Immobilized penicillin G acylase with enhanced activity and stability using glutaraldehyde-modified polydopamine-coated Fe 3 O 4 nanoparticles
In this work, Fe O nanoparticles (NPs) were coated with polydopamine (PDA) to structure Fe O @PDA NPs by the spontaneous oxygen-mediated self-polymerization of dopamine (DA) in an aqueous solution of pH = 8.5. The fabricated Fe O @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, Fe
O
nanoparticles (NPs) were coated with polydopamine (PDA) to structure Fe
O
@PDA NPs by the spontaneous oxygen-mediated self-polymerization of dopamine (DA) in an aqueous solution of pH = 8.5. The fabricated Fe
O
@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. |
| doi_str_mv | 10.1002/bab.2138 |
| format | Article |
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O
nanoparticles (NPs) were coated with polydopamine (PDA) to structure Fe
O
@PDA NPs by the spontaneous oxygen-mediated self-polymerization of dopamine (DA) in an aqueous solution of pH = 8.5. The fabricated Fe
O
@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.</description><identifier>ISSN: 0885-4513</identifier><identifier>EISSN: 1470-8744</identifier><identifier>DOI: 10.1002/bab.2138</identifier><identifier>PMID: 33650711</identifier><language>eng</language><publisher>United States</publisher><subject>Enzyme Stability ; Enzymes, Immobilized - chemistry ; Glutaral - chemistry ; Hydrogen-Ion Concentration ; Indoles ; Magnetite Nanoparticles - chemistry ; Nanoparticles - chemistry ; Penicillin Amidase - chemistry ; Polymers ; Temperature</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><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c951-146ef83a384aa50e49c0ac267704b1e75815d9ad44ed66c82467f09431df70aa3</citedby><cites>FETCH-LOGICAL-c951-146ef83a384aa50e49c0ac267704b1e75815d9ad44ed66c82467f09431df70aa3</cites><orcidid>0000-0002-9119-1126 ; 0000-0003-1291-6078</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/33650711$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></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 Fe 3 O 4 nanoparticles</title><title>Biotechnology and applied biochemistry</title><addtitle>Biotechnol Appl Biochem</addtitle><description>In this work, Fe
O
nanoparticles (NPs) were coated with polydopamine (PDA) to structure Fe
O
@PDA NPs by the spontaneous oxygen-mediated self-polymerization of dopamine (DA) in an aqueous solution of pH = 8.5. The fabricated Fe
O
@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.</description><subject>Enzyme Stability</subject><subject>Enzymes, Immobilized - chemistry</subject><subject>Glutaral - chemistry</subject><subject>Hydrogen-Ion Concentration</subject><subject>Indoles</subject><subject>Magnetite Nanoparticles - chemistry</subject><subject>Nanoparticles - chemistry</subject><subject>Penicillin Amidase - chemistry</subject><subject>Polymers</subject><subject>Temperature</subject><issn>0885-4513</issn><issn>1470-8744</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kEFOwzAQRS0EoqUgcQLkJZsUO3Zid4kqWpAqddN9NLEnrZHjVHEKCofgzCQqsBrN_Dd_8Qi552zOGUufSijnKRf6gky5VCzRSspLMmVaZ4nMuJiQmxjfGWNa6fSaTITIM6Y4n5Lvt7puSufdF1p6xOCM894FuqZgeg8R6afrDhTDAYIZEDCd-3BdTyFYGjsYX4ftFF3Y070_ddCCt3joLSZ1Y13lxt7G97Y5Qu0CJqaBbritkAq6pZIGCEPUds54jLfkqgIf8e53zshu9bJbviab7fpt-bxJzCLjCZc5VlqA0BIgYygXhoFJc6WYLDmqTPPMLsBKiTbPjU5lriq2kILbSjEAMSOP51rTNjG2WBXH1tXQ9gVnxWi0GIwWo9EBfTijx1NZo_0H_xSKH0PRc4k</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><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</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 Fe 3 O 4 nanoparticles</title><author>Zhang, Boyuan ; Zhou, Yongshan ; Liu, Chunli ; Abdelrahman Mohammed, Monier Alhadi ; Chen, Zhangjun ; Chen, Zhenbin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c951-146ef83a384aa50e49c0ac267704b1e75815d9ad44ed66c82467f09431df70aa3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Enzyme Stability</topic><topic>Enzymes, Immobilized - chemistry</topic><topic>Glutaral - chemistry</topic><topic>Hydrogen-Ion Concentration</topic><topic>Indoles</topic><topic>Magnetite Nanoparticles - chemistry</topic><topic>Nanoparticles - chemistry</topic><topic>Penicillin Amidase - chemistry</topic><topic>Polymers</topic><topic>Temperature</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><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><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><jtitle>Biotechnology and applied biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhang, Boyuan</au><au>Zhou, Yongshan</au><au>Liu, Chunli</au><au>Abdelrahman Mohammed, Monier Alhadi</au><au>Chen, Zhangjun</au><au>Chen, Zhenbin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Immobilized penicillin G acylase with enhanced activity and stability using glutaraldehyde-modified polydopamine-coated Fe 3 O 4 nanoparticles</atitle><jtitle>Biotechnology and applied biochemistry</jtitle><addtitle>Biotechnol Appl Biochem</addtitle><date>2022-04</date><risdate>2022</risdate><volume>69</volume><issue>2</issue><spage>629</spage><epage>641</epage><pages>629-641</pages><issn>0885-4513</issn><eissn>1470-8744</eissn><abstract>In this work, Fe
O
nanoparticles (NPs) were coated with polydopamine (PDA) to structure Fe
O
@PDA NPs by the spontaneous oxygen-mediated self-polymerization of dopamine (DA) in an aqueous solution of pH = 8.5. The fabricated Fe
O
@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.</abstract><cop>United States</cop><pmid>33650711</pmid><doi>10.1002/bab.2138</doi><tpages>13</tpages><orcidid>https://orcid.org/0000-0002-9119-1126</orcidid><orcidid>https://orcid.org/0000-0003-1291-6078</orcidid></addata></record> |
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| ispartof | Biotechnology and applied biochemistry, 2022-04, Vol.69 (2), p.629-641 |
| issn | 0885-4513 1470-8744 |
| language | eng |
| recordid | cdi_crossref_primary_10_1002_bab_2138 |
| source | MEDLINE; Wiley Online Library Journals Frontfile Complete |
| subjects | Enzyme Stability Enzymes, Immobilized - chemistry Glutaral - chemistry Hydrogen-Ion Concentration Indoles Magnetite Nanoparticles - chemistry Nanoparticles - chemistry Penicillin Amidase - chemistry Polymers Temperature |
| title | Immobilized penicillin G acylase with enhanced activity and stability using glutaraldehyde-modified polydopamine-coated Fe 3 O 4 nanoparticles |
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