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Characterization and Secretory Expression of a Thermostable Tannase from Aureobasidium melanogenum T9: Potential Candidate for Food and Agricultural Industries
Being a key industrial enzyme, tannase is extensively applied in various fields. Despite the characterizations of a large number of tannases, there are hardly a few tannases with exceptional thermostability. In this detailed study, a tannase-encoding gene named tanA was identified from Aureobasidium...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8861512/ https://www.ncbi.nlm.nih.gov/pubmed/35211468 http://dx.doi.org/10.3389/fbioe.2021.769816 |
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author | Liu, Lu Guo, Jing Zhou, Xue-Feng Li, Ze Zhou, Hai-Xiang Song, Wei-Qing |
author_facet | Liu, Lu Guo, Jing Zhou, Xue-Feng Li, Ze Zhou, Hai-Xiang Song, Wei-Qing |
author_sort | Liu, Lu |
collection | PubMed |
description | Being a key industrial enzyme, tannase is extensively applied in various fields. Despite the characterizations of a large number of tannases, there are hardly a few tannases with exceptional thermostability. In this detailed study, a tannase-encoding gene named tanA was identified from Aureobasidium melanogenum T9 and heterologously expressed in Yarrowia lipolytica host of food grade. The purified tannase TanA with a molecular weight of above 63.0 kDa displayed a specific activity of 941.4 U/mg. Moreover, TanA showed optimum activity at 60°C and pH 6.0. Interestingly, TanA exhibited up to 61.3% activity after incubation for 12 h at 55°C, signifying its thermophilic property and distinguished thermostability. Additionally, TanA was a multifunctional tannase with high specific activities to catalyze the degradation of various gallic acid esters. Therefore, this study presents a novel tannase, TanA, with remarkable properties, posing as a potential candidate for food and agricultural processing. |
format | Online Article Text |
id | pubmed-8861512 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-88615122022-02-23 Characterization and Secretory Expression of a Thermostable Tannase from Aureobasidium melanogenum T9: Potential Candidate for Food and Agricultural Industries Liu, Lu Guo, Jing Zhou, Xue-Feng Li, Ze Zhou, Hai-Xiang Song, Wei-Qing Front Bioeng Biotechnol Bioengineering and Biotechnology Being a key industrial enzyme, tannase is extensively applied in various fields. Despite the characterizations of a large number of tannases, there are hardly a few tannases with exceptional thermostability. In this detailed study, a tannase-encoding gene named tanA was identified from Aureobasidium melanogenum T9 and heterologously expressed in Yarrowia lipolytica host of food grade. The purified tannase TanA with a molecular weight of above 63.0 kDa displayed a specific activity of 941.4 U/mg. Moreover, TanA showed optimum activity at 60°C and pH 6.0. Interestingly, TanA exhibited up to 61.3% activity after incubation for 12 h at 55°C, signifying its thermophilic property and distinguished thermostability. Additionally, TanA was a multifunctional tannase with high specific activities to catalyze the degradation of various gallic acid esters. Therefore, this study presents a novel tannase, TanA, with remarkable properties, posing as a potential candidate for food and agricultural processing. Frontiers Media S.A. 2022-02-08 /pmc/articles/PMC8861512/ /pubmed/35211468 http://dx.doi.org/10.3389/fbioe.2021.769816 Text en Copyright © 2022 Liu, Guo, Zhou, Li, Zhou and Song. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Bioengineering and Biotechnology Liu, Lu Guo, Jing Zhou, Xue-Feng Li, Ze Zhou, Hai-Xiang Song, Wei-Qing Characterization and Secretory Expression of a Thermostable Tannase from Aureobasidium melanogenum T9: Potential Candidate for Food and Agricultural Industries |
title | Characterization and Secretory Expression of a Thermostable Tannase from Aureobasidium melanogenum T9: Potential Candidate for Food and Agricultural Industries |
title_full | Characterization and Secretory Expression of a Thermostable Tannase from Aureobasidium melanogenum T9: Potential Candidate for Food and Agricultural Industries |
title_fullStr | Characterization and Secretory Expression of a Thermostable Tannase from Aureobasidium melanogenum T9: Potential Candidate for Food and Agricultural Industries |
title_full_unstemmed | Characterization and Secretory Expression of a Thermostable Tannase from Aureobasidium melanogenum T9: Potential Candidate for Food and Agricultural Industries |
title_short | Characterization and Secretory Expression of a Thermostable Tannase from Aureobasidium melanogenum T9: Potential Candidate for Food and Agricultural Industries |
title_sort | characterization and secretory expression of a thermostable tannase from aureobasidium melanogenum t9: potential candidate for food and agricultural industries |
topic | Bioengineering and Biotechnology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8861512/ https://www.ncbi.nlm.nih.gov/pubmed/35211468 http://dx.doi.org/10.3389/fbioe.2021.769816 |
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