Purification and characterization of tannase from Paecilomyces variotii: hydrolysis of tannic acid using immobilized tannase

Mahendran, B.; Raman, N.; Kim, D.-J.

doi:10.1007/s00253-005-0082-y

Cited by 86 publications

(59 citation statements)

References 20 publications

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“…This observation is comparable with the earlier study by Mahendran et al [36] which showed that purified tannase from P. varoitii was present in a monomeric form the specific detection of tannase activity on the SDS-PAGE during zymogram analysis. Previously, Lactobacillus plantarum and K. pneumonia tannase were also found to be a monomer with a molecular mass of 46.5 and 50 kDa, respectively [37,38].…”

Section: Discussionsupporting

confidence: 82%

Digestion of Tannin by Bacteria Enterobacter cloacae from the Gut of Indian Mole Cricket (Gryllotalpa krishnani)

RK¹,

Revathi²,

Rameshkumar³

et al. 2017

J Bioprocess Biotech

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Insects are the most successful animal on earth; the gut microbes present might play an important role in food digestion as well as the interaction with hosts. In this study insect Gryllotalpa krishnani has been used to isolate the symbiotic associated organisms which play role in host metabolism, promote efficient digestion and to protect the host from the harmful microbes. In the present study, microorganisms were isolated from the gut of G. krishnani and characterized for tannase enzyme activity. It was observed that 5 isolates (TAH 6, TAH 13, TAH 36, TAH 38 and TAH 41) out of total 120 tested were able to show significant growth on tannic acid plate. Among these five potential isolates, strain TAH 41 exhibited maximum tannase activity in tannase plate assay and was selected for the further study. The bacterial strain TAH41 was analyzed for biochemical analysis, 16S rDNA sequencing and the result confirmed the strain as Enterobacter cloacae. HPLC analysis showed the formation two peaks representing gallic acid and glucose as a by-product FT-IR analysis also confirmed the same. The polyacrylamide gel electrophoresis (SDS-PAGE) and zymogram analysis showed the molecular mass of tannase enzyme in cell free extract was ~45 kDa, the analysis suggested this tannase enzyme to be one of the smallest of the bacterial source, which could be attributed to the formation of di or tri-galloyl glucose. The present study was the first report E. cloacae with tannase activity from G. krishnani gut. E. cloacae which may endow the insect with some ecological advantages by enabling them to overcome the anti-nutritional effects of plant tannins.Citation: Rasiravuthanahalli KG, Revathi S, Rameshkumar N, Krishnan M, Kayalvizhi N (2017) Digestion of Tannin by Bacteria Enterobacter cloacae from the Gut of Indian Mole Cricket (Gryllotalpa krishnani).

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Section: Discussionsupporting

confidence: 82%

Digestion of Tannin by Bacteria Enterobacter cloacae from the Gut of Indian Mole Cricket (Gryllotalpa krishnani)

RK¹,

Revathi²,

Rameshkumar³

et al. 2017

J Bioprocess Biotech

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“…For example, the Paecilomyces variotii tannase is a monomeric enzyme with a molecular mass of only 45 kDa (Mahendran et al, 2006), whereas the A. oryzae tannase is an octamer, consisting of four identical heterodimeric units (Hatamoto et al, 1996) and the same tannase produced by P. pastoris forms single heterodimers (Zhong et al, 2004). The molecular mass of the native, glycosylated A. adeninivorans tannase was estimated here to be 320 kDa, implying that it comprises four subunits with molecular sizes of about 80 kDa.…”

Section: Discussionmentioning

confidence: 99%

Atan1p—an extracellular tannase from the dimorphic yeast Arxula adeninivorans: molecular cloning of the ATAN1 gene and characterization of the recombinant enzyme

Böer¹,

Bode²,

Mock³

et al. 2009

Yeast

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The tannase-encoding Arxula adeninivorans gene ATAN1 was isolated from genomic DNA by PCR, using as primers oligonucleotide sequences derived from peptides obtained after tryptic digestion of the purified tannase protein. The gene harbours an ORF of 1764 bp, encoding a 587-amino acid protein, preceded by an N-terminal secretion sequence comprising 28 residues. The deduced amino acid sequence was similar to those of tannases from Aspergillus oryzae (50% identity), A. niger (48%) and putative tannases from A. fumigatus (52%) and A. nidulans (50%). The sequence contains the consensus pentapeptide motif (-Gly-X-Ser-X-Gly-) which forms part of the catalytic centre of serine hydrolases. Expression of ATAN1 is regulated by the carbon source. Supplementation with tannic acid or gallic acid leads to induction of ATAN1, and accumulation of the native tannase enzyme in the medium. The enzymes recovered from both wild-type and recombinant strains were essentially indistinguishable. A molecular mass of ∼320 kDa was determined, indicating that the native, glycosylated tannase consists of four identical subunits. The enzyme has a temperature optimum at 35-40• C and a pH optimum at ∼6.0. The enzyme is able to remove gallic acid from both condensed and hydrolysable tannins. The wildtype strain LS3 secreted amounts of tannase equivalent to 100 U/l under inducing conditions, while the transformant strain, which overexpresses the ATAN1 gene from the strong, constitutively active A. adeninivorans TEF1 promoter, produced levels of up to 400 U/l when grown in glucose medium in shake flasks.

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“…The crude tannase from Paecilomyces variotii was stable in a temperature range from 20 to 50 °C, in which it retained 99 and 96 % residual activity at 20 and 50 °C, respectively (13). The thermal stability profi le of crude tannase from Penicillium notatum NCIM 923 revealed that above 95 % was retained at 40 °C (53).…”

Section: Tannase Thermal Stabilitymentioning

confidence: 99%

“…Tannic acid, for example, is a hydrolysable tannin, which can be hydrolyzed by tannase to gallic acid and glucose. Among its applications are: preparation of instant tea (8), manufacture of beverages (juices, beer and wine) (11), production of gallic and ellagic acids (12), ester synthesis and effl uent processing (13), and as an additive for animal feed (14).…”

Section: Introductionmentioning

confidence: 99%

Production, Characterization and Application of a Thermostable Tannase from Pestalotiopsis guepinii URM 7114

Sena¹,

Santos

Gouveia

et al. 2014

Food. Technol. Biotechnol.

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SummaryTannase (EC 3.1.1.20) is an enzyme that hydrolyzes the ester and depside bonds of tannic acid to gallic acid and glucose. In the production of foods and beverages, it contributes to the removal of the undesirable eff ects of tannins. The aim of this study is to investigate the potential of endophytic fungi isolated from jamun (Syzygium cumini (L.) Skeels) leaves, and identifi ed as Pestalotiopsis guepinii, in the production of tannase. Tannase was produced extracellularly by P. guepinii under submerged, slurry-state and solid-state fermentations. The submerged fermentation was found to be the most promising (98.6 U/mL). Response surface methodology was employed to evaluate the eff ect of variables (pH and temperature), and the results showed that the best conditions for tannase activity were pH=6.9 and 30 °C. K m was found to be 7.18·10 -4 mol/L and v max =250.00 U/mL. The tannase activity was the highest in the presence of Ca 2+ at a concentration of 5·10 -3 mol/L. Moreover, the enzyme was not inhibited by the tested chelators and detergents. The stability of the enzyme was also studied, and crude enzyme was evaluated in simulation of gastrointestinal digestion of monogastric animals. The crude enzyme was highly stable under simulated conditions; it retained 87.3 % of its original activity a er 6 h. The study contributes to the identifi cation of microbial species that produce tannase, with potential application in biotechnology.

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Purification and characterization of tannase from Paecilomyces variotii: hydrolysis of tannic acid using immobilized tannase

Cited by 86 publications

References 20 publications

Digestion of Tannin by Bacteria Enterobacter cloacae from the Gut of Indian Mole Cricket (Gryllotalpa krishnani)

Digestion of Tannin by Bacteria Enterobacter cloacae from the Gut of Indian Mole Cricket (Gryllotalpa krishnani)

Atan1p—an extracellular tannase from the dimorphic yeast Arxula adeninivorans: molecular cloning of the ATAN1 gene and characterization of the recombinant enzyme

Production, Characterization and Application of a Thermostable Tannase from Pestalotiopsis guepinii URM 7114

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