Influence of organic solvents on the structural and thermal characteristics of silk protein from the web of Orthaga exvinacea Hampson (Lepidoptera: Pyralidae)
Abstract The silk protein from the web of Orthaga exvinacea was isolated, purified, and casted into films. This film was treated separately with methanol, acetone, ethyl acetate, and isopropyl alcohol in 50 % concentration for about 30 min. The treated films were thus dried in a desiccator and subje...
Ausführliche Beschreibung
Autor*in: |
Narayanan, Sajitha [verfasserIn] Gokuldas, Mankadath [verfasserIn] |
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Format: |
E-Artikel |
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Sprache: |
Englisch |
Erschienen: |
2016 |
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Schlagwörter: |
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Übergeordnetes Werk: |
Enthalten in: Journal of chemical biology - Berlin : Springer, 2008, 9(2016), 4 vom: 22. Aug., Seite 121-125 |
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Übergeordnetes Werk: |
volume:9 ; year:2016 ; number:4 ; day:22 ; month:08 ; pages:121-125 |
Links: |
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DOI / URN: |
10.1007/s12154-016-0158-4 |
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Katalog-ID: |
SPR02451666X |
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520 | |a Abstract The silk protein from the web of Orthaga exvinacea was isolated, purified, and casted into films. This film was treated separately with methanol, acetone, ethyl acetate, and isopropyl alcohol in 50 % concentration for about 30 min. The treated films were thus dried in a desiccator and subjected to FTIR and TG-DTA analysis. The structural studies revealed that the organic solvents induce conformatory changes in the protein film, especially the most sensitive amide I (1650 $ cm^{−1} $) band. This band had shifted to lower wavenumber (1633–1636 $ cm^{−1} $). Furthermore, the conformatory characteristics associated with amide I band also changed from random coil to β-sheet. Generally, β-sheet contributes strength to the protein film. Among the treated films, film treated with acetone showed much thermal stability. Moreover, the film treated with methanol had shown two different temperatures of maximum degradation. It is concluded that in addition to β-sheet content, various other factors such as various processing conditions and structural organization of protein may influence the stability of the films. | ||
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10.1007/s12154-016-0158-4 doi (DE-627)SPR02451666X (SPR)s12154-016-0158-4-e DE-627 ger DE-627 rakwb eng 540 ASE Narayanan, Sajitha verfasserin aut Influence of organic solvents on the structural and thermal characteristics of silk protein from the web of Orthaga exvinacea Hampson (Lepidoptera: Pyralidae) 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract The silk protein from the web of Orthaga exvinacea was isolated, purified, and casted into films. This film was treated separately with methanol, acetone, ethyl acetate, and isopropyl alcohol in 50 % concentration for about 30 min. The treated films were thus dried in a desiccator and subjected to FTIR and TG-DTA analysis. The structural studies revealed that the organic solvents induce conformatory changes in the protein film, especially the most sensitive amide I (1650 $ cm^{−1} $) band. This band had shifted to lower wavenumber (1633–1636 $ cm^{−1} $). Furthermore, the conformatory characteristics associated with amide I band also changed from random coil to β-sheet. Generally, β-sheet contributes strength to the protein film. Among the treated films, film treated with acetone showed much thermal stability. Moreover, the film treated with methanol had shown two different temperatures of maximum degradation. It is concluded that in addition to β-sheet content, various other factors such as various processing conditions and structural organization of protein may influence the stability of the films. FTIR (dpeaa)DE-He213 Silk protein (dpeaa)DE-He213 TG-DTA (dpeaa)DE-He213 Silk film (dpeaa)DE-He213 Silken web (dpeaa)DE-He213 Gokuldas, Mankadath verfasserin aut Enthalten in Journal of chemical biology Berlin : Springer, 2008 9(2016), 4 vom: 22. Aug., Seite 121-125 (DE-627)570503191 (DE-600)2432741-4 1864-6166 nnns volume:9 year:2016 number:4 day:22 month:08 pages:121-125 https://dx.doi.org/10.1007/s12154-016-0158-4 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 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_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 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_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 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_4012 GBV_ILN_4035 GBV_ILN_4037 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 9 2016 4 22 08 121-125 |
spelling |
10.1007/s12154-016-0158-4 doi (DE-627)SPR02451666X (SPR)s12154-016-0158-4-e DE-627 ger DE-627 rakwb eng 540 ASE Narayanan, Sajitha verfasserin aut Influence of organic solvents on the structural and thermal characteristics of silk protein from the web of Orthaga exvinacea Hampson (Lepidoptera: Pyralidae) 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract The silk protein from the web of Orthaga exvinacea was isolated, purified, and casted into films. This film was treated separately with methanol, acetone, ethyl acetate, and isopropyl alcohol in 50 % concentration for about 30 min. The treated films were thus dried in a desiccator and subjected to FTIR and TG-DTA analysis. The structural studies revealed that the organic solvents induce conformatory changes in the protein film, especially the most sensitive amide I (1650 $ cm^{−1} $) band. This band had shifted to lower wavenumber (1633–1636 $ cm^{−1} $). Furthermore, the conformatory characteristics associated with amide I band also changed from random coil to β-sheet. Generally, β-sheet contributes strength to the protein film. Among the treated films, film treated with acetone showed much thermal stability. Moreover, the film treated with methanol had shown two different temperatures of maximum degradation. It is concluded that in addition to β-sheet content, various other factors such as various processing conditions and structural organization of protein may influence the stability of the films. FTIR (dpeaa)DE-He213 Silk protein (dpeaa)DE-He213 TG-DTA (dpeaa)DE-He213 Silk film (dpeaa)DE-He213 Silken web (dpeaa)DE-He213 Gokuldas, Mankadath verfasserin aut Enthalten in Journal of chemical biology Berlin : Springer, 2008 9(2016), 4 vom: 22. Aug., Seite 121-125 (DE-627)570503191 (DE-600)2432741-4 1864-6166 nnns volume:9 year:2016 number:4 day:22 month:08 pages:121-125 https://dx.doi.org/10.1007/s12154-016-0158-4 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 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_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 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_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 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_4012 GBV_ILN_4035 GBV_ILN_4037 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 9 2016 4 22 08 121-125 |
allfields_unstemmed |
10.1007/s12154-016-0158-4 doi (DE-627)SPR02451666X (SPR)s12154-016-0158-4-e DE-627 ger DE-627 rakwb eng 540 ASE Narayanan, Sajitha verfasserin aut Influence of organic solvents on the structural and thermal characteristics of silk protein from the web of Orthaga exvinacea Hampson (Lepidoptera: Pyralidae) 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract The silk protein from the web of Orthaga exvinacea was isolated, purified, and casted into films. This film was treated separately with methanol, acetone, ethyl acetate, and isopropyl alcohol in 50 % concentration for about 30 min. The treated films were thus dried in a desiccator and subjected to FTIR and TG-DTA analysis. The structural studies revealed that the organic solvents induce conformatory changes in the protein film, especially the most sensitive amide I (1650 $ cm^{−1} $) band. This band had shifted to lower wavenumber (1633–1636 $ cm^{−1} $). Furthermore, the conformatory characteristics associated with amide I band also changed from random coil to β-sheet. Generally, β-sheet contributes strength to the protein film. Among the treated films, film treated with acetone showed much thermal stability. Moreover, the film treated with methanol had shown two different temperatures of maximum degradation. It is concluded that in addition to β-sheet content, various other factors such as various processing conditions and structural organization of protein may influence the stability of the films. FTIR (dpeaa)DE-He213 Silk protein (dpeaa)DE-He213 TG-DTA (dpeaa)DE-He213 Silk film (dpeaa)DE-He213 Silken web (dpeaa)DE-He213 Gokuldas, Mankadath verfasserin aut Enthalten in Journal of chemical biology Berlin : Springer, 2008 9(2016), 4 vom: 22. Aug., Seite 121-125 (DE-627)570503191 (DE-600)2432741-4 1864-6166 nnns volume:9 year:2016 number:4 day:22 month:08 pages:121-125 https://dx.doi.org/10.1007/s12154-016-0158-4 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 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_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 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_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 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_4012 GBV_ILN_4035 GBV_ILN_4037 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 9 2016 4 22 08 121-125 |
allfieldsGer |
10.1007/s12154-016-0158-4 doi (DE-627)SPR02451666X (SPR)s12154-016-0158-4-e DE-627 ger DE-627 rakwb eng 540 ASE Narayanan, Sajitha verfasserin aut Influence of organic solvents on the structural and thermal characteristics of silk protein from the web of Orthaga exvinacea Hampson (Lepidoptera: Pyralidae) 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract The silk protein from the web of Orthaga exvinacea was isolated, purified, and casted into films. This film was treated separately with methanol, acetone, ethyl acetate, and isopropyl alcohol in 50 % concentration for about 30 min. The treated films were thus dried in a desiccator and subjected to FTIR and TG-DTA analysis. The structural studies revealed that the organic solvents induce conformatory changes in the protein film, especially the most sensitive amide I (1650 $ cm^{−1} $) band. This band had shifted to lower wavenumber (1633–1636 $ cm^{−1} $). Furthermore, the conformatory characteristics associated with amide I band also changed from random coil to β-sheet. Generally, β-sheet contributes strength to the protein film. Among the treated films, film treated with acetone showed much thermal stability. Moreover, the film treated with methanol had shown two different temperatures of maximum degradation. It is concluded that in addition to β-sheet content, various other factors such as various processing conditions and structural organization of protein may influence the stability of the films. FTIR (dpeaa)DE-He213 Silk protein (dpeaa)DE-He213 TG-DTA (dpeaa)DE-He213 Silk film (dpeaa)DE-He213 Silken web (dpeaa)DE-He213 Gokuldas, Mankadath verfasserin aut Enthalten in Journal of chemical biology Berlin : Springer, 2008 9(2016), 4 vom: 22. Aug., Seite 121-125 (DE-627)570503191 (DE-600)2432741-4 1864-6166 nnns volume:9 year:2016 number:4 day:22 month:08 pages:121-125 https://dx.doi.org/10.1007/s12154-016-0158-4 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 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_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 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_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 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_4012 GBV_ILN_4035 GBV_ILN_4037 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 9 2016 4 22 08 121-125 |
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10.1007/s12154-016-0158-4 doi (DE-627)SPR02451666X (SPR)s12154-016-0158-4-e DE-627 ger DE-627 rakwb eng 540 ASE Narayanan, Sajitha verfasserin aut Influence of organic solvents on the structural and thermal characteristics of silk protein from the web of Orthaga exvinacea Hampson (Lepidoptera: Pyralidae) 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract The silk protein from the web of Orthaga exvinacea was isolated, purified, and casted into films. This film was treated separately with methanol, acetone, ethyl acetate, and isopropyl alcohol in 50 % concentration for about 30 min. The treated films were thus dried in a desiccator and subjected to FTIR and TG-DTA analysis. The structural studies revealed that the organic solvents induce conformatory changes in the protein film, especially the most sensitive amide I (1650 $ cm^{−1} $) band. This band had shifted to lower wavenumber (1633–1636 $ cm^{−1} $). Furthermore, the conformatory characteristics associated with amide I band also changed from random coil to β-sheet. Generally, β-sheet contributes strength to the protein film. Among the treated films, film treated with acetone showed much thermal stability. Moreover, the film treated with methanol had shown two different temperatures of maximum degradation. It is concluded that in addition to β-sheet content, various other factors such as various processing conditions and structural organization of protein may influence the stability of the films. FTIR (dpeaa)DE-He213 Silk protein (dpeaa)DE-He213 TG-DTA (dpeaa)DE-He213 Silk film (dpeaa)DE-He213 Silken web (dpeaa)DE-He213 Gokuldas, Mankadath verfasserin aut Enthalten in Journal of chemical biology Berlin : Springer, 2008 9(2016), 4 vom: 22. Aug., Seite 121-125 (DE-627)570503191 (DE-600)2432741-4 1864-6166 nnns volume:9 year:2016 number:4 day:22 month:08 pages:121-125 https://dx.doi.org/10.1007/s12154-016-0158-4 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 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_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 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_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 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_4012 GBV_ILN_4035 GBV_ILN_4037 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 9 2016 4 22 08 121-125 |
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Enthalten in Journal of chemical biology 9(2016), 4 vom: 22. Aug., Seite 121-125 volume:9 year:2016 number:4 day:22 month:08 pages:121-125 |
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Enthalten in Journal of chemical biology 9(2016), 4 vom: 22. Aug., Seite 121-125 volume:9 year:2016 number:4 day:22 month:08 pages:121-125 |
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Journal of chemical biology |
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Narayanan, Sajitha @@aut@@ Gokuldas, Mankadath @@aut@@ |
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2016-08-22T00:00:00Z |
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Narayanan, Sajitha ddc 540 misc FTIR misc Silk protein misc TG-DTA misc Silk film misc Silken web Influence of organic solvents on the structural and thermal characteristics of silk protein from the web of Orthaga exvinacea Hampson (Lepidoptera: Pyralidae) |
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540 ASE Influence of organic solvents on the structural and thermal characteristics of silk protein from the web of Orthaga exvinacea Hampson (Lepidoptera: Pyralidae) FTIR (dpeaa)DE-He213 Silk protein (dpeaa)DE-He213 TG-DTA (dpeaa)DE-He213 Silk film (dpeaa)DE-He213 Silken web (dpeaa)DE-He213 |
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Influence of organic solvents on the structural and thermal characteristics of silk protein from the web of Orthaga exvinacea Hampson (Lepidoptera: Pyralidae) |
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Influence of organic solvents on the structural and thermal characteristics of silk protein from the web of Orthaga exvinacea Hampson (Lepidoptera: Pyralidae) |
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influence of organic solvents on the structural and thermal characteristics of silk protein from the web of orthaga exvinacea hampson (lepidoptera: pyralidae) |
title_auth |
Influence of organic solvents on the structural and thermal characteristics of silk protein from the web of Orthaga exvinacea Hampson (Lepidoptera: Pyralidae) |
abstract |
Abstract The silk protein from the web of Orthaga exvinacea was isolated, purified, and casted into films. This film was treated separately with methanol, acetone, ethyl acetate, and isopropyl alcohol in 50 % concentration for about 30 min. The treated films were thus dried in a desiccator and subjected to FTIR and TG-DTA analysis. The structural studies revealed that the organic solvents induce conformatory changes in the protein film, especially the most sensitive amide I (1650 $ cm^{−1} $) band. This band had shifted to lower wavenumber (1633–1636 $ cm^{−1} $). Furthermore, the conformatory characteristics associated with amide I band also changed from random coil to β-sheet. Generally, β-sheet contributes strength to the protein film. Among the treated films, film treated with acetone showed much thermal stability. Moreover, the film treated with methanol had shown two different temperatures of maximum degradation. It is concluded that in addition to β-sheet content, various other factors such as various processing conditions and structural organization of protein may influence the stability of the films. |
abstractGer |
Abstract The silk protein from the web of Orthaga exvinacea was isolated, purified, and casted into films. This film was treated separately with methanol, acetone, ethyl acetate, and isopropyl alcohol in 50 % concentration for about 30 min. The treated films were thus dried in a desiccator and subjected to FTIR and TG-DTA analysis. The structural studies revealed that the organic solvents induce conformatory changes in the protein film, especially the most sensitive amide I (1650 $ cm^{−1} $) band. This band had shifted to lower wavenumber (1633–1636 $ cm^{−1} $). Furthermore, the conformatory characteristics associated with amide I band also changed from random coil to β-sheet. Generally, β-sheet contributes strength to the protein film. Among the treated films, film treated with acetone showed much thermal stability. Moreover, the film treated with methanol had shown two different temperatures of maximum degradation. It is concluded that in addition to β-sheet content, various other factors such as various processing conditions and structural organization of protein may influence the stability of the films. |
abstract_unstemmed |
Abstract The silk protein from the web of Orthaga exvinacea was isolated, purified, and casted into films. This film was treated separately with methanol, acetone, ethyl acetate, and isopropyl alcohol in 50 % concentration for about 30 min. The treated films were thus dried in a desiccator and subjected to FTIR and TG-DTA analysis. The structural studies revealed that the organic solvents induce conformatory changes in the protein film, especially the most sensitive amide I (1650 $ cm^{−1} $) band. This band had shifted to lower wavenumber (1633–1636 $ cm^{−1} $). Furthermore, the conformatory characteristics associated with amide I band also changed from random coil to β-sheet. Generally, β-sheet contributes strength to the protein film. Among the treated films, film treated with acetone showed much thermal stability. Moreover, the film treated with methanol had shown two different temperatures of maximum degradation. It is concluded that in addition to β-sheet content, various other factors such as various processing conditions and structural organization of protein may influence the stability of the films. |
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Influence of organic solvents on the structural and thermal characteristics of silk protein from the web of Orthaga exvinacea Hampson (Lepidoptera: Pyralidae) |
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