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, S. A., Slizyte, R., Honkapää, K., Løes, A. K.
Format: Article in Journal/Newspaper
Language:English
Published: 2018
Subjects:
Online Access: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
id ftvttcrispub:oai:cris.vtt.fi:publications/c74b9568-6f0d-4a98-9610-9d9aac5e7dcb
record_format openpolar
spelling 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
institution Open Polar
collection VTT's Research Information Portal
op_collection_id ftvttcrispub
language 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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