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Enhancing the thermostability of α-L-rhamnosidase from Aspergillus terreus and the enzymatic conversion of rutin to isoquercitrin by adding sorbitol
BACKGROUND: Thermally stable α-L-rhamnosidase with cleaving terminal α-L-rhamnose activity has great potential in industrial application. Therefore, it is necessary to find a proper method to improve the thermal stability of α-L-rhamnosidase. RESULTS: In this study, addition of sorbitol has been fou...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5327507/ https://www.ncbi.nlm.nih.gov/pubmed/28241810 http://dx.doi.org/10.1186/s12896-017-0342-9 |
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author | Ge, Lin Chen, Anna Pei, Jianjun Zhao, Linguo Fang, Xianying Ding, Gang Wang, Zhenzhong Xiao, Wei Tang, Feng |
author_facet | Ge, Lin Chen, Anna Pei, Jianjun Zhao, Linguo Fang, Xianying Ding, Gang Wang, Zhenzhong Xiao, Wei Tang, Feng |
author_sort | Ge, Lin |
collection | PubMed |
description | BACKGROUND: Thermally stable α-L-rhamnosidase with cleaving terminal α-L-rhamnose activity has great potential in industrial application. Therefore, it is necessary to find a proper method to improve the thermal stability of α-L-rhamnosidase. RESULTS: In this study, addition of sorbitol has been found to increase the thermostability of α-L-rhamnosidase from Aspergillus terreus at temperatures ranging from 65 °C to 80 °C. Half-life and activation free energy with addition of 2.0 M sorbitol at 70 °C were increased by 17.2-fold, 8.2 kJ/mol, respectively. The analyses of the results of fluorescence spectroscopy and CD have indicated that sorbitol helped to protect the tertiary and secondary structure of α-L-rhamnosidase. Moreover, the isoquercitrin yield increased from 60.01 to 96.43% with the addition of 1.5 M of sorbitol at 70 °C. CONCLUSION: Our findings provide an effective approach for enhancing the thermostability of α-L-rhamnosidase from Aspergillus terreus, which makes it a good candidate for industrial processes of isoquercitrin preparation. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12896-017-0342-9) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-5327507 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-53275072017-03-03 Enhancing the thermostability of α-L-rhamnosidase from Aspergillus terreus and the enzymatic conversion of rutin to isoquercitrin by adding sorbitol Ge, Lin Chen, Anna Pei, Jianjun Zhao, Linguo Fang, Xianying Ding, Gang Wang, Zhenzhong Xiao, Wei Tang, Feng BMC Biotechnol Research Article BACKGROUND: Thermally stable α-L-rhamnosidase with cleaving terminal α-L-rhamnose activity has great potential in industrial application. Therefore, it is necessary to find a proper method to improve the thermal stability of α-L-rhamnosidase. RESULTS: In this study, addition of sorbitol has been found to increase the thermostability of α-L-rhamnosidase from Aspergillus terreus at temperatures ranging from 65 °C to 80 °C. Half-life and activation free energy with addition of 2.0 M sorbitol at 70 °C were increased by 17.2-fold, 8.2 kJ/mol, respectively. The analyses of the results of fluorescence spectroscopy and CD have indicated that sorbitol helped to protect the tertiary and secondary structure of α-L-rhamnosidase. Moreover, the isoquercitrin yield increased from 60.01 to 96.43% with the addition of 1.5 M of sorbitol at 70 °C. CONCLUSION: Our findings provide an effective approach for enhancing the thermostability of α-L-rhamnosidase from Aspergillus terreus, which makes it a good candidate for industrial processes of isoquercitrin preparation. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12896-017-0342-9) contains supplementary material, which is available to authorized users. BioMed Central 2017-02-27 /pmc/articles/PMC5327507/ /pubmed/28241810 http://dx.doi.org/10.1186/s12896-017-0342-9 Text en © The Author(s). 2017 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Research Article Ge, Lin Chen, Anna Pei, Jianjun Zhao, Linguo Fang, Xianying Ding, Gang Wang, Zhenzhong Xiao, Wei Tang, Feng Enhancing the thermostability of α-L-rhamnosidase from Aspergillus terreus and the enzymatic conversion of rutin to isoquercitrin by adding sorbitol |
title | Enhancing the thermostability of α-L-rhamnosidase from Aspergillus terreus and the enzymatic conversion of rutin to isoquercitrin by adding sorbitol |
title_full | Enhancing the thermostability of α-L-rhamnosidase from Aspergillus terreus and the enzymatic conversion of rutin to isoquercitrin by adding sorbitol |
title_fullStr | Enhancing the thermostability of α-L-rhamnosidase from Aspergillus terreus and the enzymatic conversion of rutin to isoquercitrin by adding sorbitol |
title_full_unstemmed | Enhancing the thermostability of α-L-rhamnosidase from Aspergillus terreus and the enzymatic conversion of rutin to isoquercitrin by adding sorbitol |
title_short | Enhancing the thermostability of α-L-rhamnosidase from Aspergillus terreus and the enzymatic conversion of rutin to isoquercitrin by adding sorbitol |
title_sort | enhancing the thermostability of α-l-rhamnosidase from aspergillus terreus and the enzymatic conversion of rutin to isoquercitrin by adding sorbitol |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5327507/ https://www.ncbi.nlm.nih.gov/pubmed/28241810 http://dx.doi.org/10.1186/s12896-017-0342-9 |
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