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Rapeseed napin and cruciferin are readily digested by poultry
Summary Rapeseed proteins have been considered as being poorly digestible in the gut of non‐ruminants. The aim of the study was to assess the digestibility of napin and cruciferin in ileal digesta of broiler chickens, testing sixteen samples of rapeseed co‐products with protein levels ranging from 2...
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Published in: | Journal of animal physiology and animal nutrition 2017-08, Vol.101 (4), p.658-666 |
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container_title | Journal of animal physiology and animal nutrition |
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creator | Kasprzak, M. M. Houdijk, J. G. M. Liddell, S. Davis, K. Olukosi, O. A. Kightley, S. White, G. A. Wiseman, J. |
description | Summary
Rapeseed proteins have been considered as being poorly digestible in the gut of non‐ruminants. The aim of the study was to assess the digestibility of napin and cruciferin in ileal digesta of broiler chickens, testing sixteen samples of rapeseed co‐products with protein levels ranging from 293 g/kg to 560 g/kg dry matter. Each sample was included into a semi‐synthetic diet at a rate of 500 g/kg and evaluated with broiler chickens in a randomised design. Dietary and ileal digesta proteins were extracted and identified by gel‐based liquid chromatography–tandem mass spectrometry (LC‐MS/MS). Three isomers of napin (a 2S albumin) and nine cruciferins (an 11S globulin) were identified in the rapeseed co‐products, whereas six endogenous enzymes such as trypsin (I‐P1, II‐P29), chymotrypsin (elastase and precursor), carboxypeptidase B and α‐amylase were found in the ileal digesta. It is concluded that as none of the rapeseed proteins were detected in the ileal digesta, rapeseed proteins can be readily digested by broiler chickens, irrespective of the protein content in the diet. |
doi_str_mv | 10.1111/jpn.12576 |
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Rapeseed proteins have been considered as being poorly digestible in the gut of non‐ruminants. The aim of the study was to assess the digestibility of napin and cruciferin in ileal digesta of broiler chickens, testing sixteen samples of rapeseed co‐products with protein levels ranging from 293 g/kg to 560 g/kg dry matter. Each sample was included into a semi‐synthetic diet at a rate of 500 g/kg and evaluated with broiler chickens in a randomised design. Dietary and ileal digesta proteins were extracted and identified by gel‐based liquid chromatography–tandem mass spectrometry (LC‐MS/MS). Three isomers of napin (a 2S albumin) and nine cruciferins (an 11S globulin) were identified in the rapeseed co‐products, whereas six endogenous enzymes such as trypsin (I‐P1, II‐P29), chymotrypsin (elastase and precursor), carboxypeptidase B and α‐amylase were found in the ileal digesta. It is concluded that as none of the rapeseed proteins were detected in the ileal digesta, rapeseed proteins can be readily digested by broiler chickens, irrespective of the protein content in the diet.</description><identifier>ISSN: 0931-2439</identifier><identifier>EISSN: 1439-0396</identifier><identifier>DOI: 10.1111/jpn.12576</identifier><identifier>PMID: 27562881</identifier><language>eng</language><publisher>Germany: Wiley Subscription Services, Inc</publisher><subject>2S Albumins, Plant - chemistry ; 2S Albumins, Plant - metabolism ; Albumin ; Amylases ; Animal Feed - analysis ; Animal Nutritional Physiological Phenomena ; Animals ; Antigens, Plant - chemistry ; Antigens, Plant - metabolism ; Brassica rapa - chemistry ; Carboxypeptidase B ; Chickens ; Chickens - metabolism ; Chymotrypsin ; cruciferin ; Diet - veterinary ; Digestibility ; Dry matter ; Elastase ; Enzymes ; Gastrointestinal tract ; Globulins ; Isomers ; Liquid chromatography ; Male ; Mass spectrometry ; Mass spectroscopy ; napin ; Poultry ; protein ; Proteins ; Rapeseed ; rapeseed cake ; rapeseed meal ; Seed Storage Proteins - chemistry ; Seed Storage Proteins - metabolism ; Trypsin ; α-Amylase</subject><ispartof>Journal of animal physiology and animal nutrition, 2017-08, Vol.101 (4), p.658-666</ispartof><rights>Journal of Animal Physiology and Animal Nutrition © 2016 Blackwell Verlag GmbH</rights><rights>Journal of Animal Physiology and Animal Nutrition © 2016 Blackwell Verlag GmbH.</rights><rights>2017 Blackwell Verlag GmbH</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3886-d0f0ec39b8ec844a4f0022af71a6fb5b86030363a9efaf19c9cce9d61f2fe7633</citedby><cites>FETCH-LOGICAL-c3886-d0f0ec39b8ec844a4f0022af71a6fb5b86030363a9efaf19c9cce9d61f2fe7633</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27562881$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kasprzak, M. M.</creatorcontrib><creatorcontrib>Houdijk, J. G. M.</creatorcontrib><creatorcontrib>Liddell, S.</creatorcontrib><creatorcontrib>Davis, K.</creatorcontrib><creatorcontrib>Olukosi, O. A.</creatorcontrib><creatorcontrib>Kightley, S.</creatorcontrib><creatorcontrib>White, G. A.</creatorcontrib><creatorcontrib>Wiseman, J.</creatorcontrib><title>Rapeseed napin and cruciferin are readily digested by poultry</title><title>Journal of animal physiology and animal nutrition</title><addtitle>J Anim Physiol Anim Nutr (Berl)</addtitle><description>Summary
Rapeseed proteins have been considered as being poorly digestible in the gut of non‐ruminants. The aim of the study was to assess the digestibility of napin and cruciferin in ileal digesta of broiler chickens, testing sixteen samples of rapeseed co‐products with protein levels ranging from 293 g/kg to 560 g/kg dry matter. Each sample was included into a semi‐synthetic diet at a rate of 500 g/kg and evaluated with broiler chickens in a randomised design. Dietary and ileal digesta proteins were extracted and identified by gel‐based liquid chromatography–tandem mass spectrometry (LC‐MS/MS). Three isomers of napin (a 2S albumin) and nine cruciferins (an 11S globulin) were identified in the rapeseed co‐products, whereas six endogenous enzymes such as trypsin (I‐P1, II‐P29), chymotrypsin (elastase and precursor), carboxypeptidase B and α‐amylase were found in the ileal digesta. It is concluded that as none of the rapeseed proteins were detected in the ileal digesta, rapeseed proteins can be readily digested by broiler chickens, irrespective of the protein content in the diet.</description><subject>2S Albumins, Plant - chemistry</subject><subject>2S Albumins, Plant - metabolism</subject><subject>Albumin</subject><subject>Amylases</subject><subject>Animal Feed - analysis</subject><subject>Animal Nutritional Physiological Phenomena</subject><subject>Animals</subject><subject>Antigens, Plant - chemistry</subject><subject>Antigens, Plant - metabolism</subject><subject>Brassica rapa - chemistry</subject><subject>Carboxypeptidase B</subject><subject>Chickens</subject><subject>Chickens - metabolism</subject><subject>Chymotrypsin</subject><subject>cruciferin</subject><subject>Diet - veterinary</subject><subject>Digestibility</subject><subject>Dry matter</subject><subject>Elastase</subject><subject>Enzymes</subject><subject>Gastrointestinal tract</subject><subject>Globulins</subject><subject>Isomers</subject><subject>Liquid chromatography</subject><subject>Male</subject><subject>Mass spectrometry</subject><subject>Mass spectroscopy</subject><subject>napin</subject><subject>Poultry</subject><subject>protein</subject><subject>Proteins</subject><subject>Rapeseed</subject><subject>rapeseed cake</subject><subject>rapeseed meal</subject><subject>Seed Storage Proteins - chemistry</subject><subject>Seed Storage Proteins - metabolism</subject><subject>Trypsin</subject><subject>α-Amylase</subject><issn>0931-2439</issn><issn>1439-0396</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><recordid>eNp10E1LxDAQBuAgirt-HPwDUvCih2omadPk4EEWPxEV0XNI04l06bY12SL990Z39SA4lzDh4WV4CTkAegpxzuZ9ewosL8QGmULGVUq5EptkShWHlMWPCdkJYU4pFDkV22TCilwwKWFKzp9NjwGxSlrT121i2iqxfrC1Q_-1ekw8mqpuxqSq3zAsoyzHpO-GZunHPbLlTBNwf_3uktery5fZTXr_eH07u7hPLZdSpBV1FC1XpUQrs8xkjlLGjCvACFfmpRSUUy64UeiMA2WVtagqAY45LATnu-R4ldv77n2IV-hFHSw2jWmxG4IGmasC8gxopEd_6LwbfBuv06CgYDKXDKI6WSnruxA8Ot37emH8qIHqr0517FR_dxrt4TpxKBdY_cqfEiM4W4GPusHx_yR99_SwivwE2N1_hg</recordid><startdate>201708</startdate><enddate>201708</enddate><creator>Kasprzak, M. M.</creator><creator>Houdijk, J. G. M.</creator><creator>Liddell, S.</creator><creator>Davis, K.</creator><creator>Olukosi, O. A.</creator><creator>Kightley, S.</creator><creator>White, G. A.</creator><creator>Wiseman, J.</creator><general>Wiley Subscription Services, Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QG</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>201708</creationdate><title>Rapeseed napin and cruciferin are readily digested by poultry</title><author>Kasprzak, M. M. ; Houdijk, J. G. M. ; Liddell, S. ; Davis, K. ; Olukosi, O. A. ; Kightley, S. ; White, G. 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A.</creatorcontrib><creatorcontrib>Wiseman, J.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of animal physiology and animal nutrition</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kasprzak, M. M.</au><au>Houdijk, J. G. M.</au><au>Liddell, S.</au><au>Davis, K.</au><au>Olukosi, O. A.</au><au>Kightley, S.</au><au>White, G. A.</au><au>Wiseman, J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Rapeseed napin and cruciferin are readily digested by poultry</atitle><jtitle>Journal of animal physiology and animal nutrition</jtitle><addtitle>J Anim Physiol Anim Nutr (Berl)</addtitle><date>2017-08</date><risdate>2017</risdate><volume>101</volume><issue>4</issue><spage>658</spage><epage>666</epage><pages>658-666</pages><issn>0931-2439</issn><eissn>1439-0396</eissn><abstract>Summary
Rapeseed proteins have been considered as being poorly digestible in the gut of non‐ruminants. The aim of the study was to assess the digestibility of napin and cruciferin in ileal digesta of broiler chickens, testing sixteen samples of rapeseed co‐products with protein levels ranging from 293 g/kg to 560 g/kg dry matter. Each sample was included into a semi‐synthetic diet at a rate of 500 g/kg and evaluated with broiler chickens in a randomised design. Dietary and ileal digesta proteins were extracted and identified by gel‐based liquid chromatography–tandem mass spectrometry (LC‐MS/MS). Three isomers of napin (a 2S albumin) and nine cruciferins (an 11S globulin) were identified in the rapeseed co‐products, whereas six endogenous enzymes such as trypsin (I‐P1, II‐P29), chymotrypsin (elastase and precursor), carboxypeptidase B and α‐amylase were found in the ileal digesta. It is concluded that as none of the rapeseed proteins were detected in the ileal digesta, rapeseed proteins can be readily digested by broiler chickens, irrespective of the protein content in the diet.</abstract><cop>Germany</cop><pub>Wiley Subscription Services, Inc</pub><pmid>27562881</pmid><doi>10.1111/jpn.12576</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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subjects | 2S Albumins, Plant - chemistry 2S Albumins, Plant - metabolism Albumin Amylases Animal Feed - analysis Animal Nutritional Physiological Phenomena Animals Antigens, Plant - chemistry Antigens, Plant - metabolism Brassica rapa - chemistry Carboxypeptidase B Chickens Chickens - metabolism Chymotrypsin cruciferin Diet - veterinary Digestibility Dry matter Elastase Enzymes Gastrointestinal tract Globulins Isomers Liquid chromatography Male Mass spectrometry Mass spectroscopy napin Poultry protein Proteins Rapeseed rapeseed cake rapeseed meal Seed Storage Proteins - chemistry Seed Storage Proteins - metabolism Trypsin α-Amylase |
title | Rapeseed napin and cruciferin are readily digested by poultry |
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