Abstract
Fourier Transform Infrared (FTIR) Analysis was used to characterize secondary structure of gelatins extracted from shaari skin and compared with bovine and porcine gelatin obtained from commercial source. The concentration and temperature of extracted solutions were varied from 0.01 to 1.0 N and 4 to 80°C, respectively. The intensity ratio of amide III and I as a measure of denaturation process showed that all samples had almost the same protein structure at 0.1 and 1.0 N concentration for all extraction temperatures. At low acid concentration (0.01 N) and low temperature (4°C) significant amount of triple helix remained intact (i.e. less denaturation). As the temperature increased from 20°C, the random coil structure increased as the protein became denatured and protein losses its triple structure. The cluster analysis showed that secondary structure of gelatin extracted using mild treatment (concentration: 0.01 N and temperature: 4°C) behaved completely different from other extracted gelatin.
| Original language | English |
|---|---|
| Pages (from-to) | 1167-1173 |
| Number of pages | 7 |
| Journal | International Food Research Journal |
| Volume | 19 |
| Issue number | 3 |
| Publication status | Published - 2012 |
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Keywords
- Fish skin
- Fourier transform analysis (FTIR)
- Gelatin
- glass transition
- State diagram
ASJC Scopus subject areas
- Food Science
Cite this
Fourier transform infrared (FTIR) spectroscopic study of extracted gelatin from shaari (Lithrinus microdon) skin : Effects of extraction conditions. / Al-Saidi, G. S.; Al-Alawi, A.; Rahman, M. S.; Guizani, N.
In: International Food Research Journal, Vol. 19, No. 3, 2012, p. 1167-1173.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Fourier transform infrared (FTIR) spectroscopic study of extracted gelatin from shaari (Lithrinus microdon) skin
T2 - Effects of extraction conditions
AU - Al-Saidi, G. S.
AU - Al-Alawi, A.
AU - Rahman, M. S.
AU - Guizani, N.
PY - 2012
Y1 - 2012
N2 - Fourier Transform Infrared (FTIR) Analysis was used to characterize secondary structure of gelatins extracted from shaari skin and compared with bovine and porcine gelatin obtained from commercial source. The concentration and temperature of extracted solutions were varied from 0.01 to 1.0 N and 4 to 80°C, respectively. The intensity ratio of amide III and I as a measure of denaturation process showed that all samples had almost the same protein structure at 0.1 and 1.0 N concentration for all extraction temperatures. At low acid concentration (0.01 N) and low temperature (4°C) significant amount of triple helix remained intact (i.e. less denaturation). As the temperature increased from 20°C, the random coil structure increased as the protein became denatured and protein losses its triple structure. The cluster analysis showed that secondary structure of gelatin extracted using mild treatment (concentration: 0.01 N and temperature: 4°C) behaved completely different from other extracted gelatin.
AB - Fourier Transform Infrared (FTIR) Analysis was used to characterize secondary structure of gelatins extracted from shaari skin and compared with bovine and porcine gelatin obtained from commercial source. The concentration and temperature of extracted solutions were varied from 0.01 to 1.0 N and 4 to 80°C, respectively. The intensity ratio of amide III and I as a measure of denaturation process showed that all samples had almost the same protein structure at 0.1 and 1.0 N concentration for all extraction temperatures. At low acid concentration (0.01 N) and low temperature (4°C) significant amount of triple helix remained intact (i.e. less denaturation). As the temperature increased from 20°C, the random coil structure increased as the protein became denatured and protein losses its triple structure. The cluster analysis showed that secondary structure of gelatin extracted using mild treatment (concentration: 0.01 N and temperature: 4°C) behaved completely different from other extracted gelatin.
KW - Fish skin
KW - Fourier transform analysis (FTIR)
KW - Gelatin
KW - glass transition
KW - State diagram
UR - http://www.scopus.com/inward/record.url?scp=84864822314&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84864822314&partnerID=8YFLogxK
M3 - Article
AN - SCOPUS:84864822314
VL - 19
SP - 1167
EP - 1173
JO - International Food Research Journal
JF - International Food Research Journal
SN - 1985-4668
IS - 3
ER -