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Research Article
Bo Yang
Qingdao University of Science and Technology
Corresponding Author
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Amino modified mesoporous silica (SBA-15-NH2) was prepared by hydrothermal method, which is a kind of excellent carrier for enzyme immobilization. The structure of SBA-15 was characterized by SEM and FTIR, which proved that amino group was successfully attached to the surface of SBA-15. The carrier had good mesoporous structure by nitrogen adsorption and desorption test. Using SBA-15-NH2 as the carrier, the optimal conditions of laccase immobilization by two different cross-linking methods were explored. At the same time, the properties of immobilized enzyme and free enzyme were compared. The results showed that the activity of immobilized laccase by two-step method (2977.5 U/g) was much higher than that by one-step method (239.5 U/g). The optimal conditions were as follows: free laccase (35℃, pH = 4.5), two-step immobilized laccase (40℃, pH = 4.0), one-step immobilized laccase (35℃, pH = 4.0). The two-step method was more adaptable to temperature. The pH adaptation range of immobilized enzyme was wider, and the thermal stability was greatly enhanced. After five cycles of repeated reaction, the residual enzyme activity of two-step and one-step methods were 56% and 43% of the original. The treatment of simulated wastewater containing 2,4-dichlorophenol (2,4-DCP) by immobilized laccase was also studied. Under the optimum conditions (40℃, pH = 5.0, 20 mg/L), the removal of 2,4-DCP can reach 89.06%.
Keywords
SBA-15-NH2, Cross-linking, Immobilization, Laccase, 2,4-DCP, Water treatment
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View the published article at Applied Biochemistry and Biotechnology.
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Posted 18 Feb, 2021
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Received 16 Feb, 2021
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See the published version of this preprint at Applied Biochemistry and Biotechnology.
This is a preprint, a preliminary version of a manuscript that has not completed peer review at a journal. Research Square does not conduct peer review prior to posting preprints. The posting of a preprint on this server should not be interpreted as an endorsement of its validity or suitability for dissemination as established information or for guiding clinical practice.
Learn more about In Review
Research Article
Bo Yang
Qingdao University of Science and Technology
Corresponding Author
Badges
Prescreen
This manuscript passed our Prescreen assessment
Complete author information
Appropriate declaration statements
Potential risks to human health
Prescreen
Peer Review Timeline
CURRENT STATUS: Published
View the published article at Applied Biochemistry and Biotechnology.
Version 1
Posted 18 Feb, 2021
No community comments so far
Reviews received
Received 16 Feb, 2021
Reviewers invited
Invitations sent on 15 Feb, 2021
Editor invited
On 01 Feb, 2021
First submitted
On 31 Jan, 2021
Metrics
Comments: 0
PDF Downloads: ...
HTML Views: ...
License:
This work is licensed under a CC BY 4.0 License. Read Full License
View the published article at Applied Biochemistry and Biotechnology.
Amino modified mesoporous silica (SBA-15-NH2) was prepared by hydrothermal method, which is a kind of excellent carrier for enzyme immobilization. The structure of SBA-15 was characterized by SEM and FTIR, which proved that amino group was successfully attached to the surface of SBA-15. The carrier had good mesoporous structure by nitrogen adsorption and desorption test. Using SBA-15-NH2 as the carrier, the optimal conditions of laccase immobilization by two different cross-linking methods were explored. At the same time, the properties of immobilized enzyme and free enzyme were compared. The results showed that the activity of immobilized laccase by two-step method (2977.5 U/g) was much higher than that by one-step method (239.5 U/g). The optimal conditions were as follows: free laccase (35℃, pH = 4.5), two-step immobilized laccase (40℃, pH = 4.0), one-step immobilized laccase (35℃, pH = 4.0). The two-step method was more adaptable to temperature. The pH adaptation range of immobilized enzyme was wider, and the thermal stability was greatly enhanced. After five cycles of repeated reaction, the residual enzyme activity of two-step and one-step methods were 56% and 43% of the original. The treatment of simulated wastewater containing 2,4-dichlorophenol (2,4-DCP) by immobilized laccase was also studied. Under the optimum conditions (40℃, pH = 5.0, 20 mg/L), the removal of 2,4-DCP can reach 89.06%.
Figure 1
Figure 2
Figure 3
Figure 4
Figure 5
Figure 6
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Figure 8
Figure 9
Figure 10
Figure 11
Figure 12
Figure 13
Figure 14
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Figure 16
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