classification and biochemical properties". Applied Microbiology and Biotechnology. 103 (2): 603–623. doi:10.1007/s00253-018-9519-y. hdl: 10261/203317 . ISSN   0175-7598. PMID   30460533. S2CID   253776893.
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