Expression and Characterization of a Novel Cold-Adapted Chitosanase from Marine <i>Renibacterium</i> sp. Suitable for Chitooligosaccharides Preparation

(1) Background: Chitooligosaccharides (COS) have numerous applications due to their excellent properties. Chitosan hydrolysis using chitosanases has been proposed as an advisable method for COS preparation. Although many chitosanases from various sources have been identified, the cold-adapted ones w...

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Autores principales: Lin-Lin Zhang, Xiao-Hua Jiang, Xin-Feng Xiao, Wen-Xiu Zhang, Yi-Qian Shi, Zhi-Peng Wang, Hai-Xiang Zhou
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Publicado: MDPI AG 2021
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spelling oai:doaj.org-article:8629524aad324803a6596d67ba7cb4b32021-11-25T18:12:41ZExpression and Characterization of a Novel Cold-Adapted Chitosanase from Marine <i>Renibacterium</i> sp. Suitable for Chitooligosaccharides Preparation10.3390/md191105961660-3397https://doaj.org/article/8629524aad324803a6596d67ba7cb4b32021-10-01T00:00:00Zhttps://www.mdpi.com/1660-3397/19/11/596https://doaj.org/toc/1660-3397(1) Background: Chitooligosaccharides (COS) have numerous applications due to their excellent properties. Chitosan hydrolysis using chitosanases has been proposed as an advisable method for COS preparation. Although many chitosanases from various sources have been identified, the cold-adapted ones with high stability are still rather rare but required. (2) Methods: A novel chitosanase named CsnY from marine bacterium <i>Renibacterium</i> sp. Y82 was expressed in <i>Escherichia coli</i>, following sequence analysis. Then, the characterizations of recombinant CsnY purified through Ni–NTA affinity chromatography were conducted, including effects of pH and temperature, effects of metal ions and chemicals, and final product analysis. (3) Results: The GH46 family chitosanase CsnY possessed promising thermostability at broad temperature range (0–50 °C), and with optimal activity at 40 °C and pH 6.0, especially showing relatively high activity (over 80% of its maximum activity) at low temperatures (20–30 °C), which demonstrated the cold-adapted property. Common metal ions or chemicals had no obvious effect on CsnY except Mn<sup>2+</sup> and Co<sup>2+</sup>. Finally, CsnY was determined to be an endo-type chitosanase generating chitodisaccharides and -trisaccharides as main products, whose total concentration reached 56.74 mM within 2 h against 2% (<i>w</i>/<i>v</i>) initial chitosan substrate. (4) Conclusions: The results suggest the cold-adapted CsnY with favorable stability has desirable potential for the industrial production of COS.Lin-Lin ZhangXiao-Hua JiangXin-Feng XiaoWen-Xiu ZhangYi-Qian ShiZhi-Peng WangHai-Xiang ZhouMDPI AGarticlechitosanasecold adaptationchitooligosaccharide<i>Renibacterium</i> sp.Biology (General)QH301-705.5ENMarine Drugs, Vol 19, Iss 596, p 596 (2021)
institution DOAJ
collection DOAJ
language EN
topic chitosanase
cold adaptation
chitooligosaccharide
<i>Renibacterium</i> sp.
Biology (General)
QH301-705.5
spellingShingle chitosanase
cold adaptation
chitooligosaccharide
<i>Renibacterium</i> sp.
Biology (General)
QH301-705.5
Lin-Lin Zhang
Xiao-Hua Jiang
Xin-Feng Xiao
Wen-Xiu Zhang
Yi-Qian Shi
Zhi-Peng Wang
Hai-Xiang Zhou
Expression and Characterization of a Novel Cold-Adapted Chitosanase from Marine <i>Renibacterium</i> sp. Suitable for Chitooligosaccharides Preparation
description (1) Background: Chitooligosaccharides (COS) have numerous applications due to their excellent properties. Chitosan hydrolysis using chitosanases has been proposed as an advisable method for COS preparation. Although many chitosanases from various sources have been identified, the cold-adapted ones with high stability are still rather rare but required. (2) Methods: A novel chitosanase named CsnY from marine bacterium <i>Renibacterium</i> sp. Y82 was expressed in <i>Escherichia coli</i>, following sequence analysis. Then, the characterizations of recombinant CsnY purified through Ni–NTA affinity chromatography were conducted, including effects of pH and temperature, effects of metal ions and chemicals, and final product analysis. (3) Results: The GH46 family chitosanase CsnY possessed promising thermostability at broad temperature range (0–50 °C), and with optimal activity at 40 °C and pH 6.0, especially showing relatively high activity (over 80% of its maximum activity) at low temperatures (20–30 °C), which demonstrated the cold-adapted property. Common metal ions or chemicals had no obvious effect on CsnY except Mn<sup>2+</sup> and Co<sup>2+</sup>. Finally, CsnY was determined to be an endo-type chitosanase generating chitodisaccharides and -trisaccharides as main products, whose total concentration reached 56.74 mM within 2 h against 2% (<i>w</i>/<i>v</i>) initial chitosan substrate. (4) Conclusions: The results suggest the cold-adapted CsnY with favorable stability has desirable potential for the industrial production of COS.
format article
author Lin-Lin Zhang
Xiao-Hua Jiang
Xin-Feng Xiao
Wen-Xiu Zhang
Yi-Qian Shi
Zhi-Peng Wang
Hai-Xiang Zhou
author_facet Lin-Lin Zhang
Xiao-Hua Jiang
Xin-Feng Xiao
Wen-Xiu Zhang
Yi-Qian Shi
Zhi-Peng Wang
Hai-Xiang Zhou
author_sort Lin-Lin Zhang
title Expression and Characterization of a Novel Cold-Adapted Chitosanase from Marine <i>Renibacterium</i> sp. Suitable for Chitooligosaccharides Preparation
title_short Expression and Characterization of a Novel Cold-Adapted Chitosanase from Marine <i>Renibacterium</i> sp. Suitable for Chitooligosaccharides Preparation
title_full Expression and Characterization of a Novel Cold-Adapted Chitosanase from Marine <i>Renibacterium</i> sp. Suitable for Chitooligosaccharides Preparation
title_fullStr Expression and Characterization of a Novel Cold-Adapted Chitosanase from Marine <i>Renibacterium</i> sp. Suitable for Chitooligosaccharides Preparation
title_full_unstemmed Expression and Characterization of a Novel Cold-Adapted Chitosanase from Marine <i>Renibacterium</i> sp. Suitable for Chitooligosaccharides Preparation
title_sort expression and characterization of a novel cold-adapted chitosanase from marine <i>renibacterium</i> sp. suitable for chitooligosaccharides preparation
publisher MDPI AG
publishDate 2021
url https://doaj.org/article/8629524aad324803a6596d67ba7cb4b3
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