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Protein Digestion

Protein Digestion

Protein digestion begins in the stomach, where the highly acidic environment can easily disrupt protein structure by exposing the peptide bonds of polypeptide chains. After polypeptide chains are broken into individual amino acids by a series of digestive enzymes, the amino acids are transported to the liver via the bloodstream to produce energy.

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Related Experiment Video

Updated: Mar 15, 2026

An Efficient Method for the Isolation of Highly Purified RNA from Seeds for Use in Quantitative Transcriptome Analysis

An Efficient Method for the Isolation of Highly Purified RNA from Seeds for Use in Quantitative Transcriptome Analysis

Published on: January 11, 2017

Rapeseed napin and cruciferin are readily digested by poultry.

M M Kasprzak¹, J G M Houdijk², S Liddell¹

¹School of Biosciences, University of Nottingham, Loughborough, UK.

Journal of Animal Physiology and Animal Nutrition

|August 27, 2016

Summary

This summary is machine-generated.

Rapeseed proteins, napin and cruciferin, are readily digested by broiler chickens. This study found no detectable rapeseed proteins in ileal digesta, challenging previous assumptions about their poor digestibility.

Keywords:

chickens cruciferin napin protein rapeseed cake rapeseed meal

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Last Updated: Mar 15, 2026

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Published on: January 11, 2017

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Laboratory Production of Biofuels and Biochemicals from a Rapeseed Oil through Catalytic Cracking Conversion

Laboratory Production of Biofuels and Biochemicals from a Rapeseed Oil through Catalytic Cracking Conversion

Published on: September 2, 2016

Area of Science:

Animal Nutrition
Protein Biochemistry
Poultry Science

Background:

Rapeseed proteins, specifically napin and cruciferin, have been historically considered poorly digestible in non-ruminant animals.
Understanding the digestibility of these proteins is crucial for optimizing poultry feed formulations.

Purpose of the Study:

To assess the ileal digestibility of napin and cruciferin in broiler chickens.
To evaluate the impact of varying protein levels in rapeseed co-products on protein digestion.

Main Methods:

Sixteen rapeseed co-product samples with diverse protein content were incorporated into semi-synthetic diets for broiler chickens.
Proteins in dietary samples and ileal digesta were extracted and analyzed using gel-based liquid chromatography-tandem mass spectrometry (LC-MS/MS).

Main Results:

Three napin isomers and nine cruciferin types were identified in the rapeseed co-products.
No rapeseed proteins (napin or cruciferin) were detected in the ileal digesta of broiler chickens.
Endogenous digestive enzymes like trypsin and chymotrypsin were identified in the ileal digesta.

Conclusions:

Rapeseed proteins are readily digestible by broiler chickens, contrary to prior beliefs.
Digestibility is not significantly affected by the protein content of the rapeseed co-products within the tested range.