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

Gespeichert in:

Autor*in:	Narayanan, Sajitha [verfasserIn] Gokuldas, Mankadath [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2016

Schlagwörter:	FTIR Silk protein TG-DTA Silk film Silken web

Übergeordnetes Werk:	Enthalten in: Journal of chemical biology - Berlin : Springer, 2008, 9(2016), 4 vom: 22. Aug., Seite 121-125
Übergeordnetes Werk:	volume:9 ; year:2016 ; number:4 ; day:22 ; month:08 ; pages:121-125

Links:	Volltext

DOI / URN:	10.1007/s12154-016-0158-4

Katalog-ID:	SPR02451666X

Internformat


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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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912			\|a GBV_ILN_60
912			\|a GBV_ILN_62
912			\|a GBV_ILN_63
912			\|a GBV_ILN_65
912			\|a GBV_ILN_69
912			\|a GBV_ILN_70
912			\|a GBV_ILN_73
912			\|a GBV_ILN_95
912			\|a GBV_ILN_105
912			\|a GBV_ILN_110
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912			\|a GBV_ILN_285
912			\|a GBV_ILN_293
912			\|a GBV_ILN_602
912			\|a GBV_ILN_702
912			\|a GBV_ILN_2001
912			\|a GBV_ILN_2003
912			\|a GBV_ILN_2005
912			\|a GBV_ILN_2006
912			\|a GBV_ILN_2007
912			\|a GBV_ILN_2009
912			\|a GBV_ILN_2010
912			\|a GBV_ILN_2011
912			\|a GBV_ILN_2014
912			\|a GBV_ILN_2015
912			\|a GBV_ILN_2020
912			\|a GBV_ILN_2021
912			\|a GBV_ILN_2025
912			\|a GBV_ILN_2026
912			\|a GBV_ILN_2031
912			\|a GBV_ILN_2034
912			\|a GBV_ILN_2037
912			\|a GBV_ILN_2038
912			\|a GBV_ILN_2039
912			\|a GBV_ILN_2044
912			\|a GBV_ILN_2055
912			\|a GBV_ILN_2057
912			\|a GBV_ILN_2059
912			\|a GBV_ILN_2064
912			\|a GBV_ILN_2065
912			\|a GBV_ILN_2068
912			\|a GBV_ILN_2070
912			\|a GBV_ILN_2086
912			\|a GBV_ILN_2106
912			\|a GBV_ILN_2108
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912			\|a GBV_ILN_2129
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912			\|a GBV_ILN_2144
912			\|a GBV_ILN_2147
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912			\|a GBV_ILN_2152
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912			\|a GBV_ILN_4249
912			\|a GBV_ILN_4251
912			\|a GBV_ILN_4305
912			\|a GBV_ILN_4306
912			\|a GBV_ILN_4307
912			\|a GBV_ILN_4313
912			\|a GBV_ILN_4322
912			\|a GBV_ILN_4323
912			\|a GBV_ILN_4324
912			\|a GBV_ILN_4325
912			\|a GBV_ILN_4338
912			\|a GBV_ILN_4367
912			\|a GBV_ILN_4700
951			\|a AR
952			\|d 9 \|j 2016 \|e 4 \|b 22 \|c 08 \|h 121-125

Indexfelder

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hierarchy_sort_str	2016
publishDate	2016
allfields	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
allfieldsSound	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
language	English
source	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
sourceStr	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
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	FTIR Silk protein TG-DTA Silk film Silken web
dewey-raw	540
isfreeaccess_bool	false
container_title	Journal of chemical biology
authorswithroles_txt_mv	Narayanan, Sajitha @@aut@@ Gokuldas, Mankadath @@aut@@
publishDateDaySort_date	2016-08-22T00:00:00Z
hierarchy_top_id	570503191
dewey-sort	3540
id	SPR02451666X
language_de	englisch
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author	Narayanan, Sajitha
spellingShingle	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)
authorStr	Narayanan, Sajitha
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topic_title	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
topic	ddc 540 misc FTIR misc Silk protein misc TG-DTA misc Silk film misc Silken web
topic_unstemmed	ddc 540 misc FTIR misc Silk protein misc TG-DTA misc Silk film misc Silken web
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title	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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title_full	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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author_browse	Narayanan, Sajitha Gokuldas, Mankadath
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title_sort	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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title_short	Influence of organic solvents on the structural and thermal characteristics of silk protein from the web of Orthaga exvinacea Hampson (Lepidoptera: Pyralidae)
url	https://dx.doi.org/10.1007/s12154-016-0158-4
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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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