Kinetic,thermodynamic parameters and in vitro digestion of tannase from Aspergillus tamarii URM 7115 |
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Authors: | Amanda Reges de Sena Tonny Cley Campos Leite Talita Camila Evaristo da Silva Nascimento Anna Carolina da Silva Catiane S. Souza Antônio Fernando de Mello Vaz |
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Affiliation: | 1. Microbiology Laboratory, Federal Institute of Education, Science and Technology of Pernambuco, Barreiros, Pernambuco, Brazil;2. Central Laboratory of Garanhuns, Laboratory of Biotechnology, Academic Unit of Garanhuns, Federal Rural University of Pernambuco, Garanhuns, Pernambuco, Brazil;3. Laboratory of Enzymology, Department of Health, State University of Feira de Santana, Feira de Santana, Bahia, Brazil;4. Center for Rural Health and Technology, Federal University of Campina Grande, Patos, Paraíba, Brazil |
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Abstract: | Tannase is an enzyme used in various industries and produced by a large number of microorganisms. The aim of this study was to evaluate tannase production to determine the biochemical, kinetic, and thermodynamic properties and to simulate tannase in vitro digestion. The tannase-producing fungal strain was isolated from “jamun” leaves and identified as Aspergillus tamarii. Temperature at 26°C for 67?h was the best combination for maximum tannase activity (6.35-fold; initial activity in Plackett–Burman design—15.53?U/mL and average final activity in Doehlert design—98.68?U/mL). The crude extract of tannase was optimally active at 40°C, pH 5.5 and 6.5. Moreover, tannase was stimulated by Na+, Ca2+, Mg2+, and Mn2+. The half-life at 40°C lasted 247.55?min. The free energy of Gibbs, enthalpy, and entropy, at 40°C, was 81.47, 16.85, and ?0.21?kJ/mol?·?K, respectively. After total digestion, 123.95% of the original activity was retained. Results suggested that tannase from A. tamarii URM 7115 is an enzyme of interest for industrial applications, such as gallic acid production, additive for feed industry, and for beverage manufacturing, due to its catalytic and thermodynamic properties. |
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Keywords: | Animal feed industry catalytic properties experimental design submerged fermentation tannin acyl hydrolase thermodynamics |
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