Efficient Immobilization of Enzymes on Amino Functionalized MIL-125-NH2 Metal Organic Framework
As a series of metal organic framework (MOFs), materials of institute lavoisier frameworks (MILs) are expected to be excellent supports for enzyme immobilization due to their good water-stability and acid tolerance. However, enzyme loading on MIL-125-NH 2 is very low due to small pore size and few a...
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| Published in | Biotechnology and bioprocess engineering Vol. 27; no. 1; pp. 135 - 144 |
|---|---|
| Main Authors | , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Seoul
The Korean Society for Biotechnology and Bioengineering
01.02.2022
한국생물공학회 |
| Subjects | |
| Online Access | Get full text |
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| Abstract | As a series of metal organic framework (MOFs), materials of institute lavoisier frameworks (MILs) are expected to be excellent supports for enzyme immobilization due to their good water-stability and acid tolerance. However, enzyme loading on MIL-125-NH
2
is very low due to small pore size and few amino groups on the surface of the MIL-125-NH
2
. In this work, catalase (CAT) was immobilized on the MIL-125-NH
2
and amino functionalized MIL-125-NH
2
by adsorption (CAT@MIL-125-NH
2
) and covalent binding (CAT@Amino MIL-125-NH
2
), respectively. Compared with the CAT@MIL-125-NH
2
and free CAT, the CAT@Amino MIL-125-NH
2
displayed high activity recovery, good pH stability, stability against denaturants, and thermostability. Furthermore, activity recovery of CAT@Amino MIL-125-NH
2
was 56% higher than CAT@MIL-125-NH
2
. The CAT@Amino MIL-125-NH
2
still retained 50% residual activity for 14 days at room temperature, whereas free CAT lost activity after storage for 1 day at the same storage conditions. Furthermore, the CAT@Amino MIL-125-NH
2
maintained 62% of its initial activity after 4 consecutive uses, showing good reusability. The results showed that the amino functionalized MIL-125-NH
2
is an excellent carrier of enzyme immobilization. |
|---|---|
| AbstractList | As a series of metal organic framework (MOFs), materials of institute lavoisier frameworks (MILs) are expected to be excellent supports for enzyme immobilization due to their good water-stability and acid tolerance. However, enzyme loading on MIL-125-NH
2
is very low due to small pore size and few amino groups on the surface of the MIL-125-NH
2
. In this work, catalase (CAT) was immobilized on the MIL-125-NH
2
and amino functionalized MIL-125-NH
2
by adsorption (CAT@MIL-125-NH
2
) and covalent binding (CAT@Amino MIL-125-NH
2
), respectively. Compared with the CAT@MIL-125-NH
2
and free CAT, the CAT@Amino MIL-125-NH
2
displayed high activity recovery, good pH stability, stability against denaturants, and thermostability. Furthermore, activity recovery of CAT@Amino MIL-125-NH
2
was 56% higher than CAT@MIL-125-NH
2
. The CAT@Amino MIL-125-NH
2
still retained 50% residual activity for 14 days at room temperature, whereas free CAT lost activity after storage for 1 day at the same storage conditions. Furthermore, the CAT@Amino MIL-125-NH
2
maintained 62% of its initial activity after 4 consecutive uses, showing good reusability. The results showed that the amino functionalized MIL-125-NH
2
is an excellent carrier of enzyme immobilization. As a series of metal organic framework (MOFs), materials of institute lavoisier frameworks (MILs) are expected to be excellent supports for enzyme immobilization due to their good water-stability and acid tolerance. However, enzyme loading on MIL-125-NH₂ is very low due to small pore size and few amino groups on the surface of the MIL-125-NH₂. In this work, catalase (CAT) was immobilized on the MIL-125-NH₂ and amino functionalized MIL-125-NH₂ by adsorption (CAT@MIL-125-NH₂) and covalent binding (CAT@Amino MIL-125-NH₂), respectively. Compared with the CAT@MIL-125-NH₂ and free CAT, the CAT@Amino MIL-125-NH₂ displayed high activity recovery, good pH stability, stability against denaturants, and thermostability. Furthermore, activity recovery of CAT@Amino MIL-125-NH₂ was 56% higher than CAT@MIL-125-NH₂. The CAT@Amino MIL-125-NH₂ still retained 50% residual activity for 14 days at room temperature, whereas free CAT lost activity after storage for 1 day at the same storage conditions. Furthermore, the CAT@Amino MIL-125-NH₂ maintained 62% of its initial activity after 4 consecutive uses, showing good reusability. The results showed that the amino functionalized MIL-125-NH₂ is an excellent carrier of enzyme immobilization. As a series of metal organic framework (MOFs), materials of institute lavoisier frameworks (MILs) are expected to be excellent supports for enzyme immobilization due to their good water-stability and acid tolerance. However, enzyme loading on MIL-125-NH2 is very low due to small pore size and few amino groups on the surface of the MIL-125-NH2. In this work, catalase (CAT) was immobilized on the MIL-125-NH2 and amino functionalized MIL-125-NH2 by adsorption (CAT@MIL-125-NH2) and covalent binding (CAT@Amino MIL-125-NH2), respectively. Compared with the CAT@MIL-125-NH2 and free CAT, the CAT@Amino MIL-125-NH2 displayed high activity recovery, good pH stability, stability against denaturants, and thermostability. Furthermore, activity recovery of CAT@Amino MIL-125-NH2 was 56% higher than CAT@MIL-125-NH2. The CAT@Amino MIL-125-NH2 still retained 50% residual activity for 14 days at room temperature, whereas free CAT lost activity after storage for 1 day at the same storage conditions. Furthermore, the CAT@Amino MIL-125-NH2 maintained 62% of its initial activity after 4 consecutive uses, showing good reusability. The results showed that the amino functionalized MIL- 125-NH2 is an excellent carrier of enzyme immobilization. KCI Citation Count: 0 |
| Author | Zhu, Daoyu Cui, Jiandong Meng, Guoqing Wang, Zichen Li, Jinhong Liu, Yang Jia, Shiru |
| Author_xml | – sequence: 1 givenname: Zichen surname: Wang fullname: Wang, Zichen organization: State Key Laboratory of Food Nutrition and Safety, Tianjin University of Science and Technology, Key Laboratory of Industrial Fermentation Microbiology, Ministry of Education, Tianjin University of Science and Technology – sequence: 2 givenname: Yang surname: Liu fullname: Liu, Yang organization: State Key Laboratory of Food Nutrition and Safety, Tianjin University of Science and Technology, Key Laboratory of Industrial Fermentation Microbiology, Ministry of Education, Tianjin University of Science and Technology – sequence: 3 givenname: Jinhong surname: Li fullname: Li, Jinhong organization: State Key Laboratory of Food Nutrition and Safety, Tianjin University of Science and Technology, Key Laboratory of Industrial Fermentation Microbiology, Ministry of Education, Tianjin University of Science and Technology – sequence: 4 givenname: Guoqing surname: Meng fullname: Meng, Guoqing organization: College of agriculture and Bioengineering, Heze University – sequence: 5 givenname: Daoyu surname: Zhu fullname: Zhu, Daoyu email: daoyuzh@sina.com organization: College of agriculture and Bioengineering, Heze University – sequence: 6 givenname: Jiandong surname: Cui fullname: Cui, Jiandong email: jdcui@tust.edu.cn organization: State Key Laboratory of Food Nutrition and Safety, Tianjin University of Science and Technology, Key Laboratory of Industrial Fermentation Microbiology, Ministry of Education, Tianjin University of Science and Technology – sequence: 7 givenname: Shiru surname: Jia fullname: Jia, Shiru organization: State Key Laboratory of Food Nutrition and Safety, Tianjin University of Science and Technology, Key Laboratory of Industrial Fermentation Microbiology, Ministry of Education, Tianjin University of Science and Technology |
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| Keywords | covalent binding enzyme immobilization MIL-125-NH amino nationalization |
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| SubjectTerms | acid tolerance adsorption ambient temperature bioprocessing Biotechnology catalase Chemistry Chemistry and Materials Science coordination polymers immobilized enzymes Industrial and Production Engineering pH stability porosity Research Paper thermal stability 생물공학 |
| Title | Efficient Immobilization of Enzymes on Amino Functionalized MIL-125-NH2 Metal Organic Framework |
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