Green synthesis of enzyme/metal-organic framework composites with high stability in protein denaturing solvents ...

Abstract Objectives Enzyme/metal-organic framework composites with high stability in protein denaturing solvents were reported in this study. Results Encapsulation of enzyme in metal-organic frameworks (MOFs) via co-precipitation process was realized, and the generality of the synthesis was validate...

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Main Authors: Wu, Xiaoling, Yang, Cheng, Ge, Jun
Format: Article in Journal/Newspaper
Language:unknown
Published: figshare 2017
Subjects:
Online Access:https://dx.doi.org/10.6084/m9.figshare.c.3784241
https://springernature.figshare.com/collections/Green_synthesis_of_enzyme_metal-organic_framework_composites_with_high_stability_in_protein_denaturing_solvents/3784241
id ftdatacite:10.6084/m9.figshare.c.3784241
record_format openpolar
spelling ftdatacite:10.6084/m9.figshare.c.3784241 2024-04-28T08:00:24+00:00 Green synthesis of enzyme/metal-organic framework composites with high stability in protein denaturing solvents ... Wu, Xiaoling Yang, Cheng Ge, Jun 2017 https://dx.doi.org/10.6084/m9.figshare.c.3784241 https://springernature.figshare.com/collections/Green_synthesis_of_enzyme_metal-organic_framework_composites_with_high_stability_in_protein_denaturing_solvents/3784241 unknown figshare Creative Commons Attribution 4.0 International https://creativecommons.org/licenses/by/4.0/legalcode cc-by-4.0 Biochemistry Microbiology FOS Biological sciences Biotechnology Chemical Sciences not elsewhere classified Astronomical and Space Sciences not elsewhere classified Biological Sciences not elsewhere classified Collection article 2017 ftdatacite https://doi.org/10.6084/m9.figshare.c.3784241 2024-04-02T11:54:48Z Abstract Objectives Enzyme/metal-organic framework composites with high stability in protein denaturing solvents were reported in this study. Results Encapsulation of enzyme in metal-organic frameworks (MOFs) via co-precipitation process was realized, and the generality of the synthesis was validated by using cytochrome c, horseradish peroxidase, and Candida antarctica lipase B as model enzymes. The stability of encapsulated enzyme was greatly increased after immobilization on MOFs. Remarkably, when exposed to protein denaturing solvents including dimethyl sulfoxide, dimethyl formamide, methanol, and ethanol, the enzyme/MOF composites still preserved almost 100% of activity. In contrast, free enzymes retained no more than 20% of their original activities at the same condition. This study shows the extraordinary protecting effect of MOF shell on increasing enzyme stability at extremely harsh conditions. Conclusion The enzyme immobilized in MOF exhibited enhanced thermal stability and high tolerance towards ... Article in Journal/Newspaper Antarc* Antarctica DataCite Metadata Store (German National Library of Science and Technology)
institution Open Polar
collection DataCite Metadata Store (German National Library of Science and Technology)
op_collection_id ftdatacite
language unknown
topic Biochemistry
Microbiology
FOS Biological sciences
Biotechnology
Chemical Sciences not elsewhere classified
Astronomical and Space Sciences not elsewhere classified
Biological Sciences not elsewhere classified
spellingShingle Biochemistry
Microbiology
FOS Biological sciences
Biotechnology
Chemical Sciences not elsewhere classified
Astronomical and Space Sciences not elsewhere classified
Biological Sciences not elsewhere classified
Wu, Xiaoling
Yang, Cheng
Ge, Jun
Green synthesis of enzyme/metal-organic framework composites with high stability in protein denaturing solvents ...
topic_facet Biochemistry
Microbiology
FOS Biological sciences
Biotechnology
Chemical Sciences not elsewhere classified
Astronomical and Space Sciences not elsewhere classified
Biological Sciences not elsewhere classified
description Abstract Objectives Enzyme/metal-organic framework composites with high stability in protein denaturing solvents were reported in this study. Results Encapsulation of enzyme in metal-organic frameworks (MOFs) via co-precipitation process was realized, and the generality of the synthesis was validated by using cytochrome c, horseradish peroxidase, and Candida antarctica lipase B as model enzymes. The stability of encapsulated enzyme was greatly increased after immobilization on MOFs. Remarkably, when exposed to protein denaturing solvents including dimethyl sulfoxide, dimethyl formamide, methanol, and ethanol, the enzyme/MOF composites still preserved almost 100% of activity. In contrast, free enzymes retained no more than 20% of their original activities at the same condition. This study shows the extraordinary protecting effect of MOF shell on increasing enzyme stability at extremely harsh conditions. Conclusion The enzyme immobilized in MOF exhibited enhanced thermal stability and high tolerance towards ...
format Article in Journal/Newspaper
author Wu, Xiaoling
Yang, Cheng
Ge, Jun
author_facet Wu, Xiaoling
Yang, Cheng
Ge, Jun
author_sort Wu, Xiaoling
title Green synthesis of enzyme/metal-organic framework composites with high stability in protein denaturing solvents ...
title_short Green synthesis of enzyme/metal-organic framework composites with high stability in protein denaturing solvents ...
title_full Green synthesis of enzyme/metal-organic framework composites with high stability in protein denaturing solvents ...
title_fullStr Green synthesis of enzyme/metal-organic framework composites with high stability in protein denaturing solvents ...
title_full_unstemmed Green synthesis of enzyme/metal-organic framework composites with high stability in protein denaturing solvents ...
title_sort green synthesis of enzyme/metal-organic framework composites with high stability in protein denaturing solvents ...
publisher figshare
publishDate 2017
url https://dx.doi.org/10.6084/m9.figshare.c.3784241
https://springernature.figshare.com/collections/Green_synthesis_of_enzyme_metal-organic_framework_composites_with_high_stability_in_protein_denaturing_solvents/3784241
genre Antarc*
Antarctica
genre_facet Antarc*
Antarctica
op_rights Creative Commons Attribution 4.0 International
https://creativecommons.org/licenses/by/4.0/legalcode
cc-by-4.0
op_doi https://doi.org/10.6084/m9.figshare.c.3784241
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