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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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 |
work_keys_str_mv |
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