Immobilized penicillin G acylase with enhanced activity and stability using glutaraldehyde‐modified polydopamine‐coated Fe3O4 nanoparticles
In this work, Fe3O4 nanoparticles (NPs) were coated with polydopamine (PDA) to structure Fe3O4@PDA NPs by the spontaneous oxygen‐mediated self‐polymerization of dopamine (DA) in an aqueous solution of pH = 8.5. The fabricated Fe3O4@PDA NPs were grafted by glutaraldehyde to realize the immobilization...
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| Veröffentlicht in: | Biotechnology and applied biochemistry 2022-04, Vol.69 (2), p.629-641 |
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| creator | Zhang, Boyuan Zhou, Yongshan Liu, Chunli Abdelrahman Mohammed, Monier Alhadi Chen, Zhangjun Chen, Zhenbin |
| description | In this work, Fe3O4 nanoparticles (NPs) were coated with polydopamine (PDA) to structure Fe3O4@PDA NPs by the spontaneous oxygen‐mediated self‐polymerization of dopamine (DA) in an aqueous solution of pH = 8.5. The fabricated Fe3O4@PDA NPs were grafted by glutaraldehyde to realize the immobilization of penicillin G acylase (PGA) under mild conditions. The carriers of each stage were characterized and investigated by transmission electron microscopy, X‐ray diffraction, Fourier transform infrared, and vibrating sample magnetometry. To improve the catalytic activity and stability of immobilized PGA, the immobilization conditions were investigated and optimized. Under the optimal immobilization conditions, the enzyme loading capacity, enzyme activity, and enzyme activity recovery of immobilized PGA were 114 mg/g, 26,308 U/g, and 78.5%, respectively. In addition, the immobilized PGA presented better temperature and pH stability compared with free PGA. The reusability study ensured that the immobilized PGA showed an excellent repeating application performance. In particular, the recovery rate of immobilized PGA could reach 94.8% and immobilized PGA could retain 73.0% of its original activity after 12 cycles, indicating that the immobilized PGA exhibited a high operation stability and broad application potential in the biocatalysis field.
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| doi_str_mv | 10.1002/bab.2138 |
| format | Article |
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Graphical :</description><identifier>ISSN: 0885-4513</identifier><identifier>EISSN: 1470-8744</identifier><identifier>DOI: 10.1002/bab.2138</identifier><language>eng</language><publisher>Calgary: Wiley Subscription Services, Inc</publisher><subject>Antibiotics ; Aqueous solutions ; Catalysis ; Catalytic activity ; Dopamine ; Enzymatic activity ; Enzyme activity ; Enzymes ; Fe3O4 nanoparticles ; Fourier transforms ; Glutaraldehyde ; Immobilization ; Iron oxides ; Magnetic measurement ; Nanoparticles ; Penicillin ; Penicillin G acylase ; pH effects ; polydopamine ; Recovery ; Stability ; Transmission electron microscopy</subject><ispartof>Biotechnology and applied biochemistry, 2022-04, Vol.69 (2), p.629-641</ispartof><rights>2021 International Union of Biochemistry and Molecular Biology, Inc.</rights><rights>2022 International Union of Biochemistry and Molecular Biology, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><orcidid>0000-0002-9119-1126 ; 0000-0003-1291-6078</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fbab.2138$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fbab.2138$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1416,27922,27923,45572,45573</link.rule.ids></links><search><creatorcontrib>Zhang, Boyuan</creatorcontrib><creatorcontrib>Zhou, Yongshan</creatorcontrib><creatorcontrib>Liu, Chunli</creatorcontrib><creatorcontrib>Abdelrahman Mohammed, Monier Alhadi</creatorcontrib><creatorcontrib>Chen, Zhangjun</creatorcontrib><creatorcontrib>Chen, Zhenbin</creatorcontrib><title>Immobilized penicillin G acylase with enhanced activity and stability using glutaraldehyde‐modified polydopamine‐coated Fe3O4 nanoparticles</title><title>Biotechnology and applied biochemistry</title><description>In this work, Fe3O4 nanoparticles (NPs) were coated with polydopamine (PDA) to structure Fe3O4@PDA NPs by the spontaneous oxygen‐mediated self‐polymerization of dopamine (DA) in an aqueous solution of pH = 8.5. The fabricated Fe3O4@PDA NPs were grafted by glutaraldehyde to realize the immobilization of penicillin G acylase (PGA) under mild conditions. The carriers of each stage were characterized and investigated by transmission electron microscopy, X‐ray diffraction, Fourier transform infrared, and vibrating sample magnetometry. To improve the catalytic activity and stability of immobilized PGA, the immobilization conditions were investigated and optimized. Under the optimal immobilization conditions, the enzyme loading capacity, enzyme activity, and enzyme activity recovery of immobilized PGA were 114 mg/g, 26,308 U/g, and 78.5%, respectively. In addition, the immobilized PGA presented better temperature and pH stability compared with free PGA. The reusability study ensured that the immobilized PGA showed an excellent repeating application performance. In particular, the recovery rate of immobilized PGA could reach 94.8% and immobilized PGA could retain 73.0% of its original activity after 12 cycles, indicating that the immobilized PGA exhibited a high operation stability and broad application potential in the biocatalysis field.
Graphical :</description><subject>Antibiotics</subject><subject>Aqueous solutions</subject><subject>Catalysis</subject><subject>Catalytic activity</subject><subject>Dopamine</subject><subject>Enzymatic activity</subject><subject>Enzyme activity</subject><subject>Enzymes</subject><subject>Fe3O4 nanoparticles</subject><subject>Fourier transforms</subject><subject>Glutaraldehyde</subject><subject>Immobilization</subject><subject>Iron oxides</subject><subject>Magnetic measurement</subject><subject>Nanoparticles</subject><subject>Penicillin</subject><subject>Penicillin G acylase</subject><subject>pH effects</subject><subject>polydopamine</subject><subject>Recovery</subject><subject>Stability</subject><subject>Transmission electron microscopy</subject><issn>0885-4513</issn><issn>1470-8744</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><recordid>eNotkEFOwzAQRS0EEqUgcQRLrFNsx7GdZVvRUqlSN7C2Jo7TunKckKSgsOIGcEZOQqKy-po_f_5ID6F7SmaUEPaYQTZjNFYXaEK5JJGSnF-iCVEqiXhC42t007ZHQoiSik3Q96Ysq8x592lzXNvgjPPeBbzGYHoPrcUfrjtgGw4QzBAB07l31_UYQo7bDsbTYTq1Luzx3p86aMDn9tDn9vfrp6xyV7ixufJ9XtVQujD6poJucFc23nEcIAybpnPG2_YWXRXgW3v3r1P0unp6WT5H2916s5xvo5oxqiKWFzxL04SkvCgyQeKcJ5AKSphlUibGSCEJt1ZlJBaCSxAQF9IQlSiWMiHiKXo499ZN9XaybaeP1akJw0vNRMII5SylQyo6pz6ct72uG1dC02tK9MhaD6z1yFov5otR4z9ecHc0</recordid><startdate>202204</startdate><enddate>202204</enddate><creator>Zhang, Boyuan</creator><creator>Zhou, Yongshan</creator><creator>Liu, Chunli</creator><creator>Abdelrahman Mohammed, Monier Alhadi</creator><creator>Chen, Zhangjun</creator><creator>Chen, Zhenbin</creator><general>Wiley Subscription Services, Inc</general><scope>7QL</scope><scope>7QO</scope><scope>7T7</scope><scope>7TB</scope><scope>7TK</scope><scope>7U5</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>K9.</scope><scope>L7M</scope><scope>M7N</scope><scope>P64</scope><orcidid>https://orcid.org/0000-0002-9119-1126</orcidid><orcidid>https://orcid.org/0000-0003-1291-6078</orcidid></search><sort><creationdate>202204</creationdate><title>Immobilized penicillin G acylase with enhanced activity and stability using glutaraldehyde‐modified polydopamine‐coated Fe3O4 nanoparticles</title><author>Zhang, Boyuan ; 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The fabricated Fe3O4@PDA NPs were grafted by glutaraldehyde to realize the immobilization of penicillin G acylase (PGA) under mild conditions. The carriers of each stage were characterized and investigated by transmission electron microscopy, X‐ray diffraction, Fourier transform infrared, and vibrating sample magnetometry. To improve the catalytic activity and stability of immobilized PGA, the immobilization conditions were investigated and optimized. Under the optimal immobilization conditions, the enzyme loading capacity, enzyme activity, and enzyme activity recovery of immobilized PGA were 114 mg/g, 26,308 U/g, and 78.5%, respectively. In addition, the immobilized PGA presented better temperature and pH stability compared with free PGA. The reusability study ensured that the immobilized PGA showed an excellent repeating application performance. In particular, the recovery rate of immobilized PGA could reach 94.8% and immobilized PGA could retain 73.0% of its original activity after 12 cycles, indicating that the immobilized PGA exhibited a high operation stability and broad application potential in the biocatalysis field.
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| source | Wiley Online Library Journals Frontfile Complete |
| subjects | Antibiotics Aqueous solutions Catalysis Catalytic activity Dopamine Enzymatic activity Enzyme activity Enzymes Fe3O4 nanoparticles Fourier transforms Glutaraldehyde Immobilization Iron oxides Magnetic measurement Nanoparticles Penicillin Penicillin G acylase pH effects polydopamine Recovery Stability Transmission electron microscopy |
| title | Immobilized penicillin G acylase with enhanced activity and stability using glutaraldehyde‐modified polydopamine‐coated Fe3O4 nanoparticles |
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