Further stabilization of lipase from
The lipase from Pseudomonas fluorescens (PFL) was adsorbed on superparamagnetic NiZnFe2O4 octyl-nanoparticles via interfacial activation, producing the biocatalyst OCTYL-NANO-PFL. In order to further improve the stability of the immobilized lipase, the immobilized enzyme biocatalyst was chemically m...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Rios, Nathalia Saraiva [verfasserIn] Morais, Eva Gomes [verfasserIn] dos Santos Galvão, Wesley [verfasserIn] Andrade Neto, Davino M. [verfasserIn] dos Santos, José Cleiton Sousa [verfasserIn] Bohn, Felipe [verfasserIn] Correa, Marcio A. [verfasserIn] Fechine, Pierre Basílio Almeida [verfasserIn] Fernandez-Lafuente, Roberto [verfasserIn] Gonçalves, Luciana Rocha Barros [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2019 |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: International journal of biological macromolecules - New York, NY [u.a.] : Elsevier, 1979, 141, Seite 313-324 |
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| Übergeordnetes Werk: |
volume:141 ; pages:313-324 |
| DOI / URN: |
10.1016/j.ijbiomac.2019.09.003 |
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| 520 | |a The lipase from Pseudomonas fluorescens (PFL) was adsorbed on superparamagnetic NiZnFe2O4 octyl-nanoparticles via interfacial activation, producing the biocatalyst OCTYL-NANO-PFL. In order to further improve the stability of the immobilized lipase, the immobilized enzyme biocatalyst was chemically modified with different concentrations of diverse bifunctional molecules (glutaraldehyde (GA), divinylsulfone (DVS) or p-benzoquinone (BQ)). The concentrations of bifunctional agents were varied (0.5, 1, 2.5 and 5% (v/v for GA and DVS and w/v for BQ)). The results showed a greatly improved stability after chemical modification with all bifunctional molecules, mainly with 5% (v/v) GA or 1% (v/v) DVS. The biocatalysts OCTYL-NANO-PFL-GA 5% and -DVS 1% were about 60 folds more stable at pH 7 than the unmodified preparation and, at pH 5, >200 folds for 5% GA modified enzyme. The most stable BQ treated biocatalysts, OCTYL-NANO-PFL-BQ 0.5%, was about 8.3 more stable than OCTYL-NANO-PFL at pH 7, while was 20 fold more stable at pH 9. | ||
| 650 | 4 | |a Interfacial activation | |
| 650 | 4 | |a Intermolecular crosslinking | |
| 650 | 4 | |a Solid phase chemical modification | |
| 650 | 4 | |a Prevention of enzyme release | |
| 700 | 1 | |a Morais, Eva Gomes |e verfasserin |4 aut | |
| 700 | 1 | |a dos Santos Galvão, Wesley |e verfasserin |4 aut | |
| 700 | 1 | |a Andrade Neto, Davino M. |e verfasserin |4 aut | |
| 700 | 1 | |a dos Santos, José Cleiton Sousa |e verfasserin |4 aut | |
| 700 | 1 | |a Bohn, Felipe |e verfasserin |4 aut | |
| 700 | 1 | |a Correa, Marcio A. |e verfasserin |4 aut | |
| 700 | 1 | |a Fechine, Pierre Basílio Almeida |e verfasserin |4 aut | |
| 700 | 1 | |a Fernandez-Lafuente, Roberto |e verfasserin |4 aut | |
| 700 | 1 | |a Gonçalves, Luciana Rocha Barros |e verfasserin |4 aut | |
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10.1016/j.ijbiomac.2019.09.003 doi (DE-627)ELV003364569 (ELSEVIER)S0141-8130(19)36234-8 DE-627 ger DE-627 rda eng 540 570 DE-600 BIODIV DE-30 fid 35.80 bkl 58.30 bkl Rios, Nathalia Saraiva verfasserin aut Further stabilization of lipase from 2019 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The lipase from Pseudomonas fluorescens (PFL) was adsorbed on superparamagnetic NiZnFe2O4 octyl-nanoparticles via interfacial activation, producing the biocatalyst OCTYL-NANO-PFL. In order to further improve the stability of the immobilized lipase, the immobilized enzyme biocatalyst was chemically modified with different concentrations of diverse bifunctional molecules (glutaraldehyde (GA), divinylsulfone (DVS) or p-benzoquinone (BQ)). The concentrations of bifunctional agents were varied (0.5, 1, 2.5 and 5% (v/v for GA and DVS and w/v for BQ)). The results showed a greatly improved stability after chemical modification with all bifunctional molecules, mainly with 5% (v/v) GA or 1% (v/v) DVS. The biocatalysts OCTYL-NANO-PFL-GA 5% and -DVS 1% were about 60 folds more stable at pH 7 than the unmodified preparation and, at pH 5, >200 folds for 5% GA modified enzyme. The most stable BQ treated biocatalysts, OCTYL-NANO-PFL-BQ 0.5%, was about 8.3 more stable than OCTYL-NANO-PFL at pH 7, while was 20 fold more stable at pH 9. Interfacial activation Intermolecular crosslinking Solid phase chemical modification Prevention of enzyme release Morais, Eva Gomes verfasserin aut dos Santos Galvão, Wesley verfasserin aut Andrade Neto, Davino M. verfasserin aut dos Santos, José Cleiton Sousa verfasserin aut Bohn, Felipe verfasserin aut Correa, Marcio A. verfasserin aut Fechine, Pierre Basílio Almeida verfasserin aut Fernandez-Lafuente, Roberto verfasserin aut Gonçalves, Luciana Rocha Barros verfasserin aut Enthalten in International journal of biological macromolecules New York, NY [u.a.] : Elsevier, 1979 141, Seite 313-324 Online-Ressource (DE-627)30089502X (DE-600)1483284-7 (DE-576)259270814 1879-0003 nnns volume:141 pages:313-324 GBV_USEFLAG_U SYSFLAG_U GBV_ELV FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.80 Makromolekulare Chemie 58.30 Biotechnologie AR 141 313-324 |
| spelling |
10.1016/j.ijbiomac.2019.09.003 doi (DE-627)ELV003364569 (ELSEVIER)S0141-8130(19)36234-8 DE-627 ger DE-627 rda eng 540 570 DE-600 BIODIV DE-30 fid 35.80 bkl 58.30 bkl Rios, Nathalia Saraiva verfasserin aut Further stabilization of lipase from 2019 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The lipase from Pseudomonas fluorescens (PFL) was adsorbed on superparamagnetic NiZnFe2O4 octyl-nanoparticles via interfacial activation, producing the biocatalyst OCTYL-NANO-PFL. In order to further improve the stability of the immobilized lipase, the immobilized enzyme biocatalyst was chemically modified with different concentrations of diverse bifunctional molecules (glutaraldehyde (GA), divinylsulfone (DVS) or p-benzoquinone (BQ)). The concentrations of bifunctional agents were varied (0.5, 1, 2.5 and 5% (v/v for GA and DVS and w/v for BQ)). The results showed a greatly improved stability after chemical modification with all bifunctional molecules, mainly with 5% (v/v) GA or 1% (v/v) DVS. The biocatalysts OCTYL-NANO-PFL-GA 5% and -DVS 1% were about 60 folds more stable at pH 7 than the unmodified preparation and, at pH 5, >200 folds for 5% GA modified enzyme. The most stable BQ treated biocatalysts, OCTYL-NANO-PFL-BQ 0.5%, was about 8.3 more stable than OCTYL-NANO-PFL at pH 7, while was 20 fold more stable at pH 9. Interfacial activation Intermolecular crosslinking Solid phase chemical modification Prevention of enzyme release Morais, Eva Gomes verfasserin aut dos Santos Galvão, Wesley verfasserin aut Andrade Neto, Davino M. verfasserin aut dos Santos, José Cleiton Sousa verfasserin aut Bohn, Felipe verfasserin aut Correa, Marcio A. verfasserin aut Fechine, Pierre Basílio Almeida verfasserin aut Fernandez-Lafuente, Roberto verfasserin aut Gonçalves, Luciana Rocha Barros verfasserin aut Enthalten in International journal of biological macromolecules New York, NY [u.a.] : Elsevier, 1979 141, Seite 313-324 Online-Ressource (DE-627)30089502X (DE-600)1483284-7 (DE-576)259270814 1879-0003 nnns volume:141 pages:313-324 GBV_USEFLAG_U SYSFLAG_U GBV_ELV FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.80 Makromolekulare Chemie 58.30 Biotechnologie AR 141 313-324 |
| allfields_unstemmed |
10.1016/j.ijbiomac.2019.09.003 doi (DE-627)ELV003364569 (ELSEVIER)S0141-8130(19)36234-8 DE-627 ger DE-627 rda eng 540 570 DE-600 BIODIV DE-30 fid 35.80 bkl 58.30 bkl Rios, Nathalia Saraiva verfasserin aut Further stabilization of lipase from 2019 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The lipase from Pseudomonas fluorescens (PFL) was adsorbed on superparamagnetic NiZnFe2O4 octyl-nanoparticles via interfacial activation, producing the biocatalyst OCTYL-NANO-PFL. In order to further improve the stability of the immobilized lipase, the immobilized enzyme biocatalyst was chemically modified with different concentrations of diverse bifunctional molecules (glutaraldehyde (GA), divinylsulfone (DVS) or p-benzoquinone (BQ)). The concentrations of bifunctional agents were varied (0.5, 1, 2.5 and 5% (v/v for GA and DVS and w/v for BQ)). The results showed a greatly improved stability after chemical modification with all bifunctional molecules, mainly with 5% (v/v) GA or 1% (v/v) DVS. The biocatalysts OCTYL-NANO-PFL-GA 5% and -DVS 1% were about 60 folds more stable at pH 7 than the unmodified preparation and, at pH 5, >200 folds for 5% GA modified enzyme. The most stable BQ treated biocatalysts, OCTYL-NANO-PFL-BQ 0.5%, was about 8.3 more stable than OCTYL-NANO-PFL at pH 7, while was 20 fold more stable at pH 9. Interfacial activation Intermolecular crosslinking Solid phase chemical modification Prevention of enzyme release Morais, Eva Gomes verfasserin aut dos Santos Galvão, Wesley verfasserin aut Andrade Neto, Davino M. verfasserin aut dos Santos, José Cleiton Sousa verfasserin aut Bohn, Felipe verfasserin aut Correa, Marcio A. verfasserin aut Fechine, Pierre Basílio Almeida verfasserin aut Fernandez-Lafuente, Roberto verfasserin aut Gonçalves, Luciana Rocha Barros verfasserin aut Enthalten in International journal of biological macromolecules New York, NY [u.a.] : Elsevier, 1979 141, Seite 313-324 Online-Ressource (DE-627)30089502X (DE-600)1483284-7 (DE-576)259270814 1879-0003 nnns volume:141 pages:313-324 GBV_USEFLAG_U SYSFLAG_U GBV_ELV FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.80 Makromolekulare Chemie 58.30 Biotechnologie AR 141 313-324 |
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10.1016/j.ijbiomac.2019.09.003 doi (DE-627)ELV003364569 (ELSEVIER)S0141-8130(19)36234-8 DE-627 ger DE-627 rda eng 540 570 DE-600 BIODIV DE-30 fid 35.80 bkl 58.30 bkl Rios, Nathalia Saraiva verfasserin aut Further stabilization of lipase from 2019 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The lipase from Pseudomonas fluorescens (PFL) was adsorbed on superparamagnetic NiZnFe2O4 octyl-nanoparticles via interfacial activation, producing the biocatalyst OCTYL-NANO-PFL. In order to further improve the stability of the immobilized lipase, the immobilized enzyme biocatalyst was chemically modified with different concentrations of diverse bifunctional molecules (glutaraldehyde (GA), divinylsulfone (DVS) or p-benzoquinone (BQ)). The concentrations of bifunctional agents were varied (0.5, 1, 2.5 and 5% (v/v for GA and DVS and w/v for BQ)). The results showed a greatly improved stability after chemical modification with all bifunctional molecules, mainly with 5% (v/v) GA or 1% (v/v) DVS. The biocatalysts OCTYL-NANO-PFL-GA 5% and -DVS 1% were about 60 folds more stable at pH 7 than the unmodified preparation and, at pH 5, >200 folds for 5% GA modified enzyme. The most stable BQ treated biocatalysts, OCTYL-NANO-PFL-BQ 0.5%, was about 8.3 more stable than OCTYL-NANO-PFL at pH 7, while was 20 fold more stable at pH 9. Interfacial activation Intermolecular crosslinking Solid phase chemical modification Prevention of enzyme release Morais, Eva Gomes verfasserin aut dos Santos Galvão, Wesley verfasserin aut Andrade Neto, Davino M. verfasserin aut dos Santos, José Cleiton Sousa verfasserin aut Bohn, Felipe verfasserin aut Correa, Marcio A. verfasserin aut Fechine, Pierre Basílio Almeida verfasserin aut Fernandez-Lafuente, Roberto verfasserin aut Gonçalves, Luciana Rocha Barros verfasserin aut Enthalten in International journal of biological macromolecules New York, NY [u.a.] : Elsevier, 1979 141, Seite 313-324 Online-Ressource (DE-627)30089502X (DE-600)1483284-7 (DE-576)259270814 1879-0003 nnns volume:141 pages:313-324 GBV_USEFLAG_U SYSFLAG_U GBV_ELV FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.80 Makromolekulare Chemie 58.30 Biotechnologie AR 141 313-324 |
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10.1016/j.ijbiomac.2019.09.003 doi (DE-627)ELV003364569 (ELSEVIER)S0141-8130(19)36234-8 DE-627 ger DE-627 rda eng 540 570 DE-600 BIODIV DE-30 fid 35.80 bkl 58.30 bkl Rios, Nathalia Saraiva verfasserin aut Further stabilization of lipase from 2019 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The lipase from Pseudomonas fluorescens (PFL) was adsorbed on superparamagnetic NiZnFe2O4 octyl-nanoparticles via interfacial activation, producing the biocatalyst OCTYL-NANO-PFL. In order to further improve the stability of the immobilized lipase, the immobilized enzyme biocatalyst was chemically modified with different concentrations of diverse bifunctional molecules (glutaraldehyde (GA), divinylsulfone (DVS) or p-benzoquinone (BQ)). The concentrations of bifunctional agents were varied (0.5, 1, 2.5 and 5% (v/v for GA and DVS and w/v for BQ)). The results showed a greatly improved stability after chemical modification with all bifunctional molecules, mainly with 5% (v/v) GA or 1% (v/v) DVS. The biocatalysts OCTYL-NANO-PFL-GA 5% and -DVS 1% were about 60 folds more stable at pH 7 than the unmodified preparation and, at pH 5, >200 folds for 5% GA modified enzyme. The most stable BQ treated biocatalysts, OCTYL-NANO-PFL-BQ 0.5%, was about 8.3 more stable than OCTYL-NANO-PFL at pH 7, while was 20 fold more stable at pH 9. Interfacial activation Intermolecular crosslinking Solid phase chemical modification Prevention of enzyme release Morais, Eva Gomes verfasserin aut dos Santos Galvão, Wesley verfasserin aut Andrade Neto, Davino M. verfasserin aut dos Santos, José Cleiton Sousa verfasserin aut Bohn, Felipe verfasserin aut Correa, Marcio A. verfasserin aut Fechine, Pierre Basílio Almeida verfasserin aut Fernandez-Lafuente, Roberto verfasserin aut Gonçalves, Luciana Rocha Barros verfasserin aut Enthalten in International journal of biological macromolecules New York, NY [u.a.] : Elsevier, 1979 141, Seite 313-324 Online-Ressource (DE-627)30089502X (DE-600)1483284-7 (DE-576)259270814 1879-0003 nnns volume:141 pages:313-324 GBV_USEFLAG_U SYSFLAG_U GBV_ELV FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.80 Makromolekulare Chemie 58.30 Biotechnologie AR 141 313-324 |
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English |
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Enthalten in International journal of biological macromolecules 141, Seite 313-324 volume:141 pages:313-324 |
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Enthalten in International journal of biological macromolecules 141, Seite 313-324 volume:141 pages:313-324 |
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Makromolekulare Chemie Biotechnologie |
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findex.gbv.de |
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Interfacial activation Intermolecular crosslinking Solid phase chemical modification Prevention of enzyme release |
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International journal of biological macromolecules |
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Rios, Nathalia Saraiva @@aut@@ Morais, Eva Gomes @@aut@@ dos Santos Galvão, Wesley @@aut@@ Andrade Neto, Davino M. @@aut@@ dos Santos, José Cleiton Sousa @@aut@@ Bohn, Felipe @@aut@@ Correa, Marcio A. @@aut@@ Fechine, Pierre Basílio Almeida @@aut@@ Fernandez-Lafuente, Roberto @@aut@@ Gonçalves, Luciana Rocha Barros @@aut@@ |
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2019-01-01T00:00:00Z |
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30089502X |
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englisch |
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Rios, Nathalia Saraiva |
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540 570 DE-600 BIODIV DE-30 fid 35.80 bkl 58.30 bkl Further stabilization of lipase from Interfacial activation Intermolecular crosslinking Solid phase chemical modification Prevention of enzyme release |
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ddc 540 fid BIODIV bkl 35.80 bkl 58.30 misc Interfacial activation misc Intermolecular crosslinking misc Solid phase chemical modification misc Prevention of enzyme release |
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ddc 540 fid BIODIV bkl 35.80 bkl 58.30 misc Interfacial activation misc Intermolecular crosslinking misc Solid phase chemical modification misc Prevention of enzyme release |
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Further stabilization of lipase from |
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Further stabilization of lipase from |
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Rios, Nathalia Saraiva |
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International journal of biological macromolecules |
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Rios, Nathalia Saraiva Morais, Eva Gomes dos Santos Galvão, Wesley Andrade Neto, Davino M. dos Santos, José Cleiton Sousa Bohn, Felipe Correa, Marcio A. Fechine, Pierre Basílio Almeida Fernandez-Lafuente, Roberto Gonçalves, Luciana Rocha Barros |
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Rios, Nathalia Saraiva |
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10.1016/j.ijbiomac.2019.09.003 |
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further stabilization of lipase from |
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Further stabilization of lipase from |
| abstract |
The lipase from Pseudomonas fluorescens (PFL) was adsorbed on superparamagnetic NiZnFe2O4 octyl-nanoparticles via interfacial activation, producing the biocatalyst OCTYL-NANO-PFL. In order to further improve the stability of the immobilized lipase, the immobilized enzyme biocatalyst was chemically modified with different concentrations of diverse bifunctional molecules (glutaraldehyde (GA), divinylsulfone (DVS) or p-benzoquinone (BQ)). The concentrations of bifunctional agents were varied (0.5, 1, 2.5 and 5% (v/v for GA and DVS and w/v for BQ)). The results showed a greatly improved stability after chemical modification with all bifunctional molecules, mainly with 5% (v/v) GA or 1% (v/v) DVS. The biocatalysts OCTYL-NANO-PFL-GA 5% and -DVS 1% were about 60 folds more stable at pH 7 than the unmodified preparation and, at pH 5, >200 folds for 5% GA modified enzyme. The most stable BQ treated biocatalysts, OCTYL-NANO-PFL-BQ 0.5%, was about 8.3 more stable than OCTYL-NANO-PFL at pH 7, while was 20 fold more stable at pH 9. |
| abstractGer |
The lipase from Pseudomonas fluorescens (PFL) was adsorbed on superparamagnetic NiZnFe2O4 octyl-nanoparticles via interfacial activation, producing the biocatalyst OCTYL-NANO-PFL. In order to further improve the stability of the immobilized lipase, the immobilized enzyme biocatalyst was chemically modified with different concentrations of diverse bifunctional molecules (glutaraldehyde (GA), divinylsulfone (DVS) or p-benzoquinone (BQ)). The concentrations of bifunctional agents were varied (0.5, 1, 2.5 and 5% (v/v for GA and DVS and w/v for BQ)). The results showed a greatly improved stability after chemical modification with all bifunctional molecules, mainly with 5% (v/v) GA or 1% (v/v) DVS. The biocatalysts OCTYL-NANO-PFL-GA 5% and -DVS 1% were about 60 folds more stable at pH 7 than the unmodified preparation and, at pH 5, >200 folds for 5% GA modified enzyme. The most stable BQ treated biocatalysts, OCTYL-NANO-PFL-BQ 0.5%, was about 8.3 more stable than OCTYL-NANO-PFL at pH 7, while was 20 fold more stable at pH 9. |
| abstract_unstemmed |
The lipase from Pseudomonas fluorescens (PFL) was adsorbed on superparamagnetic NiZnFe2O4 octyl-nanoparticles via interfacial activation, producing the biocatalyst OCTYL-NANO-PFL. In order to further improve the stability of the immobilized lipase, the immobilized enzyme biocatalyst was chemically modified with different concentrations of diverse bifunctional molecules (glutaraldehyde (GA), divinylsulfone (DVS) or p-benzoquinone (BQ)). The concentrations of bifunctional agents were varied (0.5, 1, 2.5 and 5% (v/v for GA and DVS and w/v for BQ)). The results showed a greatly improved stability after chemical modification with all bifunctional molecules, mainly with 5% (v/v) GA or 1% (v/v) DVS. The biocatalysts OCTYL-NANO-PFL-GA 5% and -DVS 1% were about 60 folds more stable at pH 7 than the unmodified preparation and, at pH 5, >200 folds for 5% GA modified enzyme. The most stable BQ treated biocatalysts, OCTYL-NANO-PFL-BQ 0.5%, was about 8.3 more stable than OCTYL-NANO-PFL at pH 7, while was 20 fold more stable at pH 9. |
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| title_short |
Further stabilization of lipase from |
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Morais, Eva Gomes dos Santos Galvão, Wesley Andrade Neto, Davino M. dos Santos, José Cleiton Sousa Bohn, Felipe Correa, Marcio A. Fechine, Pierre Basílio Almeida Fernandez-Lafuente, Roberto Gonçalves, Luciana Rocha Barros |
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| score |
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