Catalytic Biomaterials for Atrazine Degradation
In this paper, triazine hydrolase from <i>Arthrobacter aurescens</i> TC1 (TrzN) was successfully immobilized in alginate beads (TrzN:alginate), alginate beads coated in chitosan (TrzN:chitosan), and tetramethylorthosilicate (TMOS) gels using the sol–gel method (TrzN:sol–gel) for the firs...
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| Format: | Article |
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MDPI AG
2023-01-01
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| Series: | Catalysts |
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| Online Access: | https://www.mdpi.com/2073-4344/13/1/140 |
| _version_ | 1797444588805292032 |
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| author | Karla Diviesti Richard C. Holz |
| author_facet | Karla Diviesti Richard C. Holz |
| author_sort | Karla Diviesti |
| collection | DOAJ |
| description | In this paper, triazine hydrolase from <i>Arthrobacter aurescens</i> TC1 (TrzN) was successfully immobilized in alginate beads (TrzN:alginate), alginate beads coated in chitosan (TrzN:chitosan), and tetramethylorthosilicate (TMOS) gels using the sol–gel method (TrzN:sol–gel) for the first time. TrzN:alginate and TrzN:chitosan hydrolyzed 50 µM of atrazine in 6 h with negligible protein loss with an ~80% conversion rate. However, the TrzN:sol–gel biomaterial converted >95% of a 50 µM atrazine solution in an hour with negligible protein loss. The treatment of each of these biomaterials with trypsin confirmed that the catalytic activity was due to the encapsulated enzyme and not surface-bound TrzN. All three of the biomaterials showed potential for long-term storage and reuse, with the only limitation arising from the loss of protein in the storage buffer for the TrzN:alginate and TrzN:chitosan biomaterials, not the denaturation of the encapsulated TrzN. TrzN:sol–gel stood out, with ~100% activity being retained after 10 consecutive reactions. Additionally, the materials stayed active in methanol concentrations <10%, suggesting the ability to increase the solubility of atrazine with organic solvents. The structural integrity of the TrzN:alginate and TrzN:chitosan materials became limiting in extreme pH conditions, while TrzN:sol–gel outperformed WT TrzN. Overall, the TrzN:sol–gel biomaterial proved to be the best atrazine dichlorination biocatalyst. As sol–gels can be cast into any desired shape, including pellets, which can be used in columns, the TrzN:sol–gel biomaterial provides a new avenue for the design of bioremediation methodologies for the removal of atrazine from the environment. |
| first_indexed | 2024-03-09T13:14:46Z |
| format | Article |
| id | doaj.art-a3a0fb75cd204d6f91ba5c9129d660a5 |
| institution | Directory Open Access Journal |
| issn | 2073-4344 |
| language | English |
| last_indexed | 2024-03-09T13:14:46Z |
| publishDate | 2023-01-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Catalysts |
| spelling | doaj.art-a3a0fb75cd204d6f91ba5c9129d660a52023-11-30T21:37:52ZengMDPI AGCatalysts2073-43442023-01-0113114010.3390/catal13010140Catalytic Biomaterials for Atrazine DegradationKarla Diviesti0Richard C. Holz1Department of Chemistry, Colorado School of Mines, Golden, CO 80401, USADepartment of Chemistry, Colorado School of Mines, Golden, CO 80401, USAIn this paper, triazine hydrolase from <i>Arthrobacter aurescens</i> TC1 (TrzN) was successfully immobilized in alginate beads (TrzN:alginate), alginate beads coated in chitosan (TrzN:chitosan), and tetramethylorthosilicate (TMOS) gels using the sol–gel method (TrzN:sol–gel) for the first time. TrzN:alginate and TrzN:chitosan hydrolyzed 50 µM of atrazine in 6 h with negligible protein loss with an ~80% conversion rate. However, the TrzN:sol–gel biomaterial converted >95% of a 50 µM atrazine solution in an hour with negligible protein loss. The treatment of each of these biomaterials with trypsin confirmed that the catalytic activity was due to the encapsulated enzyme and not surface-bound TrzN. All three of the biomaterials showed potential for long-term storage and reuse, with the only limitation arising from the loss of protein in the storage buffer for the TrzN:alginate and TrzN:chitosan biomaterials, not the denaturation of the encapsulated TrzN. TrzN:sol–gel stood out, with ~100% activity being retained after 10 consecutive reactions. Additionally, the materials stayed active in methanol concentrations <10%, suggesting the ability to increase the solubility of atrazine with organic solvents. The structural integrity of the TrzN:alginate and TrzN:chitosan materials became limiting in extreme pH conditions, while TrzN:sol–gel outperformed WT TrzN. Overall, the TrzN:sol–gel biomaterial proved to be the best atrazine dichlorination biocatalyst. As sol–gels can be cast into any desired shape, including pellets, which can be used in columns, the TrzN:sol–gel biomaterial provides a new avenue for the design of bioremediation methodologies for the removal of atrazine from the environment.https://www.mdpi.com/2073-4344/13/1/140zincdehalogenasebiomaterialskinetics |
| spellingShingle | Karla Diviesti Richard C. Holz Catalytic Biomaterials for Atrazine Degradation Catalysts zinc dehalogenase biomaterials kinetics |
| title | Catalytic Biomaterials for Atrazine Degradation |
| title_full | Catalytic Biomaterials for Atrazine Degradation |
| title_fullStr | Catalytic Biomaterials for Atrazine Degradation |
| title_full_unstemmed | Catalytic Biomaterials for Atrazine Degradation |
| title_short | Catalytic Biomaterials for Atrazine Degradation |
| title_sort | catalytic biomaterials for atrazine degradation |
| topic | zinc dehalogenase biomaterials kinetics |
| url | https://www.mdpi.com/2073-4344/13/1/140 |
| work_keys_str_mv | AT karladiviesti catalyticbiomaterialsforatrazinedegradation AT richardcholz catalyticbiomaterialsforatrazinedegradation |