In vitro pepsin digestibility and amino acid composition in soluble and residual fractions of hydrolyzed chicken feathers
Beta-keratin in poultry feathers is a structural protein that is resistant to degradation due to disulfide and hydrogen bonds. Feather meal can be a valuable feed compound if the digestibility can be increased. The objective of the present study was to analyze the effects of chemical, enzymatic, and...
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2018
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ftvttcrispub:oai:cris.vtt.fi:publications/c74b9568-6f0d-4a98-9610-9d9aac5e7dcb 2024-09-09T19:30:53+00:00 In vitro pepsin digestibility and amino acid composition in soluble and residual fractions of hydrolyzed chicken feathers Adler, S. A. Slizyte, R. Honkapää, K. Løes, A. K. 2018-09-01 https://cris.vtt.fi/en/publications/c74b9568-6f0d-4a98-9610-9d9aac5e7dcb https://doi.org/10.3382/ps/pey175 http://www.scopus.com/inward/record.url?scp=85055075113&partnerID=8YFLogxK eng eng https://cris.vtt.fi/en/publications/c74b9568-6f0d-4a98-9610-9d9aac5e7dcb info:eu-repo/semantics/openAccess Adler , S A , Slizyte , R , Honkapää , K & Løes , A K 2018 , ' In vitro pepsin digestibility and amino acid composition in soluble and residual fractions of hydrolyzed chicken feathers ' , Poultry Science , vol. 97 , no. 9 , pp. 3343-3357 . https://doi.org/10.3382/ps/pey175 amino acid avian protein pepsin A animal food Salmo salar solubility protein degration chicken article 2018 ftvttcrispub https://doi.org/10.3382/ps/pey175 2024-07-17T23:31:50Z Beta-keratin in poultry feathers is a structural protein that is resistant to degradation due to disulfide and hydrogen bonds. Feather meal can be a valuable feed compound if the digestibility can be increased. The objective of the present study was to analyze the effects of chemical, enzymatic, and pressure-thermic treatments for chicken feathers on solubility, in vitro protein digestibility (IVPD), and amino acid composition of solubilized and residual fractions. Two experiments were conducted. In experiment 1, models for solubility and IVPD were developed including the above factors applying a central composite face-centered design. Addition of sodium hydroxide (NaOH) and sodium sulfite (Na 2 SO 3 ) and autoclaving time affected solubility and IVPD of the feather hydrolysates, but not addition of keratinolytic enzyme. In experiment 2, 7 combinations of the hydrolysis factors NaOH, Na 2 SO 3 , and autoclaving time with a predicted IVPD of 900 g/kg of DM, calculated for the sum of solubilized and residual feather fractions, were included to measure effects on IVPD and amino acid composition in each fraction. The IVPD values were higher for solubilized than residual fractions when treated with NaOH and autoclaving, but no differences were found when treated with Na 2 SO 3 and autoclaving. Losses of cystine were substantial for all treatments, but lower for Na 2 SO 3 than for NaOH. Furthermore, use of lower Na 2 SO 3 concentration and longer autoclaving time reduced losses of cystine. Compared with NaOH treatments, Na 2 SO 3 gave lower losses of threonine, arginine, serine, and tyrosine. With reference to the ideal protein profile for Atlantic salmon (Salmo salar L.), the treatments with 60 or 90 min autoclaving and 0.36 or 0.21% Na 2 SO 3 had the highest chemical scores. The scores were generally higher for amino acids in residual than solubilized fractions, but with 90 min autoclaving and 0.21% Na 2 SO 3 differences were small. In conclusion, hydrolysis of chicken feathers with low concentrations of Na 2 SO 3 ... Article in Journal/Newspaper Atlantic salmon Salmo salar VTT's Research Information Portal Poultry Science 97 9 3343 3357 |
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Open Polar |
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VTT's Research Information Portal |
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English |
topic |
amino acid avian protein pepsin A animal food Salmo salar solubility protein degration chicken |
spellingShingle |
amino acid avian protein pepsin A animal food Salmo salar solubility protein degration chicken Adler, S. A. Slizyte, R. Honkapää, K. Løes, A. K. In vitro pepsin digestibility and amino acid composition in soluble and residual fractions of hydrolyzed chicken feathers |
topic_facet |
amino acid avian protein pepsin A animal food Salmo salar solubility protein degration chicken |
description |
Beta-keratin in poultry feathers is a structural protein that is resistant to degradation due to disulfide and hydrogen bonds. Feather meal can be a valuable feed compound if the digestibility can be increased. The objective of the present study was to analyze the effects of chemical, enzymatic, and pressure-thermic treatments for chicken feathers on solubility, in vitro protein digestibility (IVPD), and amino acid composition of solubilized and residual fractions. Two experiments were conducted. In experiment 1, models for solubility and IVPD were developed including the above factors applying a central composite face-centered design. Addition of sodium hydroxide (NaOH) and sodium sulfite (Na 2 SO 3 ) and autoclaving time affected solubility and IVPD of the feather hydrolysates, but not addition of keratinolytic enzyme. In experiment 2, 7 combinations of the hydrolysis factors NaOH, Na 2 SO 3 , and autoclaving time with a predicted IVPD of 900 g/kg of DM, calculated for the sum of solubilized and residual feather fractions, were included to measure effects on IVPD and amino acid composition in each fraction. The IVPD values were higher for solubilized than residual fractions when treated with NaOH and autoclaving, but no differences were found when treated with Na 2 SO 3 and autoclaving. Losses of cystine were substantial for all treatments, but lower for Na 2 SO 3 than for NaOH. Furthermore, use of lower Na 2 SO 3 concentration and longer autoclaving time reduced losses of cystine. Compared with NaOH treatments, Na 2 SO 3 gave lower losses of threonine, arginine, serine, and tyrosine. With reference to the ideal protein profile for Atlantic salmon (Salmo salar L.), the treatments with 60 or 90 min autoclaving and 0.36 or 0.21% Na 2 SO 3 had the highest chemical scores. The scores were generally higher for amino acids in residual than solubilized fractions, but with 90 min autoclaving and 0.21% Na 2 SO 3 differences were small. In conclusion, hydrolysis of chicken feathers with low concentrations of Na 2 SO 3 ... |
format |
Article in Journal/Newspaper |
author |
Adler, S. A. Slizyte, R. Honkapää, K. Løes, A. K. |
author_facet |
Adler, S. A. Slizyte, R. Honkapää, K. Løes, A. K. |
author_sort |
Adler, S. A. |
title |
In vitro pepsin digestibility and amino acid composition in soluble and residual fractions of hydrolyzed chicken feathers |
title_short |
In vitro pepsin digestibility and amino acid composition in soluble and residual fractions of hydrolyzed chicken feathers |
title_full |
In vitro pepsin digestibility and amino acid composition in soluble and residual fractions of hydrolyzed chicken feathers |
title_fullStr |
In vitro pepsin digestibility and amino acid composition in soluble and residual fractions of hydrolyzed chicken feathers |
title_full_unstemmed |
In vitro pepsin digestibility and amino acid composition in soluble and residual fractions of hydrolyzed chicken feathers |
title_sort |
in vitro pepsin digestibility and amino acid composition in soluble and residual fractions of hydrolyzed chicken feathers |
publishDate |
2018 |
url |
https://cris.vtt.fi/en/publications/c74b9568-6f0d-4a98-9610-9d9aac5e7dcb https://doi.org/10.3382/ps/pey175 http://www.scopus.com/inward/record.url?scp=85055075113&partnerID=8YFLogxK |
genre |
Atlantic salmon Salmo salar |
genre_facet |
Atlantic salmon Salmo salar |
op_source |
Adler , S A , Slizyte , R , Honkapää , K & Løes , A K 2018 , ' In vitro pepsin digestibility and amino acid composition in soluble and residual fractions of hydrolyzed chicken feathers ' , Poultry Science , vol. 97 , no. 9 , pp. 3343-3357 . https://doi.org/10.3382/ps/pey175 |
op_relation |
https://cris.vtt.fi/en/publications/c74b9568-6f0d-4a98-9610-9d9aac5e7dcb |
op_rights |
info:eu-repo/semantics/openAccess |
op_doi |
https://doi.org/10.3382/ps/pey175 |
container_title |
Poultry Science |
container_volume |
97 |
container_issue |
9 |
container_start_page |
3343 |
op_container_end_page |
3357 |
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1809899851692900352 |