Fourier transform infrared (FTIR) spectroscopic study of extracted gelatin from shaari (Lithrinus microdon) skin

Effects of extraction conditions

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43 Citations (Scopus)

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 languageEnglish
Pages (from-to)1167-1173
Number of pages7
JournalInternational Food Research Journal
Volume19
Issue number3
Publication statusPublished - 2012

Fingerprint

Microdon
Fourier Analysis
Gelatin
gelatin
skin (animal)
Skin
Temperature
temperature
denaturation
Proteins
Process Assessment (Health Care)
protein depletion
protein structure
amides
Amides
Cluster Analysis
cluster analysis
Swine
swine
Acids

Keywords

  • Fish skin
  • Fourier transform analysis (FTIR)
  • Gelatin
  • glass transition
  • State diagram

ASJC Scopus subject areas

  • Food Science

Cite this

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title = "Fourier transform infrared (FTIR) spectroscopic study of extracted gelatin from shaari (Lithrinus microdon) skin: Effects of extraction conditions",
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.",
keywords = "Fish skin, Fourier transform analysis (FTIR), Gelatin, glass transition, State diagram",
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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.

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KW - State diagram

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