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Following the Digestion of Milk Proteins from Mother to Baby

[Image: see text] Little is known about the digestive process in infants. In particular, the chronological activity of enzymes across the course of digestion in the infant remains largely unknown. To create a temporal picture of how milk proteins are digested, enzyme activity was compared between in...

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Autores principales: Holton, Thérèse A., Vijayakumar, Vaishnavi, Dallas, David C., Guerrero, Andrés, Borghese, Robyn A., Lebrilla, Carlito B., German, J. Bruce, Barile, Daniela, Underwood, Mark A., Shields, Denis C., Khaldi, Nora
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2014
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4261950/
https://www.ncbi.nlm.nih.gov/pubmed/25385259
http://dx.doi.org/10.1021/pr5006907
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author Holton, Thérèse A.
Vijayakumar, Vaishnavi
Dallas, David C.
Guerrero, Andrés
Borghese, Robyn A.
Lebrilla, Carlito B.
German, J. Bruce
Barile, Daniela
Underwood, Mark A.
Shields, Denis C.
Khaldi, Nora
author_facet Holton, Thérèse A.
Vijayakumar, Vaishnavi
Dallas, David C.
Guerrero, Andrés
Borghese, Robyn A.
Lebrilla, Carlito B.
German, J. Bruce
Barile, Daniela
Underwood, Mark A.
Shields, Denis C.
Khaldi, Nora
author_sort Holton, Thérèse A.
collection PubMed
description [Image: see text] Little is known about the digestive process in infants. In particular, the chronological activity of enzymes across the course of digestion in the infant remains largely unknown. To create a temporal picture of how milk proteins are digested, enzyme activity was compared between intact human milk samples from three mothers and the gastric samples from each of their 4–12 day postpartum infants, 2 h after breast milk ingestion. The activities of 7 distinct enzymes are predicted in the infant stomach based on their observed cleavage pattern in peptidomics data. We found that the same patterns of cleavage were evident in both intact human milk and gastric milk samples, demonstrating that the enzyme activities that begin in milk persist in the infant stomach. However, the extent of enzyme activity is found to vary greatly between the intact milk and gastric samples. Overall, we observe that milk-specific proteins are cleaved at higher levels in the stomach compared to human milk. Notably, the enzymes we predict here only explain 78% of the cleavages uniquely observed in the gastric samples, highlighting that further investigation of the specific enzyme activities associated with digestion in infants is warranted.
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spelling pubmed-42619502014-12-11 Following the Digestion of Milk Proteins from Mother to Baby Holton, Thérèse A. Vijayakumar, Vaishnavi Dallas, David C. Guerrero, Andrés Borghese, Robyn A. Lebrilla, Carlito B. German, J. Bruce Barile, Daniela Underwood, Mark A. Shields, Denis C. Khaldi, Nora J Proteome Res [Image: see text] Little is known about the digestive process in infants. In particular, the chronological activity of enzymes across the course of digestion in the infant remains largely unknown. To create a temporal picture of how milk proteins are digested, enzyme activity was compared between intact human milk samples from three mothers and the gastric samples from each of their 4–12 day postpartum infants, 2 h after breast milk ingestion. The activities of 7 distinct enzymes are predicted in the infant stomach based on their observed cleavage pattern in peptidomics data. We found that the same patterns of cleavage were evident in both intact human milk and gastric milk samples, demonstrating that the enzyme activities that begin in milk persist in the infant stomach. However, the extent of enzyme activity is found to vary greatly between the intact milk and gastric samples. Overall, we observe that milk-specific proteins are cleaved at higher levels in the stomach compared to human milk. Notably, the enzymes we predict here only explain 78% of the cleavages uniquely observed in the gastric samples, highlighting that further investigation of the specific enzyme activities associated with digestion in infants is warranted. American Chemical Society 2014-10-23 2014-12-05 /pmc/articles/PMC4261950/ /pubmed/25385259 http://dx.doi.org/10.1021/pr5006907 Text en Copyright © 2014 American Chemical Society This is an open access article published under an ACS AuthorChoice License (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html) , which permits copying and redistribution of the article or any adaptations for non-commercial purposes.
spellingShingle Holton, Thérèse A.
Vijayakumar, Vaishnavi
Dallas, David C.
Guerrero, Andrés
Borghese, Robyn A.
Lebrilla, Carlito B.
German, J. Bruce
Barile, Daniela
Underwood, Mark A.
Shields, Denis C.
Khaldi, Nora
Following the Digestion of Milk Proteins from Mother to Baby
title Following the Digestion of Milk Proteins from Mother to Baby
title_full Following the Digestion of Milk Proteins from Mother to Baby
title_fullStr Following the Digestion of Milk Proteins from Mother to Baby
title_full_unstemmed Following the Digestion of Milk Proteins from Mother to Baby
title_short Following the Digestion of Milk Proteins from Mother to Baby
title_sort following the digestion of milk proteins from mother to baby
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4261950/
https://www.ncbi.nlm.nih.gov/pubmed/25385259
http://dx.doi.org/10.1021/pr5006907
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