Microbial Production of Tannase: State of the Art

Belur, Prasanna D.; Mugeraya, Gopal

doi:10.3923/jm.2011.25.40

Cited by 64 publications

(43 citation statements)

References 35 publications

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“…Previously, it has been claimed that tannase production is performed by only a few microorganisms. However, other studies have identified that this enzyme is produced by more than 70 species, and the number is increasing as a result of the continuing search for new sources of this enzyme (25). Fungi from the Aspergillus and Penicillium genus and lactic acid bacteria mostly produce tannase.…”

Section: Discussionmentioning

confidence: 99%

A New Native Source of Tannase Producer, Penicillium sp. EZ-ZH190: Characterization of the Enzyme

et al. 2013

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Background: Tannase can be obtained from the various sources for example tannin rich plants; however microbial sources are preferred for industrial production. In microbial sources, the Aspergillus and Penicillium genus and lactic acid bacteria mostly produce tannase. However, it has been identified that this enzyme is produced by many fungi and bacteria, but researches are continuing to find new species. Objectives: The aim of this study was to isolate a tannase-producing fungi from moldy tea leaves and to study some properties of its enzyme. Materials and Methods:The present study was done via two steps. At first, industrially important tannaseproducing fungi were isolated from moldy tea leaves using the simple agar plate method followed by the screening of organisms capable of producing tannase using the enrichment culture technique in modified Czapek Dox's agar. Finally, tannase obtained from the best isolate was partially purified and characterized. Results: Tannase produced by Penicillium sp. EZ-ZH190 isolated from moldy tea leaves was partially purified and characterized. Maximum enzyme production (4.33 U.mL -1 ) was recorded after 96 hours of incubation at 30 °C in submerged culture (100 rpm) utilizing 1 % (w/v) tannic acid as a sole carbon source. This tannase exhibited optimum activity at 35 °C and at pH of 5.5, and showed nearly 50 % of its maximal activity at 50 °C. In the present study, tannase from Penicillium sp. EZ-ZH190 had KM and Vmax values of 1.24 mM and 17.09 U.mL -1 , respectively, and showed more than 50 % stability at salt (NaCl) concentration of 1 M for 24 hours. Conclusions: Tannase productivity of Penicillium sp. EZ-ZH190 (0.045 U.mL -1 .h -1 ) is comparable with the maximum tannase productivity in the reported literatures, and the biochemical characteristics showed by Penicillium sp. EZ-ZH190 tannase are considered favorable for tannin biodegradation in the industry. So, we concluded that Penicillium sp. EZ-ZH190 is a good strain for use in the efficient production of tannase.

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Section: Discussionmentioning

confidence: 99%

A New Native Source of Tannase Producer, Penicillium sp. EZ-ZH190: Characterization of the Enzyme

et al. 2013

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“…However, other compounds such as gallic acid, ethyl gallate, isoamyl gallate, propyl gallate and methyl gallate have also been reported to possess inductive properties. However, inhibition of the formation of tannase by catabolite repression or feedback inhibition can be observed (15,65).…”

Section: Simulation Of In Vitro Digestionmentioning

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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“…The operational stability of immobilized tannase is the most important factor affecting the release of gallic acid in tannin bioconversion and in other industrial applications in food, beverage and juices to remove the undesirable effects of tannins such as astringency, bitterness and deterioration of juice quality (CruzAldaco et al, 2009;Srivastava, and Kar, 2010;Belur and Mugeraya, 2011). The operational stability of immobilized tannase is evaluated in repeated batch processes.…”

Section: Operational Stability Of Immobilized Tannasementioning

confidence: 99%

Catalytic properties of immobilized tannase produced from Aspergillus aculeatus compared with the free enzyme

El-Tanash

Sherief

Nour

2011

Braz. J. Chem. Eng.

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-Aspergillus aculeatus tannase was immobilized on several carriers by entrapment and covalent binding with cross-linking. Tannase immobilized on gelatin with cross-linking agent showed the highest activity and immobilization yield. The optimum pH of the immobilized enzyme was shifted to a more acidic range compared with the free enzyme (from pH 5.5 to pH 5.0). The optimum temperature of the reaction was determined to be 50°C for the free enzyme and 60°C for the immobilized form. The thermal stability, as well as stability over a wide range of pH, was significantly improved by the immobilization process. The calculated K m of the immobilized tannase (11.8 mg ml -1 ) is higher than that of the free tannase (6.5 mg ml -1 ), while V max of the immobilized enzyme (0.32 U (µg protein) -1 ) is lower than that of the free tannase (2.7 U (µg protein) -1 ). The immobilized enzyme was able to retain 84 % of the initial catalytic activity after 5.0 cycles.

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Microbial Production of Tannase: State of the Art

Cited by 64 publications

References 35 publications

A New Native Source of Tannase Producer, Penicillium sp. EZ-ZH190: Characterization of the Enzyme

A New Native Source of Tannase Producer, Penicillium sp. EZ-ZH190: Characterization of the Enzyme

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

Catalytic properties of immobilized tannase produced from Aspergillus aculeatus compared with the free enzyme

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