Biotechnological Advances and Challenges of Tannase: An Overview

Chávez‐González, Mónica L.; Rodríguez‐Durán, Luis V.; Balagurusamy, Nagamani; Prado-Barragán, Arely; Rodríguez, Raúl; Contreras, Juan C.; Aguilar, Cristóbal N.

doi:10.1007/s11947-011-0608-5

Cited by 109 publications

(75 citation statements)

References 108 publications

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“…In relation to tannase substrates, it has been described that only the esters derived from gallic and protocatechuic acids were hydrolyzed (5,6,39,40,43). It seems that other hydroxybenzoic acids without hydroxyl groups and with substituents other than OH or OOH at position 2 are not metabolized by bacterial tannases.…”

Section: Methodsmentioning

confidence: 99%

A Lactobacillus plantarum Esterase Active on a Broad Range of Phenolic Esters

Esteban-Torres

Landete

Reverón

et al. 2015

Appl Environ Microbiol

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bLactobacillus plantarum is the lactic acid bacterial species most frequently found in the fermentation of food products of plant origin on which phenolic compounds are abundant. L. plantarum strains showed great flexibility in their ability to adapt to different environments and growth substrates. Of 28 L. plantarum strains analyzed, only cultures from 7 strains were able to hydrolyze hydroxycinnamic esters, such as methyl ferulate or methyl caffeate. As revealed by PCR, only these seven strains possessed the est_1092 gene. When the est_1092 gene was introduced into L. plantarum WCFS1 or L. lactis MG1363, their cultures acquired the ability to degrade hydroxycinnamic esters. These results support the suggestion that Est_1092 is the enzyme responsible for the degradation of hydroxycinnamic esters on the L. plantarum strains analyzed. The Est_1092 protein was recombinantly produced and biochemically characterized. Surprisingly, Est_1092 was able to hydrolyze not only hydroxycinnamic esters, since all the phenolic esters assayed were hydrolyzed. Quantitative PCR experiments revealed that the expression of est_1092 was induced in the presence of methyl ferulate, an hydroxycinnamic ester, but was inhibited on methyl gallate, an hydroxybenzoic ester. As Est_1092 is an enzyme active on a broad range of phenolic esters, simultaneously possessing feruloyl esterase and tannase activities, its presence on some L. plantarum strains provides them with additional advantages to survive and grow on plant environments. Lactobacillus plantarum is a highly versatile lactic acid bacterial species found in many different ecological niches, such as vegetables, meat, fish, and dairy products, as well as in the gastrointestinal tract (1). The genome of L. plantarum strain WCFS1 was the first to be fully sequenced, and it was, in fact, the first of any of the Lactobacillus genomes to be published (2). When the genome diversity of L. plantarum on a full genome scale was analyzed, it was revealed that L. plantarum strains are predicted to lack 9 to 20% of the genes of the L. plantarum WCFS1 reference genome, and about 50 genes appeared to be specific to strain WCFS1, as they were not found in any other strain (1). This variability confirms the flexibility of L. plantarum in its ability to adapt to different environments and growth substrates.Phenolic compounds are important constituents of food products of plant origin, as they are related to the sensory characteristics of the food and are beneficial to consumer health (3). Therefore, it is interesting to know the metabolic pathways of biosynthesis or degradation of these compounds in bacteria. L. plantarum is the lactic acid bacterium that is the most frequently found in the fermentation of food products of plant origin, being the bacterial model for the study of phenolic compound metabolism (4). Among these compounds, the metabolism of phenolic esters is greatly relevant, as they are widely spread throughout the plant kingdom (3). Esters of phenolic acids mainly belong to two distingui...

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Section: Methodsmentioning

confidence: 99%

A Lactobacillus plantarum Esterase Active on a Broad Range of Phenolic Esters

Esteban-Torres

Landete

Reverón

et al. 2015

Appl Environ Microbiol

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“…Tannase belongs to the superfamily of esterases. Since its discovery, tannase has found wide applications in the food, feed, beverage, pharmaceutical, and chemical industries (5). Despite the extensive interest and long history of the study of tannase, there is surprisingly little knowledge about the enzyme at the molecular level, which has become one of the critical factors that limit the large-scale application of tannase.…”

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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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“…Among the filamentous fungi, Aspergillus is considered the genus that best produces tannase, followed by the genus Penicillium, whether by means of submerged fermentation (SmF) or solid state fermentation (SSF) (Aguilar et al, 2007;Renovato et al, 2011;Chávez-González et al, 2012;Costa et al, 2012)). However, although the potential has been proven of species of the genus Penicillium to produce tannase, studies are still scarce.…”

Section: Introductionmentioning

confidence: 99%

Promising substrates to increase the production of tannase under solid state fermentation (SSF) by Penicillium spp.

Cruz¹,

Lima²,

Fonseca³

et al. 2017

Afr. J. Biotechnol.

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Tannase (tannin acyl hydrolse, E.C.3.1.1.20) is an enzyme that catalyzes the hydrolysis of ester and depside bonds of hydrolysable tannins. Among the filamentous fungi, the genus Penicillium is recognized as the second best producer of tannase. This enzyme presents applications in several industrial segments, such as in the production of judges and teas. The industrial production of tannase can be performed through solid state fermentation (SSF) by the use of tannin rich fruit residues, in order to minimize production costs. In the present study 31 species of Penicillium isolated from Caatinga and Atlantic Forest were tested quantitatively for the production of tannase. The species were kept in the Collection of Cultures Micoteca -URM (WDCM604) under mineral oil. The enzyme production was carried out under SSF using "cajá" (Spondias lutea L.) and Manga (Mangifera indica L.) residues that are rich in tannins. Mango residue proved to be the best inducer of the production of tannase by Penicillium species, most of which presented high tannase activity, ranging from 14.48 to 89.48 U mL . Therefore, P. rolfssi URM6216 is being indicated for optimization of tannase production by SSF, using mango residue as a substrate. This is the first study on the potential of hog-plum (cajá) and mango wastes as substrates for tannase production by filamentous fungi.

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Biotechnological Advances and Challenges of Tannase: An Overview

Cited by 109 publications

References 108 publications

A Lactobacillus plantarum Esterase Active on a Broad Range of Phenolic Esters

A Lactobacillus plantarum Esterase Active on a Broad Range of Phenolic Esters

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

Promising substrates to increase the production of tannase under solid state fermentation (SSF) by Penicillium spp.

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