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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Published in:Poultry Science
Main Authors: Adler, Steffen Andreas, Slizyte, Rasa, Honkapää, Kaisu, Løes, Anne-Kristin
Format: Article in Journal/Newspaper
Language:English
Published: Oxford Academic 2018
Subjects:
Online Access:http://hdl.handle.net/11250/2577836
https://doi.org/10.3382/ps/pey175
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spelling ftsintef:oai:sintef.brage.unit.no:11250/2577836 2023-05-15T15:32:10+02:00 In vitro pepsin digestibility and amino acid composition in soluble and residual fractions of hydrolyzed chicken feathers Adler, Steffen Andreas Slizyte, Rasa Honkapää, Kaisu Løes, Anne-Kristin 2018-05-23 application/pdf http://hdl.handle.net/11250/2577836 https://doi.org/10.3382/ps/pey175 eng eng Oxford Academic Norges forskningsråd: 225349 Poultry Science. 2018, 97 (9), 3343-3357. urn:issn:0032-5791 http://hdl.handle.net/11250/2577836 https://doi.org/10.3382/ps/pey175 cristin:1643184 Navngivelse-Ikkekommersiell 4.0 Internasjonal http://creativecommons.org/licenses/by-nc/4.0/deed.no © The Author(s) 2018. Published by Oxford University Press on behalf of Poultry Science Association. CC-BY-NC 3343-3357 97 Poultry Science Ac Journal article Peer reviewed 2018 ftsintef https://doi.org/10.3382/ps/pey175 2021-08-04T12:00:36Z 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 (Na2SO3), 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, Na2SO3, 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 Na2SO3 and autoclaving. Losses of cystine were substantial for all treatments, but lower for Na2SO3 than for NaOH. Furthermore, use of lower Na2SO3 concentration and longer autoclaving time reduced losses of cystine. Compared with NaOH treatments, Na2SO3 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% Na2SO3 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% Na2SO3 differences were small. In conclusion, hydrolysis of chicken feathers with low concentrations of Na2SO3 combined with autoclaving results in feather meal with high nutritional value for Atlantic salmon; separation of solubilized and residual fractions is not necessary. publishedVersion Article in Journal/Newspaper Atlantic salmon Salmo salar SINTEF Open (Brage) Poultry Science 97 9 3343 3357
institution Open Polar
collection SINTEF Open (Brage)
op_collection_id ftsintef
language English
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 (Na2SO3), 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, Na2SO3, 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 Na2SO3 and autoclaving. Losses of cystine were substantial for all treatments, but lower for Na2SO3 than for NaOH. Furthermore, use of lower Na2SO3 concentration and longer autoclaving time reduced losses of cystine. Compared with NaOH treatments, Na2SO3 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% Na2SO3 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% Na2SO3 differences were small. In conclusion, hydrolysis of chicken feathers with low concentrations of Na2SO3 combined with autoclaving results in feather meal with high nutritional value for Atlantic salmon; separation of solubilized and residual fractions is not necessary. publishedVersion
format Article in Journal/Newspaper
author Adler, Steffen Andreas
Slizyte, Rasa
Honkapää, Kaisu
Løes, Anne-Kristin
spellingShingle Adler, Steffen Andreas
Slizyte, Rasa
Honkapää, Kaisu
Løes, Anne-Kristin
In vitro pepsin digestibility and amino acid composition in soluble and residual fractions of hydrolyzed chicken feathers
author_facet Adler, Steffen Andreas
Slizyte, Rasa
Honkapää, Kaisu
Løes, Anne-Kristin
author_sort Adler, Steffen Andreas
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
publisher Oxford Academic
publishDate 2018
url http://hdl.handle.net/11250/2577836
https://doi.org/10.3382/ps/pey175
genre Atlantic salmon
Salmo salar
genre_facet Atlantic salmon
Salmo salar
op_source 3343-3357
97
Poultry Science
Ac
op_relation Norges forskningsråd: 225349
Poultry Science. 2018, 97 (9), 3343-3357.
urn:issn:0032-5791
http://hdl.handle.net/11250/2577836
https://doi.org/10.3382/ps/pey175
cristin:1643184
op_rights Navngivelse-Ikkekommersiell 4.0 Internasjonal
http://creativecommons.org/licenses/by-nc/4.0/deed.no
© The Author(s) 2018. Published by Oxford University Press on behalf of Poultry Science Association.
op_rightsnorm CC-BY-NC
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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