# Advances in Intestinal Glucose Absorption Regulation for Ruminant Energy Efficiency Improvement

**Authors:** Yan Ye, Xiongfei Zhang, Junhu Yao, Xinjian Lei

PMC · DOI: 10.3390/ani16040659 · Animals : an Open Access Journal from MDPI · 2026-02-19

## TL;DR

This review explores how to improve energy efficiency in ruminants by enhancing glucose absorption in the small intestine, focusing on diet, gut microbes, and hormone signaling.

## Contribution

The paper systematically reviews mechanisms and methods to improve intestinal glucose absorption in ruminants, proposing novel strategies like artificial sweeteners and GLP-2 modulation.

## Key findings

- Functional amino acids like Leu and Phe may enhance pancreatic α-amylase activity to improve starch digestion.
- Glucose absorption in ruminants is influenced by diet, age, environment, and gut microbiota, but remains inefficient compared to fermentation.
- Artificial sweeteners and glucagon-like peptide 2-related modulation are proposed as potential strategies to boost glucose absorption.

## Abstract

Ruminant animals such as cattle and sheep mainly obtain energy from microbial digestion in the rumen. Under a high-grain diet, a large amount of starch can reach the small intestine, where digestion could yield more usable energy. However, ruminants have limited capacity to break starch into glucose and to absorb glucose into the body. An enzyme released by the pancreas is central to starch digestion, and certain dietary amino acids may increase this enzyme and improve starch use. The mechanisms enhancing glucose absorption in ruminants are less understood. This review summarizes how diet, age and development, environmental conditions, and gut microbes influence glucose absorption and describes the key sensing signals, transport steps, and hormone control involved. We also compare common methods used to measure glucose absorption and propose practical strategies to improve it, aiming to boost feed efficiency and livestock productivity.

Ruminants can use volatile fatty acids from rumen fermentation for energy, but substantial starch may bypass the rumen and enter into the small intestine under a high-grain diet. In theory, intestinal starch digestion is energetically more efficient than ruminal fermentation. However, ruminants have inherent limits in starch hydrolysis and glucose transport. Small intestinal starch digestion relies on pancreatic α-amylase. Several studies have indicated that functional amino acids (Leu or Phe) may enhance amylase secretion or activity to improve starch digestion. In contrast, strategies to increase glucose absorption efficiency in the small intestine have received less attention. Thus, this review focuses on the effects of diet, ontogeny, environment, and intestinal microbiota on intestinal glucose absorption and their potential mechanisms. The T1R2/T1R3 glucose-sensing pathways, transporting pathways, and related hormones within the small intestine were systematically reviewed. The advantages and limitations of major approaches regarding glucose absorption including portal vein intubation, nutrient perfusion, everted intestinal sacs in vitro, Ussing chamber, brush-border membrane vesicle, D-xylose test, organoid, and nanosensing are also discussed. Importantly, we propose potential strategies to improve small intestinal glucose absorption (e.g., artificial sweeteners and glucagon-like peptide 2-related modulation). Overall, this review summarizes promising regulatory targets to enhance small intestinal glucose absorption and improve energy efficiency in ruminants.

## Linked entities

- **Proteins:** TAS1R2 (taste 1 receptor member 2), TAS1R3 (taste 1 receptor member 3)
- **Chemicals:** Leu (PubChem CID 6106), Phe (PubChem CID 6140), D-xylose (PubChem CID 229)

## Full-text entities

- **Genes:** SLC2A5 (solute carrier family 2 (facilitated glucose/fructose transporter), member 5) [NCBI Gene 282868] {aka GLUT5}, GCG (glucagon) [NCBI Gene 2641] {aka GLP-1, GLP1, GLP2, GRPP}, SLC5A1 (solute carrier family 5 member 1) [NCBI Gene 282361] {aka SGLT1}, SLC2A2 (solute carrier family 2 member 2) [NCBI Gene 397429] {aka GLUT2}, TAS1R2 (taste 1 receptor member 2) [NCBI Gene 80834] {aka GPR71, T1R2, TR2}, Slc5a1 (solute carrier family 5 (sodium/glucose cotransporter), member 1) [NCBI Gene 20537] {aka Sglt1}, STR (Strength) [NCBI Gene 100307244], SLC2A2 (solute carrier family 2 member 2) [NCBI Gene 282357], SGLT1 [NCBI Gene 492300], Tas1r2 (taste receptor, type 1, member 2) [NCBI Gene 83770] {aka Gpr71, T1r2, TR2}, TAS1R3 (taste 1 receptor member 3) [NCBI Gene 83756] {aka T1R3}, INS (insulin) [NCBI Gene 280829], Glp2r (glucagon-like peptide 2 receptor) [NCBI Gene 93896] {aka 9530092J08Rik, GLP-2}, GIP (gastric inhibitory polypeptide) [NCBI Gene 511073], Tas1r3 (taste receptor, type 1, member 3) [NCBI Gene 83771] {aka Sac, T1r3}, GIPR (gastric inhibitory polypeptide receptor) [NCBI Gene 617879], AMY2A (amylase alpha 2A) [NCBI Gene 279] {aka AMY2, PA}, CCK (cholecystokinin) [NCBI Gene 617510], PLCB2 (phospholipase C beta 2) [NCBI Gene 508888], vasoactive intestinal peptide [NCBI Gene 100145884], Gip (gastric inhibitory polypeptide) [NCBI Gene 14607], SLC5A1 (solute carrier family 5 member 1) [NCBI Gene 397113] {aka SGLT1}, ASAH1 (N-acylsphingosine amidohydrolase 1) [NCBI Gene 510620], IGF1 (insulin like growth factor 1) [NCBI Gene 397491] {aka IGF-1, IGF-I, Npt2B}, EGF (epidermal growth factor) [NCBI Gene 397083], GNAT3 (G protein subunit alpha transducin 3) [NCBI Gene 516262] {aka HG1E}, TRPM5 (transient receptor potential cation channel subfamily M member 5) [NCBI Gene 100299596], GLP1R (glucagon like peptide 1 receptor) [NCBI Gene 517420], Slc2a2 (solute carrier family 2 (facilitated glucose transporter), member 2) [NCBI Gene 20526] {aka Glut-2, Glut2}, pituitary adenylate cyclase-activating polypeptide [NCBI Gene 443337], Gcg (glucagon) [NCBI Gene 14526] {aka GLP-1, Glu, PPG}
- **Diseases:** acidosis (MESH:D000138), Environmental enteropathy (MESH:D018876), malabsorption (MESH:D008286), inflammation (MESH:D007249), injury to (MESH:D014947), colonic mucosal damage (MESH:D003108), intestinal damage (MESH:D007410), villous atrophy (MESH:C564019)
- **Chemicals:** carbohydrate (MESH:D002241), Phe (MESH:D010649), starch (MESH:D013213), amino acid (MESH:D000596), PIP2 (MESH:D019269), graphene oxide (MESH:C000628730), lactic acid (MESH:D019344), lactose (MESH:D007785), Na+ (MESH:D012964), K+ (MESH:D011188), phenylboronic acid (MESH:C010686), sugar (MESH:D000073893), bile acid (MESH:D001647), BBMV (-), galactose (MESH:D005690), cAMP (MESH:D000242), calcium (MESH:D002118), blood glucose (MESH:D001786), beta-glucan (MESH:D047071), SCFAs (MESH:D005232), Glucose (MESH:D005947), 5-HT (MESH:D012701), DAG (MESH:D004075), diol (MESH:D011276), D-Xylose (MESH:D014994), propionic acid (MESH:C029658), butyric acid (MESH:D020148), luminal (MESH:D010634), Metformin (MESH:D008687), ATP (MESH:D000255), Fructose (MESH:D005632), IP3 (MESH:D015544), Leu (MESH:D007930)
- **Species:** Homo sapiens (human, species) [taxon 9606], Mus musculus (house mouse, species) [taxon 10090], Capra hircus (domestic goat, species) [taxon 9925], gut metagenome (species) [taxon 749906], Sus scrofa (pig, species) [taxon 9823], Bos taurus (bovine, species) [taxon 9913], Ovis aries (domestic sheep, species) [taxon 9940]
- **Cell lines:** L — Mus musculus (Mouse), Spontaneously immortalized cell line (CVCL_0462)

## Full text

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## References

111 references — full list in the complete paper: https://tomesphere.com/paper/PMC12937285/full.md

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Source: https://tomesphere.com/paper/PMC12937285