Oxidized bacterial cellulose membrane as support for enzyme immobilization: properties and morphological features
Abstract Bacterial cellulose (BC) membrane can be architected to covalently immobilize biomolecules, generating materials with new functionality. The processes of purification (via alkaline treatment) and chemical modification (via $ NaIO_{4} $) to the wet BC membrane is the innovation of this work....
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Vasconcelos, Niédja Fittipaldi [verfasserIn] Andrade, Fábia Karine [verfasserIn] Vieira, Lídia de Araújo Pinto [verfasserIn] Vieira, Rodrigo Silveira [verfasserIn] Vaz, Juliana Miguel [verfasserIn] Chevallier, Pascale [verfasserIn] Mantovani, Diego [verfasserIn] Borges, Maria de Fátima [verfasserIn] Rosa, Morsyleide de Freitas [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2020 |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: Cellulose - Dordrecht [u.a.] : Springer Science + Business Media B.V, 1994, 27(2020), 6 vom: 25. Jan., Seite 3055-3083 |
|---|---|
| Übergeordnetes Werk: |
volume:27 ; year:2020 ; number:6 ; day:25 ; month:01 ; pages:3055-3083 |
| Links: |
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| DOI / URN: |
10.1007/s10570-020-02966-5 |
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| Katalog-ID: |
SPR039138615 |
|---|
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| 245 | 1 | 0 | |a Oxidized bacterial cellulose membrane as support for enzyme immobilization: properties and morphological features |
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| 520 | |a Abstract Bacterial cellulose (BC) membrane can be architected to covalently immobilize biomolecules, generating materials with new functionality. The processes of purification (via alkaline treatment) and chemical modification (via $ NaIO_{4} $) to the wet BC membrane is the innovation of this work. This wet oxidized BC (OxBC) membrane could act as a support matrix for covalent immobilization of enzymes. BC produced over 5 days of static fermentation, followed by purification with $ K_{2} %$ CO_{3} $ (BC-5d-$ K_{2} %$ CO_{3} $) was selected for our study due to high porosity and surface area, which are properties that favor its chemical modification. This wet BC membrane proven suitable for $ NaIO_{4} $ oxidation. Time and temperature conditions were evaluated in the oxidation reaction, with oxidation BC (OxBC) performed at 1% (w/v) $ NaIO_{4} $ for 6 h at 55 °C under most advantageous conditions, as it provided 50% oxidation degree and preserved its morphological structure. BC and OxBC were characterized by X-ray diffraction, X-ray photoelectron spectroscopy, Scanning electron microscopy, mechanical test, and thermal analysis. The oxidation reaction decreased BC crystallinity, tensile strength, and thermal stability and compacted the cellulose layers. BC and OxBC showed non-cytotoxicity. Fourier transform infrared confirmed that OxBC can covalently immobilize papain and that after immobilization the enzyme showed a recovered enzymatic activity of 93.1%. In addition, the oxidized membrane presented greater amount of immobilized papain in its study than BC, proving to be a more efficient support for enzymatic immobilization. Graphic abstract | ||
| 650 | 4 | |a Bacterial cellulose |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a K |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a CO |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a purification |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a NaIO |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a oxidation |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Covalent immobilization |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Enzyme |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Wound dressing |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Andrade, Fábia Karine |e verfasserin |4 aut | |
| 700 | 1 | |a Vieira, Lídia de Araújo Pinto |e verfasserin |4 aut | |
| 700 | 1 | |a Vieira, Rodrigo Silveira |e verfasserin |4 aut | |
| 700 | 1 | |a Vaz, Juliana Miguel |e verfasserin |4 aut | |
| 700 | 1 | |a Chevallier, Pascale |e verfasserin |4 aut | |
| 700 | 1 | |a Mantovani, Diego |e verfasserin |4 aut | |
| 700 | 1 | |a Borges, Maria de Fátima |e verfasserin |4 aut | |
| 700 | 1 | |a Rosa, Morsyleide de Freitas |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Cellulose |d Dordrecht [u.a.] : Springer Science + Business Media B.V, 1994 |g 27(2020), 6 vom: 25. Jan., Seite 3055-3083 |w (DE-627)306353857 |w (DE-600)1496831-9 |x 1572-882X |7 nnns |
| 773 | 1 | 8 | |g volume:27 |g year:2020 |g number:6 |g day:25 |g month:01 |g pages:3055-3083 |
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10.1007/s10570-020-02966-5 doi (DE-627)SPR039138615 (SPR)s10570-020-02966-5-e DE-627 ger DE-627 rakwb eng 540 ASE 35.63 bkl 35.77 bkl Vasconcelos, Niédja Fittipaldi verfasserin aut Oxidized bacterial cellulose membrane as support for enzyme immobilization: properties and morphological features 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Bacterial cellulose (BC) membrane can be architected to covalently immobilize biomolecules, generating materials with new functionality. The processes of purification (via alkaline treatment) and chemical modification (via $ NaIO_{4} $) to the wet BC membrane is the innovation of this work. This wet oxidized BC (OxBC) membrane could act as a support matrix for covalent immobilization of enzymes. BC produced over 5 days of static fermentation, followed by purification with $ K_{2} %$ CO_{3} $ (BC-5d-$ K_{2} %$ CO_{3} $) was selected for our study due to high porosity and surface area, which are properties that favor its chemical modification. This wet BC membrane proven suitable for $ NaIO_{4} $ oxidation. Time and temperature conditions were evaluated in the oxidation reaction, with oxidation BC (OxBC) performed at 1% (w/v) $ NaIO_{4} $ for 6 h at 55 °C under most advantageous conditions, as it provided 50% oxidation degree and preserved its morphological structure. BC and OxBC were characterized by X-ray diffraction, X-ray photoelectron spectroscopy, Scanning electron microscopy, mechanical test, and thermal analysis. The oxidation reaction decreased BC crystallinity, tensile strength, and thermal stability and compacted the cellulose layers. BC and OxBC showed non-cytotoxicity. Fourier transform infrared confirmed that OxBC can covalently immobilize papain and that after immobilization the enzyme showed a recovered enzymatic activity of 93.1%. In addition, the oxidized membrane presented greater amount of immobilized papain in its study than BC, proving to be a more efficient support for enzymatic immobilization. Graphic abstract Bacterial cellulose (dpeaa)DE-He213 K (dpeaa)DE-He213 CO (dpeaa)DE-He213 purification (dpeaa)DE-He213 NaIO (dpeaa)DE-He213 oxidation (dpeaa)DE-He213 Covalent immobilization (dpeaa)DE-He213 Enzyme (dpeaa)DE-He213 Wound dressing (dpeaa)DE-He213 Andrade, Fábia Karine verfasserin aut Vieira, Lídia de Araújo Pinto verfasserin aut Vieira, Rodrigo Silveira verfasserin aut Vaz, Juliana Miguel verfasserin aut Chevallier, Pascale verfasserin aut Mantovani, Diego verfasserin aut Borges, Maria de Fátima verfasserin aut Rosa, Morsyleide de Freitas verfasserin aut Enthalten in Cellulose Dordrecht [u.a.] : Springer Science + Business Media B.V, 1994 27(2020), 6 vom: 25. Jan., Seite 3055-3083 (DE-627)306353857 (DE-600)1496831-9 1572-882X nnns volume:27 year:2020 number:6 day:25 month:01 pages:3055-3083 https://dx.doi.org/10.1007/s10570-020-02966-5 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 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_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.63 ASE 35.77 ASE AR 27 2020 6 25 01 3055-3083 |
| spelling |
10.1007/s10570-020-02966-5 doi (DE-627)SPR039138615 (SPR)s10570-020-02966-5-e DE-627 ger DE-627 rakwb eng 540 ASE 35.63 bkl 35.77 bkl Vasconcelos, Niédja Fittipaldi verfasserin aut Oxidized bacterial cellulose membrane as support for enzyme immobilization: properties and morphological features 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Bacterial cellulose (BC) membrane can be architected to covalently immobilize biomolecules, generating materials with new functionality. The processes of purification (via alkaline treatment) and chemical modification (via $ NaIO_{4} $) to the wet BC membrane is the innovation of this work. This wet oxidized BC (OxBC) membrane could act as a support matrix for covalent immobilization of enzymes. BC produced over 5 days of static fermentation, followed by purification with $ K_{2} %$ CO_{3} $ (BC-5d-$ K_{2} %$ CO_{3} $) was selected for our study due to high porosity and surface area, which are properties that favor its chemical modification. This wet BC membrane proven suitable for $ NaIO_{4} $ oxidation. Time and temperature conditions were evaluated in the oxidation reaction, with oxidation BC (OxBC) performed at 1% (w/v) $ NaIO_{4} $ for 6 h at 55 °C under most advantageous conditions, as it provided 50% oxidation degree and preserved its morphological structure. BC and OxBC were characterized by X-ray diffraction, X-ray photoelectron spectroscopy, Scanning electron microscopy, mechanical test, and thermal analysis. The oxidation reaction decreased BC crystallinity, tensile strength, and thermal stability and compacted the cellulose layers. BC and OxBC showed non-cytotoxicity. Fourier transform infrared confirmed that OxBC can covalently immobilize papain and that after immobilization the enzyme showed a recovered enzymatic activity of 93.1%. In addition, the oxidized membrane presented greater amount of immobilized papain in its study than BC, proving to be a more efficient support for enzymatic immobilization. Graphic abstract Bacterial cellulose (dpeaa)DE-He213 K (dpeaa)DE-He213 CO (dpeaa)DE-He213 purification (dpeaa)DE-He213 NaIO (dpeaa)DE-He213 oxidation (dpeaa)DE-He213 Covalent immobilization (dpeaa)DE-He213 Enzyme (dpeaa)DE-He213 Wound dressing (dpeaa)DE-He213 Andrade, Fábia Karine verfasserin aut Vieira, Lídia de Araújo Pinto verfasserin aut Vieira, Rodrigo Silveira verfasserin aut Vaz, Juliana Miguel verfasserin aut Chevallier, Pascale verfasserin aut Mantovani, Diego verfasserin aut Borges, Maria de Fátima verfasserin aut Rosa, Morsyleide de Freitas verfasserin aut Enthalten in Cellulose Dordrecht [u.a.] : Springer Science + Business Media B.V, 1994 27(2020), 6 vom: 25. Jan., Seite 3055-3083 (DE-627)306353857 (DE-600)1496831-9 1572-882X nnns volume:27 year:2020 number:6 day:25 month:01 pages:3055-3083 https://dx.doi.org/10.1007/s10570-020-02966-5 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 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_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.63 ASE 35.77 ASE AR 27 2020 6 25 01 3055-3083 |
| allfields_unstemmed |
10.1007/s10570-020-02966-5 doi (DE-627)SPR039138615 (SPR)s10570-020-02966-5-e DE-627 ger DE-627 rakwb eng 540 ASE 35.63 bkl 35.77 bkl Vasconcelos, Niédja Fittipaldi verfasserin aut Oxidized bacterial cellulose membrane as support for enzyme immobilization: properties and morphological features 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Bacterial cellulose (BC) membrane can be architected to covalently immobilize biomolecules, generating materials with new functionality. The processes of purification (via alkaline treatment) and chemical modification (via $ NaIO_{4} $) to the wet BC membrane is the innovation of this work. This wet oxidized BC (OxBC) membrane could act as a support matrix for covalent immobilization of enzymes. BC produced over 5 days of static fermentation, followed by purification with $ K_{2} %$ CO_{3} $ (BC-5d-$ K_{2} %$ CO_{3} $) was selected for our study due to high porosity and surface area, which are properties that favor its chemical modification. This wet BC membrane proven suitable for $ NaIO_{4} $ oxidation. Time and temperature conditions were evaluated in the oxidation reaction, with oxidation BC (OxBC) performed at 1% (w/v) $ NaIO_{4} $ for 6 h at 55 °C under most advantageous conditions, as it provided 50% oxidation degree and preserved its morphological structure. BC and OxBC were characterized by X-ray diffraction, X-ray photoelectron spectroscopy, Scanning electron microscopy, mechanical test, and thermal analysis. The oxidation reaction decreased BC crystallinity, tensile strength, and thermal stability and compacted the cellulose layers. BC and OxBC showed non-cytotoxicity. Fourier transform infrared confirmed that OxBC can covalently immobilize papain and that after immobilization the enzyme showed a recovered enzymatic activity of 93.1%. In addition, the oxidized membrane presented greater amount of immobilized papain in its study than BC, proving to be a more efficient support for enzymatic immobilization. Graphic abstract Bacterial cellulose (dpeaa)DE-He213 K (dpeaa)DE-He213 CO (dpeaa)DE-He213 purification (dpeaa)DE-He213 NaIO (dpeaa)DE-He213 oxidation (dpeaa)DE-He213 Covalent immobilization (dpeaa)DE-He213 Enzyme (dpeaa)DE-He213 Wound dressing (dpeaa)DE-He213 Andrade, Fábia Karine verfasserin aut Vieira, Lídia de Araújo Pinto verfasserin aut Vieira, Rodrigo Silveira verfasserin aut Vaz, Juliana Miguel verfasserin aut Chevallier, Pascale verfasserin aut Mantovani, Diego verfasserin aut Borges, Maria de Fátima verfasserin aut Rosa, Morsyleide de Freitas verfasserin aut Enthalten in Cellulose Dordrecht [u.a.] : Springer Science + Business Media B.V, 1994 27(2020), 6 vom: 25. Jan., Seite 3055-3083 (DE-627)306353857 (DE-600)1496831-9 1572-882X nnns volume:27 year:2020 number:6 day:25 month:01 pages:3055-3083 https://dx.doi.org/10.1007/s10570-020-02966-5 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 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_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.63 ASE 35.77 ASE AR 27 2020 6 25 01 3055-3083 |
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10.1007/s10570-020-02966-5 doi (DE-627)SPR039138615 (SPR)s10570-020-02966-5-e DE-627 ger DE-627 rakwb eng 540 ASE 35.63 bkl 35.77 bkl Vasconcelos, Niédja Fittipaldi verfasserin aut Oxidized bacterial cellulose membrane as support for enzyme immobilization: properties and morphological features 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Bacterial cellulose (BC) membrane can be architected to covalently immobilize biomolecules, generating materials with new functionality. The processes of purification (via alkaline treatment) and chemical modification (via $ NaIO_{4} $) to the wet BC membrane is the innovation of this work. This wet oxidized BC (OxBC) membrane could act as a support matrix for covalent immobilization of enzymes. BC produced over 5 days of static fermentation, followed by purification with $ K_{2} %$ CO_{3} $ (BC-5d-$ K_{2} %$ CO_{3} $) was selected for our study due to high porosity and surface area, which are properties that favor its chemical modification. This wet BC membrane proven suitable for $ NaIO_{4} $ oxidation. Time and temperature conditions were evaluated in the oxidation reaction, with oxidation BC (OxBC) performed at 1% (w/v) $ NaIO_{4} $ for 6 h at 55 °C under most advantageous conditions, as it provided 50% oxidation degree and preserved its morphological structure. BC and OxBC were characterized by X-ray diffraction, X-ray photoelectron spectroscopy, Scanning electron microscopy, mechanical test, and thermal analysis. The oxidation reaction decreased BC crystallinity, tensile strength, and thermal stability and compacted the cellulose layers. BC and OxBC showed non-cytotoxicity. Fourier transform infrared confirmed that OxBC can covalently immobilize papain and that after immobilization the enzyme showed a recovered enzymatic activity of 93.1%. In addition, the oxidized membrane presented greater amount of immobilized papain in its study than BC, proving to be a more efficient support for enzymatic immobilization. Graphic abstract Bacterial cellulose (dpeaa)DE-He213 K (dpeaa)DE-He213 CO (dpeaa)DE-He213 purification (dpeaa)DE-He213 NaIO (dpeaa)DE-He213 oxidation (dpeaa)DE-He213 Covalent immobilization (dpeaa)DE-He213 Enzyme (dpeaa)DE-He213 Wound dressing (dpeaa)DE-He213 Andrade, Fábia Karine verfasserin aut Vieira, Lídia de Araújo Pinto verfasserin aut Vieira, Rodrigo Silveira verfasserin aut Vaz, Juliana Miguel verfasserin aut Chevallier, Pascale verfasserin aut Mantovani, Diego verfasserin aut Borges, Maria de Fátima verfasserin aut Rosa, Morsyleide de Freitas verfasserin aut Enthalten in Cellulose Dordrecht [u.a.] : Springer Science + Business Media B.V, 1994 27(2020), 6 vom: 25. Jan., Seite 3055-3083 (DE-627)306353857 (DE-600)1496831-9 1572-882X nnns volume:27 year:2020 number:6 day:25 month:01 pages:3055-3083 https://dx.doi.org/10.1007/s10570-020-02966-5 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 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_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.63 ASE 35.77 ASE AR 27 2020 6 25 01 3055-3083 |
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10.1007/s10570-020-02966-5 doi (DE-627)SPR039138615 (SPR)s10570-020-02966-5-e DE-627 ger DE-627 rakwb eng 540 ASE 35.63 bkl 35.77 bkl Vasconcelos, Niédja Fittipaldi verfasserin aut Oxidized bacterial cellulose membrane as support for enzyme immobilization: properties and morphological features 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Bacterial cellulose (BC) membrane can be architected to covalently immobilize biomolecules, generating materials with new functionality. The processes of purification (via alkaline treatment) and chemical modification (via $ NaIO_{4} $) to the wet BC membrane is the innovation of this work. This wet oxidized BC (OxBC) membrane could act as a support matrix for covalent immobilization of enzymes. BC produced over 5 days of static fermentation, followed by purification with $ K_{2} %$ CO_{3} $ (BC-5d-$ K_{2} %$ CO_{3} $) was selected for our study due to high porosity and surface area, which are properties that favor its chemical modification. This wet BC membrane proven suitable for $ NaIO_{4} $ oxidation. Time and temperature conditions were evaluated in the oxidation reaction, with oxidation BC (OxBC) performed at 1% (w/v) $ NaIO_{4} $ for 6 h at 55 °C under most advantageous conditions, as it provided 50% oxidation degree and preserved its morphological structure. BC and OxBC were characterized by X-ray diffraction, X-ray photoelectron spectroscopy, Scanning electron microscopy, mechanical test, and thermal analysis. The oxidation reaction decreased BC crystallinity, tensile strength, and thermal stability and compacted the cellulose layers. BC and OxBC showed non-cytotoxicity. Fourier transform infrared confirmed that OxBC can covalently immobilize papain and that after immobilization the enzyme showed a recovered enzymatic activity of 93.1%. In addition, the oxidized membrane presented greater amount of immobilized papain in its study than BC, proving to be a more efficient support for enzymatic immobilization. Graphic abstract Bacterial cellulose (dpeaa)DE-He213 K (dpeaa)DE-He213 CO (dpeaa)DE-He213 purification (dpeaa)DE-He213 NaIO (dpeaa)DE-He213 oxidation (dpeaa)DE-He213 Covalent immobilization (dpeaa)DE-He213 Enzyme (dpeaa)DE-He213 Wound dressing (dpeaa)DE-He213 Andrade, Fábia Karine verfasserin aut Vieira, Lídia de Araújo Pinto verfasserin aut Vieira, Rodrigo Silveira verfasserin aut Vaz, Juliana Miguel verfasserin aut Chevallier, Pascale verfasserin aut Mantovani, Diego verfasserin aut Borges, Maria de Fátima verfasserin aut Rosa, Morsyleide de Freitas verfasserin aut Enthalten in Cellulose Dordrecht [u.a.] : Springer Science + Business Media B.V, 1994 27(2020), 6 vom: 25. Jan., Seite 3055-3083 (DE-627)306353857 (DE-600)1496831-9 1572-882X nnns volume:27 year:2020 number:6 day:25 month:01 pages:3055-3083 https://dx.doi.org/10.1007/s10570-020-02966-5 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 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_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.63 ASE 35.77 ASE AR 27 2020 6 25 01 3055-3083 |
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English |
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Enthalten in Cellulose 27(2020), 6 vom: 25. Jan., Seite 3055-3083 volume:27 year:2020 number:6 day:25 month:01 pages:3055-3083 |
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Enthalten in Cellulose 27(2020), 6 vom: 25. Jan., Seite 3055-3083 volume:27 year:2020 number:6 day:25 month:01 pages:3055-3083 |
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Bacterial cellulose K CO purification NaIO oxidation Covalent immobilization Enzyme Wound dressing |
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Cellulose |
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Vasconcelos, Niédja Fittipaldi @@aut@@ Andrade, Fábia Karine @@aut@@ Vieira, Lídia de Araújo Pinto @@aut@@ Vieira, Rodrigo Silveira @@aut@@ Vaz, Juliana Miguel @@aut@@ Chevallier, Pascale @@aut@@ Mantovani, Diego @@aut@@ Borges, Maria de Fátima @@aut@@ Rosa, Morsyleide de Freitas @@aut@@ |
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2020-01-25T00:00:00Z |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">SPR039138615</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230519114624.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">201007s2020 xx |||||o 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1007/s10570-020-02966-5</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)SPR039138615</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(SPR)s10570-020-02966-5-e</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">540</subfield><subfield code="q">ASE</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">35.63</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">35.77</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Vasconcelos, Niédja Fittipaldi</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Oxidized bacterial cellulose membrane as support for enzyme immobilization: properties and morphological features</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2020</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract Bacterial cellulose (BC) membrane can be architected to covalently immobilize biomolecules, generating materials with new functionality. The processes of purification (via alkaline treatment) and chemical modification (via $ NaIO_{4} $) to the wet BC membrane is the innovation of this work. This wet oxidized BC (OxBC) membrane could act as a support matrix for covalent immobilization of enzymes. BC produced over 5 days of static fermentation, followed by purification with $ K_{2} %$ CO_{3} $ (BC-5d-$ K_{2} %$ CO_{3} $) was selected for our study due to high porosity and surface area, which are properties that favor its chemical modification. This wet BC membrane proven suitable for $ NaIO_{4} $ oxidation. Time and temperature conditions were evaluated in the oxidation reaction, with oxidation BC (OxBC) performed at 1% (w/v) $ NaIO_{4} $ for 6 h at 55 °C under most advantageous conditions, as it provided 50% oxidation degree and preserved its morphological structure. BC and OxBC were characterized by X-ray diffraction, X-ray photoelectron spectroscopy, Scanning electron microscopy, mechanical test, and thermal analysis. The oxidation reaction decreased BC crystallinity, tensile strength, and thermal stability and compacted the cellulose layers. BC and OxBC showed non-cytotoxicity. Fourier transform infrared confirmed that OxBC can covalently immobilize papain and that after immobilization the enzyme showed a recovered enzymatic activity of 93.1%. In addition, the oxidized membrane presented greater amount of immobilized papain in its study than BC, proving to be a more efficient support for enzymatic immobilization. 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|
| author |
Vasconcelos, Niédja Fittipaldi |
| spellingShingle |
Vasconcelos, Niédja Fittipaldi ddc 540 bkl 35.63 bkl 35.77 misc Bacterial cellulose misc K misc CO misc purification misc NaIO misc oxidation misc Covalent immobilization misc Enzyme misc Wound dressing Oxidized bacterial cellulose membrane as support for enzyme immobilization: properties and morphological features |
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Vasconcelos, Niédja Fittipaldi |
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540 - Chemistry & allied sciences |
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1572-882X |
| topic_title |
540 ASE 35.63 bkl 35.77 bkl Oxidized bacterial cellulose membrane as support for enzyme immobilization: properties and morphological features Bacterial cellulose (dpeaa)DE-He213 K (dpeaa)DE-He213 CO (dpeaa)DE-He213 purification (dpeaa)DE-He213 NaIO (dpeaa)DE-He213 oxidation (dpeaa)DE-He213 Covalent immobilization (dpeaa)DE-He213 Enzyme (dpeaa)DE-He213 Wound dressing (dpeaa)DE-He213 |
| topic |
ddc 540 bkl 35.63 bkl 35.77 misc Bacterial cellulose misc K misc CO misc purification misc NaIO misc oxidation misc Covalent immobilization misc Enzyme misc Wound dressing |
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ddc 540 bkl 35.63 bkl 35.77 misc Bacterial cellulose misc K misc CO misc purification misc NaIO misc oxidation misc Covalent immobilization misc Enzyme misc Wound dressing |
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ddc 540 bkl 35.63 bkl 35.77 misc Bacterial cellulose misc K misc CO misc purification misc NaIO misc oxidation misc Covalent immobilization misc Enzyme misc Wound dressing |
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Elektronische Aufsätze Aufsätze Elektronische Ressource |
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540 - Chemistry |
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Oxidized bacterial cellulose membrane as support for enzyme immobilization: properties and morphological features |
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Oxidized bacterial cellulose membrane as support for enzyme immobilization: properties and morphological features |
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Vasconcelos, Niédja Fittipaldi |
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Vasconcelos, Niédja Fittipaldi Andrade, Fábia Karine Vieira, Lídia de Araújo Pinto Vieira, Rodrigo Silveira Vaz, Juliana Miguel Chevallier, Pascale Mantovani, Diego Borges, Maria de Fátima Rosa, Morsyleide de Freitas |
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oxidized bacterial cellulose membrane as support for enzyme immobilization: properties and morphological features |
| title_auth |
Oxidized bacterial cellulose membrane as support for enzyme immobilization: properties and morphological features |
| abstract |
Abstract Bacterial cellulose (BC) membrane can be architected to covalently immobilize biomolecules, generating materials with new functionality. The processes of purification (via alkaline treatment) and chemical modification (via $ NaIO_{4} $) to the wet BC membrane is the innovation of this work. This wet oxidized BC (OxBC) membrane could act as a support matrix for covalent immobilization of enzymes. BC produced over 5 days of static fermentation, followed by purification with $ K_{2} %$ CO_{3} $ (BC-5d-$ K_{2} %$ CO_{3} $) was selected for our study due to high porosity and surface area, which are properties that favor its chemical modification. This wet BC membrane proven suitable for $ NaIO_{4} $ oxidation. Time and temperature conditions were evaluated in the oxidation reaction, with oxidation BC (OxBC) performed at 1% (w/v) $ NaIO_{4} $ for 6 h at 55 °C under most advantageous conditions, as it provided 50% oxidation degree and preserved its morphological structure. BC and OxBC were characterized by X-ray diffraction, X-ray photoelectron spectroscopy, Scanning electron microscopy, mechanical test, and thermal analysis. The oxidation reaction decreased BC crystallinity, tensile strength, and thermal stability and compacted the cellulose layers. BC and OxBC showed non-cytotoxicity. Fourier transform infrared confirmed that OxBC can covalently immobilize papain and that after immobilization the enzyme showed a recovered enzymatic activity of 93.1%. In addition, the oxidized membrane presented greater amount of immobilized papain in its study than BC, proving to be a more efficient support for enzymatic immobilization. Graphic abstract |
| abstractGer |
Abstract Bacterial cellulose (BC) membrane can be architected to covalently immobilize biomolecules, generating materials with new functionality. The processes of purification (via alkaline treatment) and chemical modification (via $ NaIO_{4} $) to the wet BC membrane is the innovation of this work. This wet oxidized BC (OxBC) membrane could act as a support matrix for covalent immobilization of enzymes. BC produced over 5 days of static fermentation, followed by purification with $ K_{2} %$ CO_{3} $ (BC-5d-$ K_{2} %$ CO_{3} $) was selected for our study due to high porosity and surface area, which are properties that favor its chemical modification. This wet BC membrane proven suitable for $ NaIO_{4} $ oxidation. Time and temperature conditions were evaluated in the oxidation reaction, with oxidation BC (OxBC) performed at 1% (w/v) $ NaIO_{4} $ for 6 h at 55 °C under most advantageous conditions, as it provided 50% oxidation degree and preserved its morphological structure. BC and OxBC were characterized by X-ray diffraction, X-ray photoelectron spectroscopy, Scanning electron microscopy, mechanical test, and thermal analysis. The oxidation reaction decreased BC crystallinity, tensile strength, and thermal stability and compacted the cellulose layers. BC and OxBC showed non-cytotoxicity. Fourier transform infrared confirmed that OxBC can covalently immobilize papain and that after immobilization the enzyme showed a recovered enzymatic activity of 93.1%. In addition, the oxidized membrane presented greater amount of immobilized papain in its study than BC, proving to be a more efficient support for enzymatic immobilization. Graphic abstract |
| abstract_unstemmed |
Abstract Bacterial cellulose (BC) membrane can be architected to covalently immobilize biomolecules, generating materials with new functionality. The processes of purification (via alkaline treatment) and chemical modification (via $ NaIO_{4} $) to the wet BC membrane is the innovation of this work. This wet oxidized BC (OxBC) membrane could act as a support matrix for covalent immobilization of enzymes. BC produced over 5 days of static fermentation, followed by purification with $ K_{2} %$ CO_{3} $ (BC-5d-$ K_{2} %$ CO_{3} $) was selected for our study due to high porosity and surface area, which are properties that favor its chemical modification. This wet BC membrane proven suitable for $ NaIO_{4} $ oxidation. Time and temperature conditions were evaluated in the oxidation reaction, with oxidation BC (OxBC) performed at 1% (w/v) $ NaIO_{4} $ for 6 h at 55 °C under most advantageous conditions, as it provided 50% oxidation degree and preserved its morphological structure. BC and OxBC were characterized by X-ray diffraction, X-ray photoelectron spectroscopy, Scanning electron microscopy, mechanical test, and thermal analysis. The oxidation reaction decreased BC crystallinity, tensile strength, and thermal stability and compacted the cellulose layers. BC and OxBC showed non-cytotoxicity. Fourier transform infrared confirmed that OxBC can covalently immobilize papain and that after immobilization the enzyme showed a recovered enzymatic activity of 93.1%. In addition, the oxidized membrane presented greater amount of immobilized papain in its study than BC, proving to be a more efficient support for enzymatic immobilization. Graphic abstract |
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Oxidized bacterial cellulose membrane as support for enzyme immobilization: properties and morphological features |
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Andrade, Fábia Karine Vieira, Lídia de Araújo Pinto Vieira, Rodrigo Silveira Vaz, Juliana Miguel Chevallier, Pascale Mantovani, Diego Borges, Maria de Fátima Rosa, Morsyleide de Freitas |
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Andrade, Fábia Karine Vieira, Lídia de Araújo Pinto Vieira, Rodrigo Silveira Vaz, Juliana Miguel Chevallier, Pascale Mantovani, Diego Borges, Maria de Fátima Rosa, Morsyleide de Freitas |
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| score |
7.4008837 |