Purification, Characterization and Application of Tannase Enzyme Isolated from Marine Aspergillus nomius GWA5
Tannase enzyme (EC 3.1.1.20) is an enzyme used in many biotechnological applications as in chemical, beverage, pharmaceutical and food industries. was isolated and purified from marine Aspergillus nomius GWA5 by 75% acetone fractional precipitation, followed by gel filtration in Sephadex G-100 and...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Journal of Pure and Applied Microbiology
2018-12-01
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| Series: | Journal of Pure and Applied Microbiology |
| Subjects: | |
| Online Access: | https://microbiologyjournal.org/purification-characterization-and-application-of-tannase-enzyme-isolated-from-marine-aspergillus-nomius-gwa5/ |
| Summary: | Tannase enzyme (EC 3.1.1.20) is an enzyme used in many biotechnological applications as in chemical, beverage,
pharmaceutical and food industries. was isolated and purified from marine Aspergillus nomius GWA5 by 75%
acetone fractional precipitation, followed by gel filtration in Sephadex G-100 and ion exchange chromatography
on DEAE-Sephadex A-50 yielding 4.48-fold purification. Estimation of tannase molecular weight was carried out
using sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS–PAGE) showing a molecular weight of 30
kDa. The highest activity (291 U/mg protein) were at pH 6.0 and 50 °C, respectively. Tannase stability was observed
in acidic range (4-6) and was stable to heat treatment. In absence of its substrate it retained about 84.5% of its
activity at 80 °C for 15 min. Effect of some metal ions and chelator on tannase activity was investigated. Mg2+
activated as activator of the pure enzyme while EDTA, Cd2+, Pb2+ and Hg2+ inhibited its activity and retained about
40.78, 51.55, 30.24 and 24.55% of its activity, respectively. Promising activity of Tannase was shown in removing
tannin stains of tea from clothes. |
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| ISSN: | 0973-7510 2581-690X |