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Optimization of κ-Selenocarrageenase Production by Pseudoalteromonas sp. Xi13 and Its Immobilization

The bioenzymatic production of selenium oligosaccharides addresses the problems resulting from high molecular weight and poor water solubility of κ-selenocarrageenan, and lays foundation for its application as adjuvant drugs for cancer treatment and food additive. κ-selenocarrageenase extracted from...

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Autores principales: Deng, Yashan, Wang, Xixi, Xu, Hui, Liu, Cui, Li, Ran, Zhang, Yuanyuan, Qu, Changfeng, Miao, Jinlai
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9694495/
https://www.ncbi.nlm.nih.gov/pubmed/36431814
http://dx.doi.org/10.3390/molecules27227716
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author Deng, Yashan
Wang, Xixi
Xu, Hui
Liu, Cui
Li, Ran
Zhang, Yuanyuan
Qu, Changfeng
Miao, Jinlai
author_facet Deng, Yashan
Wang, Xixi
Xu, Hui
Liu, Cui
Li, Ran
Zhang, Yuanyuan
Qu, Changfeng
Miao, Jinlai
author_sort Deng, Yashan
collection PubMed
description The bioenzymatic production of selenium oligosaccharides addresses the problems resulting from high molecular weight and poor water solubility of κ-selenocarrageenan, and lays foundation for its application as adjuvant drugs for cancer treatment and food additive. κ-selenocarrageenase extracted from Pseudoalteromonas sp. Xi13 can degrade κ-selenocarrageenan to selenium oligosaccharides. The maximum optimized κ-selenocarrageenase activity using Response Surface Methodology (RSM) was increased by 1.4 times, reaching 8.416 U/mL. To expand applications of the κ-selenocarrageenase in industry, the preparation conditions of it in either lyophilized or immobilized form were investigated. The activity recovery rate of the lyophilized enzyme was >70%, while that of the immobilized enzyme was 62.83%. However, the immobilized κ-selenocarrageenase exhibits good stability after being reused four times, with 58.28% of residual activity. The selenium content of κ-selenocarrageenan oligosaccharides degraded by the immobilized κ-selenocarrageenase was 47.06 µg/g, 8.3% higher than that degraded by the lyophilized enzyme. The results indicate that the immobilized κ-selenocarrageenase is suitable for industrial applications and has commercial potential.
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spelling pubmed-96944952022-11-26 Optimization of κ-Selenocarrageenase Production by Pseudoalteromonas sp. Xi13 and Its Immobilization Deng, Yashan Wang, Xixi Xu, Hui Liu, Cui Li, Ran Zhang, Yuanyuan Qu, Changfeng Miao, Jinlai Molecules Article The bioenzymatic production of selenium oligosaccharides addresses the problems resulting from high molecular weight and poor water solubility of κ-selenocarrageenan, and lays foundation for its application as adjuvant drugs for cancer treatment and food additive. κ-selenocarrageenase extracted from Pseudoalteromonas sp. Xi13 can degrade κ-selenocarrageenan to selenium oligosaccharides. The maximum optimized κ-selenocarrageenase activity using Response Surface Methodology (RSM) was increased by 1.4 times, reaching 8.416 U/mL. To expand applications of the κ-selenocarrageenase in industry, the preparation conditions of it in either lyophilized or immobilized form were investigated. The activity recovery rate of the lyophilized enzyme was >70%, while that of the immobilized enzyme was 62.83%. However, the immobilized κ-selenocarrageenase exhibits good stability after being reused four times, with 58.28% of residual activity. The selenium content of κ-selenocarrageenan oligosaccharides degraded by the immobilized κ-selenocarrageenase was 47.06 µg/g, 8.3% higher than that degraded by the lyophilized enzyme. The results indicate that the immobilized κ-selenocarrageenase is suitable for industrial applications and has commercial potential. MDPI 2022-11-09 /pmc/articles/PMC9694495/ /pubmed/36431814 http://dx.doi.org/10.3390/molecules27227716 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Deng, Yashan
Wang, Xixi
Xu, Hui
Liu, Cui
Li, Ran
Zhang, Yuanyuan
Qu, Changfeng
Miao, Jinlai
Optimization of κ-Selenocarrageenase Production by Pseudoalteromonas sp. Xi13 and Its Immobilization
title Optimization of κ-Selenocarrageenase Production by Pseudoalteromonas sp. Xi13 and Its Immobilization
title_full Optimization of κ-Selenocarrageenase Production by Pseudoalteromonas sp. Xi13 and Its Immobilization
title_fullStr Optimization of κ-Selenocarrageenase Production by Pseudoalteromonas sp. Xi13 and Its Immobilization
title_full_unstemmed Optimization of κ-Selenocarrageenase Production by Pseudoalteromonas sp. Xi13 and Its Immobilization
title_short Optimization of κ-Selenocarrageenase Production by Pseudoalteromonas sp. Xi13 and Its Immobilization
title_sort optimization of κ-selenocarrageenase production by pseudoalteromonas sp. xi13 and its immobilization
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9694495/
https://www.ncbi.nlm.nih.gov/pubmed/36431814
http://dx.doi.org/10.3390/molecules27227716
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