Fast Immobilization of Human Carbonic Anhydrase II on Ni-Based Metal-Organic Framework Nanorods with High Catalytic Performance

Carbonic anhydrase (CA) has received considerable attention for its ability to capture carbon dioxide efficiently. This study reports a simple strategy for immobilizing recombinant carbonic anhydrase II from human (hCA II) on Ni-based MOFs (Ni-BTC) nanorods, which was readily achieved in a one-pot i...

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Main Authors: Mengzhao Jiao, Jie He, Shanshan Sun, Frank Vriesekoop, Qipeng Yuan, Yanhui Liu, Hao Liang
Format: Article
Language:English
Published: MDPI AG 2020-04-01
Series:Catalysts
Subjects:
Online Access:https://www.mdpi.com/2073-4344/10/4/401
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spelling doaj-0422569c8f534e1188494777ab2f2c1e2020-11-25T03:01:16ZengMDPI AGCatalysts2073-43442020-04-011040140110.3390/catal10040401Fast Immobilization of Human Carbonic Anhydrase II on Ni-Based Metal-Organic Framework Nanorods with High Catalytic PerformanceMengzhao Jiao0Jie He1Shanshan Sun2Frank Vriesekoop3Qipeng Yuan4Yanhui Liu5Hao Liang6State Key Laboratory of Chemical Resource Engineering, Beijing University of Chemical Technology, Beijing 100029, ChinaState Key Laboratory of Chemical Resource Engineering, Beijing University of Chemical Technology, Beijing 100029, ChinaState Key Laboratory of Chemical Resource Engineering, Beijing University of Chemical Technology, Beijing 100029, ChinaDepartment of Food Technology and Innovation, Harper Adams University, Newport TF10 8NB, UKState Key Laboratory of Chemical Resource Engineering, Beijing University of Chemical Technology, Beijing 100029, ChinaState Key Laboratory of Chemical Resource Engineering, Beijing University of Chemical Technology, Beijing 100029, ChinaState Key Laboratory of Chemical Resource Engineering, Beijing University of Chemical Technology, Beijing 100029, ChinaCarbonic anhydrase (CA) has received considerable attention for its ability to capture carbon dioxide efficiently. This study reports a simple strategy for immobilizing recombinant carbonic anhydrase II from human (hCA II) on Ni-based MOFs (Ni-BTC) nanorods, which was readily achieved in a one-pot immobilization of His-tagged hCA II (His-hCA II). Consequently, His-hCA II from cell lysate could obtain an activity recovery of 99% under optimal conditions. After storing for 10 days, the immobilized His-hCA II maintained 40% activity while the free enzyme lost 91% activity. Furthermore, during the hydrolysis of p-nitrophenyl acetic acid, immobilized His-hCA II exhibited excellent reusability and still retained more than 65% of the original activity after eight cycles. In addition, we also found that Ni-BTC had no fixation effect on proteins without histidine-tag. These results show that the Ni-BTC MOFs have a great potential with high efficiency for and specific binding of immobilized enzymes.https://www.mdpi.com/2073-4344/10/4/401one-pot hydrothermalimmobilizing recombinantHis-hCA IINi-BTC nanorods
collection DOAJ
language English
format Article
sources DOAJ
author Mengzhao Jiao
Jie He
Shanshan Sun
Frank Vriesekoop
Qipeng Yuan
Yanhui Liu
Hao Liang
spellingShingle Mengzhao Jiao
Jie He
Shanshan Sun
Frank Vriesekoop
Qipeng Yuan
Yanhui Liu
Hao Liang
Fast Immobilization of Human Carbonic Anhydrase II on Ni-Based Metal-Organic Framework Nanorods with High Catalytic Performance
Catalysts
one-pot hydrothermal
immobilizing recombinant
His-hCA II
Ni-BTC nanorods
author_facet Mengzhao Jiao
Jie He
Shanshan Sun
Frank Vriesekoop
Qipeng Yuan
Yanhui Liu
Hao Liang
author_sort Mengzhao Jiao
title Fast Immobilization of Human Carbonic Anhydrase II on Ni-Based Metal-Organic Framework Nanorods with High Catalytic Performance
title_short Fast Immobilization of Human Carbonic Anhydrase II on Ni-Based Metal-Organic Framework Nanorods with High Catalytic Performance
title_full Fast Immobilization of Human Carbonic Anhydrase II on Ni-Based Metal-Organic Framework Nanorods with High Catalytic Performance
title_fullStr Fast Immobilization of Human Carbonic Anhydrase II on Ni-Based Metal-Organic Framework Nanorods with High Catalytic Performance
title_full_unstemmed Fast Immobilization of Human Carbonic Anhydrase II on Ni-Based Metal-Organic Framework Nanorods with High Catalytic Performance
title_sort fast immobilization of human carbonic anhydrase ii on ni-based metal-organic framework nanorods with high catalytic performance
publisher MDPI AG
series Catalysts
issn 2073-4344
publishDate 2020-04-01
description Carbonic anhydrase (CA) has received considerable attention for its ability to capture carbon dioxide efficiently. This study reports a simple strategy for immobilizing recombinant carbonic anhydrase II from human (hCA II) on Ni-based MOFs (Ni-BTC) nanorods, which was readily achieved in a one-pot immobilization of His-tagged hCA II (His-hCA II). Consequently, His-hCA II from cell lysate could obtain an activity recovery of 99% under optimal conditions. After storing for 10 days, the immobilized His-hCA II maintained 40% activity while the free enzyme lost 91% activity. Furthermore, during the hydrolysis of p-nitrophenyl acetic acid, immobilized His-hCA II exhibited excellent reusability and still retained more than 65% of the original activity after eight cycles. In addition, we also found that Ni-BTC had no fixation effect on proteins without histidine-tag. These results show that the Ni-BTC MOFs have a great potential with high efficiency for and specific binding of immobilized enzymes.
topic one-pot hydrothermal
immobilizing recombinant
His-hCA II
Ni-BTC nanorods
url https://www.mdpi.com/2073-4344/10/4/401
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