Isolation and characterization of collagen from chicken feet

Collagen was isolated from chicken feet by using papain and pepsin enzymes in acetic acid solution at 4°C for 24h with a yield of 18.16% and 22.94% by dry weight, respectively. Chemical composition and characteristics of chicken feet collagen such as amino acid composition, SDS-PAGE patterns, FTIR s...

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Main Authors: Hashim, Puziah, Mohd Sofberi, Mohammad Ridzwan, Bakar, Jamilah
Format: Conference or Workshop Item
Language:English
Published: 2014
Online Access:http://psasir.upm.edu.my/id/eprint/31374/1/ID%2031374.pdf
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author Hashim, Puziah
Mohd Sofberi, Mohammad Ridzwan
Bakar, Jamilah
author_facet Hashim, Puziah
Mohd Sofberi, Mohammad Ridzwan
Bakar, Jamilah
author_sort Hashim, Puziah
collection UPM
description Collagen was isolated from chicken feet by using papain and pepsin enzymes in acetic acid solution at 4°C for 24h with a yield of 18.16% and 22.94% by dry weight, respectively. Chemical composition and characteristics of chicken feet collagen such as amino acid composition, SDS-PAGE patterns, FTIR spectra and thermal properties were evaluated. The chicken feet collagen is rich in the amino acids glycine, glutamic acid, proline and hydroxyproline. Electrophoresis pattern demonstrated two distinct α-chains (α1 and α2) and β chain, indicating that type I collagen is a major component of chicken feet collagen. The thermal stability of collagen isolated by papain and pepsin revealed stable denaturation temperatures of 48.40 and 53.35°C, respectively. The FTIR spectra of both collagens were similar with amide regions in A, B, I, II and III. The study demonstrated that chicken feet collagen using papain isolation method is possible as commercial alternative ingredient.
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spelling upm.eprints-313742018-05-15T01:05:38Z http://psasir.upm.edu.my/id/eprint/31374/ Isolation and characterization of collagen from chicken feet Hashim, Puziah Mohd Sofberi, Mohammad Ridzwan Bakar, Jamilah Collagen was isolated from chicken feet by using papain and pepsin enzymes in acetic acid solution at 4°C for 24h with a yield of 18.16% and 22.94% by dry weight, respectively. Chemical composition and characteristics of chicken feet collagen such as amino acid composition, SDS-PAGE patterns, FTIR spectra and thermal properties were evaluated. The chicken feet collagen is rich in the amino acids glycine, glutamic acid, proline and hydroxyproline. Electrophoresis pattern demonstrated two distinct α-chains (α1 and α2) and β chain, indicating that type I collagen is a major component of chicken feet collagen. The thermal stability of collagen isolated by papain and pepsin revealed stable denaturation temperatures of 48.40 and 53.35°C, respectively. The FTIR spectra of both collagens were similar with amide regions in A, B, I, II and III. The study demonstrated that chicken feet collagen using papain isolation method is possible as commercial alternative ingredient. 2014 Conference or Workshop Item PeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/31374/1/ID%2031374.pdf Hashim, Puziah and Mohd Sofberi, Mohammad Ridzwan and Bakar, Jamilah (2014) Isolation and characterization of collagen from chicken feet. In: ICBAE 2014 : International Conference on Biosystems and Agricultural Engineering, 27-28 Mar. 2014, Madrid, Spain. .
spellingShingle Hashim, Puziah
Mohd Sofberi, Mohammad Ridzwan
Bakar, Jamilah
Isolation and characterization of collagen from chicken feet
title Isolation and characterization of collagen from chicken feet
title_full Isolation and characterization of collagen from chicken feet
title_fullStr Isolation and characterization of collagen from chicken feet
title_full_unstemmed Isolation and characterization of collagen from chicken feet
title_short Isolation and characterization of collagen from chicken feet
title_sort isolation and characterization of collagen from chicken feet
url http://psasir.upm.edu.my/id/eprint/31374/1/ID%2031374.pdf
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