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Tryptophan Catabolism by Gut Microbiota : = A Bridge Connecting Food Science and Human Nutrition.
Record Type:
Language materials, manuscript : Monograph/item
Title/Author:
Tryptophan Catabolism by Gut Microbiota :/
Reminder of title:
A Bridge Connecting Food Science and Human Nutrition.
Author:
Huang, Zhan.
Description:
1 online resource (233 pages)
Notes:
Source: Dissertations Abstracts International, Volume: 85-04, Section: B.
Contained By:
Dissertations Abstracts International85-04B.
Subject:
Physiology. -
Online resource:
click for full text (PQDT)
ISBN:
9798380566964
Tryptophan Catabolism by Gut Microbiota : = A Bridge Connecting Food Science and Human Nutrition.
Huang, Zhan.
Tryptophan Catabolism by Gut Microbiota :
A Bridge Connecting Food Science and Human Nutrition. - 1 online resource (233 pages)
Source: Dissertations Abstracts International, Volume: 85-04, Section: B.
Thesis (Ph.D.)--Wageningen University and Research, 2023.
Includes bibliographical references
Gut microbiota has been widely acknowledged for its essential role in human and animal health, via the production of a variety of metabolites that impact locally and systemically with aspects of host physiology. In recent years, microbiota-derived tryptophan (Trp) catabolites have gained increasing interest. Specific microbial catabolites of tryptophan can bind and activate the aryl hydrocarbon receptor (AhR), indirectly enhancing intestinal epithelial barrier function, and contributing to intestinal homeostasis. These catabolites are also suggested to be therapeutic targets in treating several diseases. It was shown that fiber-rich foods, can potentially modulate the microbial catabolism of Trp and promote the production of beneficial Trp catabolites. Therefore, this thesis aimed to gain a better understanding of the effects of dietary components on the modulation of Trp catabolism by gut microbiota. The findings highlight the necessity to consider the microbial pathway of Trp catabolism in diet-microbiome interactions.In Chapter 1,we provided a brief overview of the current knowledge regarding the Trp catabolism by gut microbiota and described the aims, the hypotheses, methodology and the content of the thesis.In Chapter 2,we used growing pigs as a model to investigate the microbiota-derived Trp catabolites present in the ileum and colon. We fed pigs with eighteen different diets and each diet had a tested food as the protein source, including algae (seaweed, spirulina), fungi (mushrooms, yeast, quorn), seeds (kidney beans, linseed, buckwheat, amaranth), cereals (wheat flour, oatmeal, millet, rice crackers, cornflakes), animal products (chicken, fish, eggs), and potato protein. The protein content in each diet was kept the same at 100 g/kg dry matter, except for rice crackers and cornflakes. Microbiota-derived Trp catabolites were extracted from ileal digesta and faeces of pigs and quantified by LC-MS. Indole (Ind), indole-3-propionic acid (IPA), indole-3-acetic acid (IAA), indole-3-lactic acid (ILA), kynurenine (Kyn), tryptamine (TA), and indole-3-aldehyde (I3A) were identified in ileal digesta. These catabolites were also identified in faeces together with skatole (Ska), oxindole (Oxi), serotonin (5-HT), and 3-indoleacrylic acid (IA). The concentration of total catabolites in faeces was higher (~200-1200 nmol/g) than that in ileal digesta (~10-50 nmol/g). Trp catabolites in ileal digesta were dominated by Ind, whereas feeding pigs with millet, kidney beans, and yeast inhibited the production of Ind in the small intestine and shifted the Trp catabolism to IAA, IPA, and ILA production. Trp catabolites in faeces were dominated by Ska, but feeding pigs with mushrooms shifted the catabolism to TA and Ind biosynthesis and feeding pigs with buckwheat shifted the catabolism to TA, IPA, Ind, and Oxi biosynthesis. Additionally, we also examined the AhR activation potential of ileal digesta and faeces of pigs. Extracts from ileal digesta failed to elicit a significant activation of AhR, while extracts from faeces significantly activated AhR.In Chapter 3, we used staticin vitrobatch fermentation inoculated with human fecal microbiota to explore the role of food matrix in Trp catabolism by gut microbiota and the resulting AhR activation. We used four different soybean preparations to reproduce different level of structural complexity of a plant matrix: single cells, cell clusters, isolated soybean protein and free Trp.
Electronic reproduction.
Ann Arbor, Mich. :
ProQuest,
2024
Mode of access: World Wide Web
ISBN: 9798380566964Subjects--Topical Terms:
673386
Physiology.
Index Terms--Genre/Form:
554714
Electronic books.
Tryptophan Catabolism by Gut Microbiota : = A Bridge Connecting Food Science and Human Nutrition.
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Source: Dissertations Abstracts International, Volume: 85-04, Section: B.
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Gut microbiota has been widely acknowledged for its essential role in human and animal health, via the production of a variety of metabolites that impact locally and systemically with aspects of host physiology. In recent years, microbiota-derived tryptophan (Trp) catabolites have gained increasing interest. Specific microbial catabolites of tryptophan can bind and activate the aryl hydrocarbon receptor (AhR), indirectly enhancing intestinal epithelial barrier function, and contributing to intestinal homeostasis. These catabolites are also suggested to be therapeutic targets in treating several diseases. It was shown that fiber-rich foods, can potentially modulate the microbial catabolism of Trp and promote the production of beneficial Trp catabolites. Therefore, this thesis aimed to gain a better understanding of the effects of dietary components on the modulation of Trp catabolism by gut microbiota. The findings highlight the necessity to consider the microbial pathway of Trp catabolism in diet-microbiome interactions.In Chapter 1,we provided a brief overview of the current knowledge regarding the Trp catabolism by gut microbiota and described the aims, the hypotheses, methodology and the content of the thesis.In Chapter 2,we used growing pigs as a model to investigate the microbiota-derived Trp catabolites present in the ileum and colon. We fed pigs with eighteen different diets and each diet had a tested food as the protein source, including algae (seaweed, spirulina), fungi (mushrooms, yeast, quorn), seeds (kidney beans, linseed, buckwheat, amaranth), cereals (wheat flour, oatmeal, millet, rice crackers, cornflakes), animal products (chicken, fish, eggs), and potato protein. The protein content in each diet was kept the same at 100 g/kg dry matter, except for rice crackers and cornflakes. Microbiota-derived Trp catabolites were extracted from ileal digesta and faeces of pigs and quantified by LC-MS. Indole (Ind), indole-3-propionic acid (IPA), indole-3-acetic acid (IAA), indole-3-lactic acid (ILA), kynurenine (Kyn), tryptamine (TA), and indole-3-aldehyde (I3A) were identified in ileal digesta. These catabolites were also identified in faeces together with skatole (Ska), oxindole (Oxi), serotonin (5-HT), and 3-indoleacrylic acid (IA). The concentration of total catabolites in faeces was higher (~200-1200 nmol/g) than that in ileal digesta (~10-50 nmol/g). Trp catabolites in ileal digesta were dominated by Ind, whereas feeding pigs with millet, kidney beans, and yeast inhibited the production of Ind in the small intestine and shifted the Trp catabolism to IAA, IPA, and ILA production. Trp catabolites in faeces were dominated by Ska, but feeding pigs with mushrooms shifted the catabolism to TA and Ind biosynthesis and feeding pigs with buckwheat shifted the catabolism to TA, IPA, Ind, and Oxi biosynthesis. Additionally, we also examined the AhR activation potential of ileal digesta and faeces of pigs. Extracts from ileal digesta failed to elicit a significant activation of AhR, while extracts from faeces significantly activated AhR.In Chapter 3, we used staticin vitrobatch fermentation inoculated with human fecal microbiota to explore the role of food matrix in Trp catabolism by gut microbiota and the resulting AhR activation. We used four different soybean preparations to reproduce different level of structural complexity of a plant matrix: single cells, cell clusters, isolated soybean protein and free Trp.
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click for full text (PQDT)
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