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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...

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Autores principales: Ge, Lin, Chen, Anna, Pei, Jianjun, Zhao, Linguo, Fang, Xianying, Ding, Gang, Wang, Zhenzhong, Xiao, Wei, Tang, Feng
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2017
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.
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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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