{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T14:34:24Z","timestamp":1790951664772,"version":"4.1.0"},"reference-count":54,"publisher":"Oxford University Press (OUP)","issue":"8","license":[{"start":{"date-parts":[[2020,7,16]],"date-time":"2020-07-16T00:00:00Z","timestamp":1594857600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2020,8,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Soybean meal (SBM) contains anti-nutritional factors (ANF) that may limit kinetics and total extent of protein digestion in pigs. This study evaluated the effects of thermomechanical and enzyme-facilitated (TE) processing on in vitro kinetics of crude protein (CP) digestion and CP and amino acid (AA) digestibility in weaned pigs. Each batch of SBM (48% CP) was divided into two parts: non-processed SBM as control vs. thermomechanical and enzyme-facilitated processed soybean meal (TES) as the experimental group. For digestion kinetics, samples (three batches of non-processed SBM vs. TES) were incubated in triplicate sequentially with pepsin at pH 3.5 for 1.5 h (stomach phase) and subsequently with pancreatin and bile extract at pH 6.8 for 0, 0.5, 1, 2, 4, or 6 h (small intestine phase). Protein was classified into CPfast, CPslow, and CPresistant corresponding to CP digested within the first 0.5 h, from 0.5 to 4 h, and after 4 h plus undigested CP, respectively. Eight weaned barrows (Large White \u00d7 Duroc, 9.43 \u00b1 0.40 kg) were surgically fitted with a T-cannula at the terminal ileum. Pigs were randomly assigned to a Youden square with three diets over four periods. The three diets were an N-free diet and two diets using 40% SBM or TES as the sole source of AA with Cr2O3 as an indigestible marker. Each period included sequentially a 5-d adaptation, 2-d collection of feces, and 2-d collection of ileal digesta. The TE processing reduced ANF content in TES by 91% for lectin, 22% for trypsin inhibitor activity, 75% for \u03b2-conglycinin, and 62% for glycinin compared with SBM. In vitro, TE processing increased (P &amp;lt; 0.05) digested CP by 5.6% and enhanced the kinetics of CP digestion by tending to increase (P = 0.056) CPfast by 25% and reducing (P &amp;lt; 0.05) CPslow and CPresistant by 48% and 11%, respectively. In pigs, TE processing increased (P &amp;lt; 0.05) apparent ileal digestibility (AID) and standardized ileal digestibility (SID) of CP in TES by 2.3% and 2.1%, respectively. The TE processing increased (P &amp;lt; 0.05) AID and SID of all AA up to 3.3%, except for AID of Pro and SID of Pro, Gly, and Cys. The TE processing did not change reactive Lys or Lys:CP but increased (P &amp;lt; 0.05) SID of Lys and reactive Lys by 3%. Combined, the greater in vitro digestion kinetics matched the greater in vivo AID and SID of CP in TES and lower ANF compared with SBM. Thus, TE processing created a protein source that is digested faster and to a greater extent than SBM, thereby lowering the chance of protein fermentation.<\/jats:p>","DOI":"10.1093\/jas\/skaa224","type":"journal-article","created":{"date-parts":[[2020,7,16]],"date-time":"2020-07-16T06:22:44Z","timestamp":1594880564000},"source":"Crossref","is-referenced-by-count":13,"title":["Thermomechanical and enzyme-facilitated processing of soybean meal enhanced in vitro kinetics of protein digestion and protein and amino acid digestibility in weaned pigs"],"prefix":"10.1093","volume":"98","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-2473-2041","authenticated-orcid":false,"given":"Mai Anh","family":"Ton Nu","sequence":"first","affiliation":[{"name":"Agilia a\/s, Videbaek, Denmark"},{"name":"AB Agri Ltd., Peterborough, UK"},{"name":"Department of Agricultural, Food and Nutritional Science, University of Alberta, Edmonton, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ingrid","family":"Lupatsch","sequence":"additional","affiliation":[{"name":"AB Agri Ltd., Peterborough, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joaquin S","family":"Zannatta","sequence":"additional","affiliation":[{"name":"Department of Agricultural, Food and Nutritional Science, University of Alberta, Edmonton, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hagen","family":"Schulze","sequence":"additional","affiliation":[{"name":"AB Agri Ltd., Peterborough, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ruurd T","family":"Zijlstra","sequence":"additional","affiliation":[{"name":"Department of Agricultural, Food and Nutritional Science, University of Alberta, Edmonton, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2020,7,16]]},"reference":[{"key":"2020081014262826700_CIT0001","first-page":"903","article-title":"Digestion and balance techniques in pigs.","volume-title":"Swine nutrition","author":"Adeola","year":"2001","edition":"2nd ed"},{"key":"2020081014262826700_CIT0002","doi-asserted-by":"crossref","first-page":"911","DOI":"10.1111\/ijfs.12386","article-title":"Structure, trypsin inhibitor activity and functional properties of germinated soybean protein isolate","volume":"49","author":"Aijie","year":"2014","journal-title":"Int. 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