Degradation Of Tannins Research Articles

Degradation of industrial tannin and lignin from pulp mill effluent by aerobic granular sludge technology

Tannin and lignin from pulp and paper wastewater (PPW) are two compounds that have been proven to cause a variety of toxic effects in several aquatic species. Aerobic granular sludge (AGS) technology has emerged with strong potential to provide the desired treatment. This work presents the first attempt at the microbial degradation of these compounds using AGS technology, with promising results. Granules were cultivated within 9 days of operation of the sequencing batch reactor (SBR), with SVI30 of 51.6 mL/g, achieving steady-state within the first three weeks of operation. On average, COD removal efficiency was 90%. Granules cultivated from the SBR were transferred into a batch system with real pulp mill effluent. Tannin/lignin removal efficiency was 97% at an initial concentration of 50 mg/L, and slowly decreased to about 60% when the influent concentration increased to 100 mg/L. The most prominent species responsible for the degradation of these toxic substances were Pseudomonas, Corynebacteriaceae and Flavobacterium. These key findings demonstrate the capability of AGS to provide adequate treatment for PPW.

Recent trends and advancements in microbial tannase-catalyzed biotransformation of tannins: a review.

The outburst of green biotechnology has facilitated a substantial upsurge in the usage of enzymes in a plethora of industrial bioconversion processes. The tremendous biocatalytic potential of industrial enzymes provides an upper edge over chemical technologies in terms of safety, reusability, and better process control. Tannase is one such enzyme loaded with huge potential for bioconversion of hydrolysable tannins to gallic acid. Tannins invariably occur in pteridophytes, gymnosperms, and angiosperms and predominately cumulate in plant parts like fruits, bark, roots, and leaves. Furthermore, toxic tannery effluents from various tanneries are loaded with significant levels of tannins in the form of tannic acid. Tannase can be principally employed for debasing the tannins that predominately occur in the toxic tannery effluents thus providing a relatively much cheaper measure for their biodegradation. Over the years, microbial tannase-catalyzed tannin degradation has gained momentum. The plentious availability of tannin-containing agro- and industrial waste paves a way for efficient utilization of microbial tannase for tannin degradation eventually resulting into gallic acid production. Gallic acid has received a great deal of attention as a molecule of enormous therapeutic and indusrial potential. The current worldwide demand of gallic acid is 8000t per annum. As a matter of fact, bioconversion of tannins into gallic acid through fermentation has not been exploited completely. This necessitates further studies for development of more efficient, economical, productive processes and improved strains for gallic acid production so as to meet its current demand.

Degradation of euptox A by tannase-producing rumen bacteria from migratory goats.

The gut microbiota capable of degrading plant biomass and antinutritional phytometabolites are of immense importance. This study reports isolation and characterization of tannase-producing rumen bacteria that could also degrade euptox A (9-oxo-10,11-dehydroageraphorone) present in Eupatorium adenophorum (Spreng). Migratory Gaddi goats were selected as source of inoculums for isolating rumen bacteria with ability to produce tannase which catalyses degradation of hydrolysable tannins (HTs). Three rumen bacterial isolates producing tannase were studied, and identified as Klebsiella variicola strain PLP G-17 LC, K. variicola strain PLP S-18 and Klebsiella pneumoniae strain PLP G-17 SC. The isolates exhibited optimal tannase activity at 40°C, and pH 6·0. The bacteria could also degrade euptox A, a potent hepatotoxin in E. adenophorum Spreng, a widely distributed noxious weed. The rumen bacteria could degrade antinutritional HTs and euptox A. Culture-independent metagenomic interventions are envisioned to completely decipher the rumen microbial ecology and exploit its genetic and metabolic potential. The bacteria producing tannase which catalyses degradation of HTs, and concurrently degrading euptox A, may have potential as microbial feed additives to increase utilization of plant biomass containing antinutritional phytometabolites.

Rational engineering of p-hydroxybenzoate hydroxylase to enable efficient gallic acid synthesis via a novel artificial biosynthetic pathway.

Gallic acid (GA) is a naturally occurring phytochemical that has strong antioxidant and antibacterial activities. It is also used as a potential platform chemical for the synthesis of diverse high-value compounds. Hydrolytic degradation of tannins by acids, bases or microorganisms serves as a major way for GA production, which however, might cause environmental pollution and low yield and efficiency. Here, we report a novel approach for efficient microbial production of GA. First, structure-based rational engineering of PobA, a p-hydroxybenzoate hydroxylase from Pseudomonas aeruginosa, generated a new mutant, Y385F/T294A PobA, which displayed much higher activity toward 3,4-dihydroxybenzoic acid (3,4-DHBA) than the wild-type and any other reported mutants. Remarkably, expression of this mutant in Escherichia coli enabled generation of 1149.59 mg/L GA from 1000 mg/L 4-hydroxybenzoic acid (4-HBA), representing a 93% molar conversion ratio. Based on that, we designed and reconstituted a novel artificial biosynthetic pathway of GA and achieved 440.53 mg/L GA production from simple carbon sources in E. coli. Further enhancement of precursor supply through reinforcing shikimate pathway was able to improve GA de novo production to 1266.39 mg/L in shake flasks. Overall, this study not only led to the development of a highly active PobA variant for hydroxylating 3,4-DHBA into GA via structure-based protein engineering approach, but also demonstrated a promising pathway for bio-based manufacturing of GA and its derived compounds. Biotechnol. Bioeng. 2017;114: 2571-2580. © 2017 Wiley Periodicals, Inc.

Differential Gene Expression by Lactobacillus plantarum WCFS1 in Response to Phenolic Compounds Reveals New Genes Involved in Tannin Degradation.

Lactobacillus plantarum is a lactic acid bacterium that can degrade food tannins by the successive action of tannase and gallate decarboxylase enzymes. In the L. plantarum genome, the gene encoding the catalytic subunit of gallate decarboxylase (lpdC, or lp_2945) is only 6.5 kb distant from the gene encoding inducible tannase (L. plantarumtanB [tanBLp ], or lp_2956). This genomic context suggests concomitant activity and regulation of both enzymatic activities. Reverse transcription analysis revealed that subunits B (lpdB, or lp_0271) and D (lpdD, or lp_0272) of the gallate decarboxylase are cotranscribed, whereas subunit C (lpdC, or lp_2945) is cotranscribed with a gene encoding a transport protein (gacP, or lp_2943). In contrast, the tannase gene is transcribed as a monocistronic mRNA. Investigation of knockout mutations of genes located in this chromosomal region indicated that only mutants of the gallate decarboxylase (subunits B and C), tannase, GacP transport protein, and TanR transcriptional regulator (lp_2942) genes exhibited altered tannin metabolism. The expression profile of genes involved in tannin metabolism was also analyzed in these mutants in the presence of methyl gallate and gallic acid. It is noteworthy that inactivation of tanR suppresses the induction of all genes overexpressed in the presence of methyl gallate and gallic acid. This transcriptional regulator was also induced in the presence of other phenolic compounds, such as kaempferol and myricetin. This study complements the catalog of L. plantarum expression profiles responsive to phenolic compounds, which enable this bacterium to adapt to a plant food environment.IMPORTANCELactobacillus plantarum is a bacterial species frequently found in the fermentation of vegetables when tannins are present. L. plantarum strains degrade tannins to the less-toxic pyrogallol by the successive action of tannase and gallate decarboxylase enzymes. The genes encoding these enzymes are located close to each other in the chromosome, suggesting concomitant regulation. Proteins involved in tannin metabolism and regulation, such GacP (gallic acid permease) and TanR (tannin transcriptional regulator), were identified by differential gene expression in knockout mutants with mutations in genes from this region. This study provides insights into the highly coordinated mechanisms that enable L. plantarum to adapt to plant food fermentations.

Halotolerant Co-Cultured Bacterial Strains used in Degradation of Tannin Isolated from Tannery Industry Contaminated Sites

The residual tannins discharged from tanning units of the leather industry have an adverse effect on living organism and causes serious environmental pollution.

Expression, purification and immobilization of tannase from Staphylococcus lugdunensis MTCC 3614.

Enzymes find their applications in various industries, due to their error free conversion of substrate into product. Tannase is an enzyme used by various industries for degradation of tannin. Biochemical characterization of a specific enzyme from one organism to other is one of the ways to search for enzymes with better traits for industrial applications. Here, tannase encoding gene from Staphylococcus lugdunensis was cloned and suitability of the enzyme in various conditions was analysed to find its application in various industry. The recombinant protein was expressed with 6× His tag and purified using nickel affinity beads. The enzyme was purified up to homogeneity, with approximate molecular weight of 66 kDa. Purified tannase exhibited specific activity of about 716 U/mg. Optimum enzyme activity was found to be 40 °C at pH 7.0. Biochemical characterization revealed; metal ions such as Zn2+, Fe2+, Fe3+ and Mn2+ inhibited tannase activity, and SDS at lower concentration, increased tannase activity. Non polar organic solvents increased the tannase activity and polar solvents inhibited the tannase activity. Tannase immobilization studies show protection of the enzyme under wide range of pH and temperature. Also in this study we report a method for recovery and repeated use of the tannase.

Blastobotrys (Arxula) adeninivorans: a promising alternative yeast for biotechnology and basic research.

Blastobotrys adeninivorans (syn. Arxula adeninivorans) is a non-conventional, non-pathogenic, imperfect, haploid yeast, belonging to the subphylum Saccharomycotina, which has to date received comparatively little attention from researchers. It possesses unusual properties such as thermo- and osmotolerance, and a broad substrate spectrum. Depending on the cultivation temperature B. (A.) adeninivorans exhibits different morphological forms and various post-translational modifications and protein expression properties that are strongly correlated with the morphology. The genome has been completely sequenced and, in addition, there is a well-developed transformation/expression platform, which makes rapid, simple gene manipulations possible. This yeast species is a very good host for homologous and heterologous gene expression and is also a useful gene donor. Blastobotrys (A.) adeninivorans is able to use a very wide range of substrates as carbon and/or nitrogen sources and is an interesting organism owing to the presence of many metabolic pathways, for example degradation of n-butanol, purines and tannin. In addition, its unusual properties and robustness make it a useful bio-component for whole cell biosensors. There are currently a number of products on the market produced by B. (A.) adeninivorans and further investigation may contribute further innovative solutions for current challenges that exist in the biotechnology industry. Additionally it may become a useful alternative to existing commercial yeast strains and as a model organism in research. In this review we present information relevant to the exploitation of B. (A.) adeninivorans in research and industrial settings. Copyright © 2016 John Wiley & Sons, Ltd.

Isolation, Identification and Molecular Characterization of Tannase Producing Klebsiella sp., from the Rumen of Migratory Goats and Sheep

Tannase, so called Tannin Acyl Hydrolase (TAH) (E.C.3.1.1.20) is one of the versatile biocatalyst with several industrial applications. It is solely responsible for the degradation of hydrolysable tannin thus surpassing the untoward effects of high concentration of tannin consumption in the gut of small ruminants. In the locality of Palampur the migratory goats and sheep have the unique property to resist excess amount of tannin consumed by them. This is because of their ruminal microflora. The concept of ruminal microflora can be used as Direct Fed Microbial (DFM) gaining momentum now-a-days. Thus in the present study attempts were made to explore new source of tannase producing microbes from the rumen of goats and sheep. Rumen samples were collected over several places of Palampur, then processed and finally the most tannin tolerable cultures were selected. Their genomic DNA were isolated and subjected for 16S rRNA sequencing to characterize the isolates. From the molecular characterization we identified Klebsiella sp. as a novel source of tannase from the rumen of these migratory animals. This is the first report of a Klebsiella sp. from the rumen of migratory small ruminants capable of degrading forage tannin.

Unraveling the mechanism of thermal and thermo-oxidative degradation of tannic acid

The thermal and thermo-oxidative degradation of hydrolysable tannin, i.e. tannic acid is reported. The study on thermal and thermo-oxidative degradation mechanism of tannic acid was carried out by using several advanced thermal characterization techniques such as Thermogravimetric analysis (TGA) coupled with Fourier-Transform Infrared (FTIR) Spectroscopy (TGA–FTIR), pyrolysis–gas chromatography–mass spectroscopy (Py–GC–MS) and Attenuated Total Reflectance (ATR)–FTIR. The condensed phase and gaseous phase degradation studies were combined to deduce a probable degradation pathway for tannic acid molecule at high temperature under nitrogen and air atmosphere.

Anaerobic degradation of tannins in Acacia nilotica pods by Enterococcus faecalis in co-culture with ruminal microbiota.

Anaerobic degradation of tannins in Acacia nilotica pods by Enterococcus faecalis in co-culture with ruminal microbiota.

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

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.

Biodegradation of coffee pulp tannin by Penicillium verrucosum for production of tannase, statistical optimization and its application

Coffee pulp is a primary by-product produced during coffee processing and represents 30% of the coffee fruit on a dry-weight basis. A novel potential tannin degrading fungi was isolated from coffee by-products. Among the various fungi isolated, Penicillium sp. CFR303 was found to be potent with 66.5±0.9% tannin degradation. The potent tannin degrader was identified as Penicillium verrucosum using internal transcribed spacer's (ITS) −5.8S rDNA analysis. Solid state fermentation was carried out on coffee pulp as a sole carbon source and yielded 28.173±1.4U/gds of tannase. Further, 3.93 fold increase in tannase production (115.995U/gds) was achieved using central composite rotatable design, a statistical approach. Model validations showed excellent agreement between the experimental results and the predicted responses with a confidence level of 95%. Coffee pulp accounts to 8–10% tannin content and the present study demonstrates coffee pulp as an excellent substrate for production of value added products. Aonla and pomegranate juice were treated with partially purified tannase and the degradation of tannins was evident by changes in the physicochemical parameters of the juice. Thus, the present investigation signifies utilization of coffee pulp for production of tannase as value addition and its potential application in the food industry.

Degrading Mimosine and Tannins of <i>Leucaena l</i><i>e</i><i>ucocephala</i> by Ensiling

Lucaena (Leucaena leucocephala) is a valuable fodder tree, but it contains high contents of anti-nutritional factors, such as mimosine and tannins. The present study investigated the silage fermentation characteristics and ensiling effects on the degradation of mimosine and tannins of leucaena. Mimosine and tannins gradually reduced during ensiling, and sucrose and lactic acid bacteria (LAB) addition promoted their degradation. The highest degradation rate of mimosine was 49.0% in sucrose treatment and the lowest was 25.5% in the control. The highest degradation rate of tannins was 54.7% in the combined treatment of sucrose and LAB and the lowest was 40% in the control. The degradation rates of mimosine and tannins had negative correlation with the pH value and had positive correlation with lactic acid content in silage.

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

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

Distribution of insoluble polysaccharides in the shoot apex of Rhododendron arboreum Linn. during the annual growth cycle

Starch grains occur all over the dormant shoot apex of <em>Rhododendron arboreum</em> except in the bud scales. They are abundant in the peripheral, rib and pith meristem cells. as well as in the youngest leaf primordia. Tannin is present in the entire dormant bud hut for the cells of the apical meristem and leaf primordia. Gradually, tannin degradation into numerous globules occurs. This is concomitant with the disappearance of starch grains and indicates the earliest structural manifestation of spring awakening by meristematic activity in the buds. The weak affinity of tannin globules to PAS is due to their hydrolysis which releases glucose for metabolic activities. Thus, a parallelism seems to exist between the metabolism of tannins and starch in relation to the various phases of bud development.

Redeeming Pieter Coecke van Aelst’s Gluttony Tapestry: Learning from Scientific Analysis

Previous articleNext article No AccessRedeeming Pieter Coecke van Aelst’s Gluttony Tapestry: Learning from Scientific AnalysisFederico Carò, Giulia Chiostrini, Elizabeth Cleland, and Nobuko ShibayamaFederico CaròAssociate Research Scientist, Department of Scientific Research, The Metropolitan Museum of Art Search for more articles by this author , Giulia ChiostriniAssistant Conservator, Department of Textile Conservation, The Metropolitan Museum of Art Search for more articles by this author , Elizabeth ClelandAssociate Curator, Department of European Sculpture and Decorative Arts, The Metropolitan Museum of Art Search for more articles by this author , and Nobuko ShibayamaAssociate Research Scientist, Department of Scientific Research, The Metropolitan Museum of Art Search for more articles by this author PDFPDF PLUSFull Text Add to favoritesDownload CitationTrack CitationsPermissionsReprints Share onFacebookTwitterLinkedInRedditEmail SectionsMoreDetailsFiguresReferencesCited by Metropolitan Museum Journal Volume 492014 Sponsored by the Metropolitan Museum of Art Article DOIhttps://doi.org/10.1086/680030 Views: 84Total views on this site Citations: 2Citations are reported from Crossref © 2014 by The Metropolitan Museum of ArtPDF download Crossref reports the following articles citing this article:Sluyts Yannick, Vanderveken Anneleen, Maekelberg Sanne, Rychtarikova Monika, De Jonge Krista An archeoacoustic reconstruction of The great hall of the Palace of Binche (1545-1554), (Sep 2021): 1–8.https://doi.org/10.1109/I3DA48870.2021.9610841 Degano, Mattonai, Sabatini, Colombini A Mass Spectrometric Study on Tannin Degradation within Dyed Woolen Yarns, Molecules 24, no.1212 (Jun 2019): 2318.https://doi.org/10.3390/molecules24122318

Study on the Inhibitory Effect of Bayberry Tannin Extract on Anaerobic Fermentation

Concerning the treatment of tannery wastewater with high COD (chemical oxygen demand), the effective process is physical-chemical and anaerobic treatment. The core technology of anaerobic treatment is to test the performance of anaerobic degradation of organic matter, clarify the inhibitory effect and inhibitory mechanism of pollutant. In this paper, anaerobic degradation and inhibitory effect of bayberry tannin extract were studied. In the course of the experiment, the production of methane, the activity of sludge and the content of coenzyme F420 were been tested, the bayberry tannin extract and degradation products were been tested by Fourier transform infrared spectroscopy (FT-IR). The results indicated that the 50% inhibitory concentration of bayberry tannin extract is about 3.3 g/L, the anaerobic fermentation has been inhibited is owing to bayberry tannin extract has the inhibition on methanogenic activity of methanogens, the production of methane, the activity of sludge and the content of coenzyme F420 are getting lower and lower with the increase in content of bayberry tannin extract. The characterization of FTIR showed that the bayberry tannin extract has been degraded in anaerobic fermentation. These all indicated that bayberry tannin extract can inhibit the anaerobic fermentation, and the greater amount, resulting in stronger inhibition, in appropriate concentrations, bayberry tannin extract can be degraded by anaerobic fermentation. The results can provide guidance for anaerobic treatment of tannery wastewater with high COD.

Enhanced tannase production by Bacillus subtilis PAB2 with concomitant antioxidant production

Abstract The present study was aimed at finding the optimal conditions for tannin biodegradation by Bacillus subtilis PAB2, a newly isolated soil bacterium, and to study its fermentative byproducts. Tannase production by B. subtilis PAB2 in optimum level was studied by one variable at a time (OVAT) approach followed by Box–Behnken response surface methodology (RSM) using six important variables. The maximum tannase production (10.69 U/ml) was achieved in the presence of 0.47% (w/v) tannic acid, 0.23% (w/v) ammonium chloride (NH 4 Cl), 0.1% (w/v) potassium dihydrogen phosphate (KH 2 PO 4 ) and 0.046% (w/v) magnesium sulphate (MgSO 4 ) with the initial medium pH of 5.9 and incubation at 34.1 °C for 36 h under shaking condition (120 rpm). An overall 2.06 fold increase in tannase production was achieved after RSM global formulation. One of the major end product of tannin degradation i.e. gallic acid, was accumulated in the highest level (6.45 mg/ml) in 36 h of fermentation. Liquid chromatography and mass spectroscopy results indicated the presence of both gallic acid and pyrogallol in the fermentative end product. Purification of gallic acid and pyrogallol was achieved through high pressure liquid chromatography followed by crystallization and confirmed by Fourier transform infrared spectroscopy. Associated production of tannase as well as gallic acid and pyrogallol by B. subtilis PAB2 makes it obvious in different biotechnological interest.

Uncovering the Lactobacillus plantarum WCFS1 gallate decarboxylase involved in tannin degradation.

Lactobacillus plantarum is a lactic acid bacterium able to degrade tannins by the subsequent action of tannase and gallate decarboxylase enzymes. The gene encoding tannase had previously been identified, whereas the gene encoding gallate decarboxylase is unknown. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of gallic-acid induced L. plantarum extracts showed a 54-kDa protein which was absent in the uninduced cells. This protein was identified as Lp_2945, putatively annotated UbiD. Homology searches identified ubiD-like genes located within three-gene operons which encoded the three subunits of nonoxidative aromatic acid decarboxylases. L. plantarum is the only bacterium in which the lpdC (lp_2945) gene and the lpdB and lpdD (lp_0271 and lp_0272) genes are separated in the chromosome. Combination of extracts from recombinant Escherichia coli cells expressing the lpdB, lpdC, and lpdC genes demonstrated that LpdC is the only protein required to yield gallate decarboxylase activity. However, the disruption of these genes in L. plantarum revealed that the lpdB and lpdC gene products are essential for gallate decarboxylase activity. Similar to L. plantarum tannase, which exhibited activity only in esters derived from gallic and protocatechuic acids, purified His6-LpdC protein from E. coli showed decarboxylase activity against gallic and protocatechuic acids. In contrast to the tannase activity, gallate decarboxylase activity is widely present among lactic acid bacteria. This study constitutes the first genetic characterization of a gallate decarboxylase enzyme and provides new insights into the role of the different subunits of bacterial nonoxidative aromatic acid decarboxylases.