Crystal Structure of Tannase from Lactobacillus plantarum

Ren, Bin; Wu, Mingbo; Wang, Qin; Peng, Xiaohong; Wen, Hui; McKinstry, William J.; Chen, Qianming

doi:10.1016/j.jmb.2013.04.032

Cited by 54 publications

(62 citation statements)

References 47 publications

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“…In both TanA proteins Asp-419 is substituted by a Gln residue. This amino acid variation was noticed previously and suggested that the conserved residue Asp-421 may fulfil the role of Asp-419 as the acidic residue of the catalytic triad [17]. The residues identified that make contacts with the three hydroxyl groups of gallic acid (Asp-421, Lys-343, and Glu-357, in TanB Lp ) are conserved in all the tannase proteins analyzed (Additional file 1: Figure S1A).…”

Section: Resultssupporting

confidence: 70%

“…The identity degree among TanA and TanB proteins is lower than 30%. The comparison of the amino acid sequence of these tannase proteins with TanB Lp , whose tridimensional structure have been recently solved [17], revealed that the residues important for activity are conserved. All the analyzed proteins possessed the conserved motif Gly-X-Ser-X-Gly typical of serine hydrolases.…”

Section: Resultsmentioning

confidence: 99%

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Genetic and biochemical approaches towards unravelling the degradation of gallotannins by Streptococcus gallolyticus

et al. 2014

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BackgroundHerbivores have developed mechanisms to overcome adverse effects of dietary tannins through the presence of tannin-resistant bacteria. Tannin degradation is an unusual characteristic among bacteria. Streptococcus gallolyticus is a common tannin-degrader inhabitant of the gut of herbivores where plant tannins are abundant. The biochemical pathway for tannin degradation followed by S. gallolyticus implies the action of tannase and gallate decarboxylase enzymes to produce pyrogallol, as final product. From these proteins, only a tannase (TanBSg) has been characterized so far, remaining still unknown relevant proteins involved in the degradation of tannins.ResultsIn addition to TanBSg, genome analysis of S. gallolyticus subsp. gallolyticus strains revealed the presence of an additional protein similar to tannases, TanASg (GALLO_0933). Interestingly, this analysis also indicated that only S. gallolyticus strains belonging to the subspecies “gallolyticus” possessed tannase copies. This observation was confirmed by PCR on representative strains from different subspecies. In S. gallolyticus subsp. gallolyticus the genes encoding gallate decarboxylase are clustered together and close to TanBSg, however, TanASg is not located in the vicinity of other genes involved in tannin metabolism. The expression of the genes enconding gallate decarboxylase and the two tannases was induced upon methyl gallate exposure. As TanBSg has been previously characterized, in this work the tannase activity of TanASg was demonstrated in presence of phenolic acid esters. TanASg showed optimum activity at pH 6.0 and 37°C. As compared to the tannin-degrader Lactobacillus plantarum strains, S. gallolyticus presented several advantages for tannin degradation. Most of the L. plantarum strains possessed only one tannase enzyme (TanBLp), whereas all the S. gallolytcius subsp. gallolyticus strains analyzed possesses both TanASg and TanBSg proteins. More interestingly, upon methyl gallate induction, only the tanBLp gene was induced from the L. plantarum tannases; in contrast, both tannase genes were highly induced in S. gallolyticus. Finally, both S. gallolyticus tannase proteins presented higher activity than their L. plantarum counterparts.ConclusionsThe specific features showed by S. gallolyticus subsp. gallolyticus in relation to tannin degradation indicated that strains from this subspecies could be considered so far the best bacterial cellular factories for tannin degradation.Electronic supplementary materialThe online version of this article (doi:10.1186/s12934-014-0154-8) contains supplementary material, which is available to authorized users.

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Section: Resultssupporting

confidence: 70%

Section: Resultsmentioning

confidence: 99%

Genetic and biochemical approaches towards unravelling the degradation of gallotannins by Streptococcus gallolyticus

et al. 2014

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“…One more simulation was conducted in the same way with tannase, which has six residues in the active sites of Ser163, Lys343, Glu357, Asp419, Asp421, and His451. As shown in Figure 7B, the GA moiety of EGCG interacts with Ser163 and Asp421, as reported by Ren et al [32] In the case of isoquercitrin with tannase, a similar conformation of isoquercitrin in the active site is obtained, which indirectly indicates the possibility of hydrolysis of the glucose moiety of isoquercitrin. These docking simulations (refer to Table S4 for the result of the docking run) may provide insights into the simultaneous catalytic actions of the two enzymes used in our study, although the exact enzyme structures of enzyme CF and tannase from A. niger were not obtained.…”

Section: Rationale Of the Enzymatic Reactions From Molecular Docking supporting

confidence: 80%

Simultaneous Optimal Production of Flavonol Aglycones and Degalloylated Catechins from Green Tea Using a Multi-Function Food-Grade Enzyme

Rha

Kim²,

Byoun

et al. 2019

Catalysts

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1) Background: Green tea (GT) contains well-known phytochemical compounds; namely, it is rich in flavan-3-ols (catechins) and flavonols comprising all glycoside forms. These compounds in GT might show better biological activities after a feasible enzymatic process, and the process on an industrial scale should consider enzyme specificity and cost-effectiveness. (2) Methods: In this study, we evaluated the most effective method for the enzymatic conversion of flavonoids from GT extract. One enzyme derived from Aspergillus niger (molecular weight 80-90 kDa) was ultimately selected, showing two distinct but simultaneous activities: intense glycoside hydrolase activity via deglycosylation and weak tannin acyl hydrolase activity via degalloylation. (3) Results: The optimum conditions for producing flavonol aglycones were pH 4.0 and 50 • C. Myricetin glycosides were cleaved 3.7-7.0 times faster than kaempferol glycosides. Flavonol aglycones were produced effectively by both enzymatic and hydrochloride treatment in a time-course reaction. Enzymatic treatment retained 80% (w/w) catechins, whereas 70% (w/w) of catechins disappeared by hydrochloride treatment. (4) Conclusions: This enzymatic process offers an effective method of conditionally producing flavonol aglycones and de-galloylated catechins from conversion of food-grade enzyme.

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“…The optimum pH value for tannase activity was determined by studying its pH dependence within the pH range between 3 and 10. Acetic acid-sodium acetate buffer was used for pH 3 to 5, citric acid-sodium citrate buffer for pH 6, sodium phosphate buffer for pH 7, Tris-HCl buffer for pH 8, glycine-NaOH buffer for pH 9, and sodium carbonate-bicarbonate for pH 10. A 100 mM concentration was used in all the buffers.…”

Section: Methodsmentioning

confidence: 99%

“…(9). In addition, L. plantarum tannase has been biochemically and structurally characterized (7,8,10).…”

mentioning

confidence: 99%

Tannin Degradation by a Novel Tannase Enzyme Present in Some Lactobacillus plantarum Strains

Jiménez

Esteban-Torres

Mancheño

et al. 2014

Appl Environ Microbiol

107

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bLactobacillus plantarum is frequently isolated from the fermentation of plant material where tannins are abundant. L. plantarum strains possess tannase activity to degrade plant tannins. An L. plantarum tannase (TanB Lp , formerly called TanLp1) was previously identified and biochemically characterized. In this study, we report the identification and characterization of a novel tannase (TanA Lp ). While all 29 L. plantarum strains analyzed in the study possess the tanB Lp gene, the gene tanA Lp was present in only four strains. Upon methyl gallate exposure, the expression of tanB Lp was induced, whereas tanA Lp expression was not affected. TanA Lp showed only 27% sequence identity to TanB Lp , but the residues involved in tannase activity are conserved. Optimum activity for TanA Lp was observed at 30°C and pH 6 in the presence of Ca 2؉ ions. TanA Lp was able to hydrolyze gallate and protocatechuate esters with a short aliphatic alcohol substituent. Moreover, TanA Lp was able to fully hydrolyze complex gallotannins, such as tannic acid. The presence of the extracellular TanA Lp tannase in some L. plantarum strains provides them an advantage for the initial degradation of complex tannins present in plant environments.

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Crystal Structure of Tannase from Lactobacillus plantarum

Cited by 54 publications

References 47 publications

Genetic and biochemical approaches towards unravelling the degradation of gallotannins by Streptococcus gallolyticus

Genetic and biochemical approaches towards unravelling the degradation of gallotannins by Streptococcus gallolyticus

Simultaneous Optimal Production of Flavonol Aglycones and Degalloylated Catechins from Green Tea Using a Multi-Function Food-Grade Enzyme

Tannin Degradation by a Novel Tannase Enzyme Present in Some Lactobacillus plantarum Strains

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