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https://doi.org/10.17113/ftb.52.04.14.3743 |
Production, Characterization and Application of a Thermostable Tannase from Pestalotiopsis guepinii URM 7114
Amanda Reges de Sena1,2, Ana Claúdia de Barros dos Santos1, Miquéas Jamesse Gouveia1, Marcelo Rodrigues Figueira de Mello1, Tonny Cley Campos Leite3, Keila Aparecida Moreira4 and Sandra Aparecida de Assis2*
1Microbiology Laboratory, Federal Institute of Education, Science and Technology of Pernambuco, Campus Barreiros, 55560-000 Barreiros, PE, Brazil
2Laboratory of Enzymology, Department of Health, State University of Feira de Santana, 44036-900 Feira de Santana, BA, Brazil
3Bioassays Laboratory for Drug Research, Federal University of Pernambuco, 50670-420 Recife, PE, Brazil
4Central Laboratory of Garanhuns, Laboratory of Biotechnology, Academic Unit of Garanhuns, Federal Rural University of Pernambuco, 55292-270 Garanhuns, PE, Brazil
Article history:
Received May 28, 2014
Accepted September 17, 2014
Key words:
endophytic fungus, Pestalotiopsis guepinii, submerged fermentation, animal feed, tannin acyl hydrolase (tannase)
Summary:
Tannase (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 identified 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 effect of variables (pH and temperature), and the results showed that the best conditions for tannase activity were pH=6.9 and 30 °C. Km was found to be 7.18·10–4 mol/L and vmax=250.00 U/mL. The tannase activity was the highest in the presence of Ca2+ 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 after 6 h. The study contributes to the identification of microbial species that produce tannase, with potential application in biotechnology.
*Corresponding author: 
+55 75 9125 0989