ABSTRACT
A protein mixture was prepared using a blend of soybean protein isolate, soybean protein concentrate, and wheat protein through high-moisture extrusion. This study investigated the effects of soybean oil/coconut oil additions (2%, 5%, and 8%) on the physiochemical properties of a soy protein-wheat protein mixture subjected to high-moisture extrusion. The protein extrudates underwent assessment for textural properties, fiber degree, sensory evaluation, microstructure, protein solubility, and protein secondary structure. The findings indicated that plant oils significantly reduced the hardness, springiness, and chewiness of the extrudates, and 5% plant oil significantly increased the fiber degree of the extrudates. In addition, the highest fiber degree and sensory evaluation score were achieved with 5% coconut oil. Observation of the macro- and microstructure indicated that the presence of unsaturated fatty acids in soybean oil did not benefit the improvement of the fibrous structure of protein extrudates during high-moisture extrusion processing. SDS-PAGE and FTIR results revealed that coconut oil, rich in saturated fatty acids, caused the clustering of medium- and low-molecular-weight subunits in texturized protein. Additionally, coconut oil elevated the ratio of 11S protein subunits containing sulfur-based amino acids and facilitated a shift from ß-turn to ß-sheet. The inclusion of plant oils increased the development of hydrogen and disulfide bonds, resulting in a denser, fibrous structure. DSC demonstrated that plant oils reduced the thermal stability of the texturized proteins but enhanced the order of protein structure.
ABSTRACT
The low rehydration properties of commercial soy protein powder (SPI), a major plant-based food ingredient, have limited the development of plant-based foods. The present study proposes a treatment of soy lecithin modification combined with Alcalase hydrolysis to improve the rehydration of soy protein powder, as well as other processing properties (emulsification, viscosity). The results show that the soy protein-soy lecithin complex powder, which is hydrolyzed for 30 min (SPH-SL-30), has the smallest particle size, the smallest zeta potential, the highest surface hydrophobicity, and a uniform microstructure. In addition, the value of the ratio of the α-helical structure/ß-folded structure was the smallest in the SPH-SL-30. After measuring the rehydration properties, emulsification properties, and viscosity, it was found that the SPH-SL-30 has the shortest wetting time of 3.04 min, the shortest dispersion time of 12.29 s, the highest solubility of 93.17%, the highest emulsifying activity of 32.42 m2/g, the highest emulsifying stability of 98.33 min, and the lowest viscosity of 0.98 pa.s. This indicates that the treatment of soy lecithin modification combined with Alcalase hydrolysis destroys the structure of soy protein, changes its physicochemical properties, and improves its functional properties. In this study, soy protein was modified by the treatment of soy lecithin modification combined with Alcalase hydrolysis to improve the processing characteristics of soy protein powders and to provide a theoretical basis for its high-value utilization in the plant-based food field.
ABSTRACT
In this study, changes in the structural and functional properties of soybean protein isolate (SPI)-naringenin (NG) complexes under different amounts of naringenin treatments were explored, elucidating the effect of the complexes as fat replacers at the 15 % substitution level on the properties of low-fat cream. Finally, the correlation between the structure and function of the complex and the properties of low-fat cream was further analyzed. The addition of NG promotes the increase of SPI aggregation and particle size, and reduces the interfacial tension of the complex. Meanwhile, at the mass ratio of 48:3, NG and SPI formed a dendritic network structure suitable for stabilizing cream. The fat properties of cream indicate that low-fat creams stabilized by appropriate proportions of SPI-NG complexes displayed small and dense fat crystal network structures. In addition, low-fat cream stabilized by the SPI-NG complexes have improved whipping time, overrun, firmness, storage stability and rheological properties compared to natural SPI. It is worth noting that the overall quality of the cream stabilized by the SPI-NG complex with a mass ratio of 48:3 was almost close to that of full-fat cream. Therefore, this study promotes the potential applications of protein-polyphenol complexes as fat replacers in the food industry.
Subject(s)
Flavanones , Soybean Proteins , Soybean Proteins/chemistry , Adsorption , Flavanones/chemistry , Protein Conformation , Protein Aggregates , Rheology , Particle SizeABSTRACT
This work aimed at building functional emulsions based on the linear dextrins (LDs) emulsion system. The gradient polyethylene glycol (PEG) precipitaion method was used to fractionate LDs into fractions with different degrees of polymerization (DP). A package, and co-precipitation procedure of LDs, and eicosapentaenoic acid (EPA) was used to fabricate LDs-EPA composites. The gas chromatograph, Fourier transform infrared spectroscopy, X-ray diffraction and differential scanning calorimetry analyses affirmed the formation of the LDs-EPA composites. The sizes of these composites were 38.55 nm, 59.14 nm to 80.62 nm, respectively, and they had good amphiphilicity. Compared with LDs, these LDs-EPA composites stabilized Pickering emulsion had higher stability and antioxidant capacity. Their emulsifying ability was positively correlated with the DP values of LDs. Furthermore, the oxidation stability results showed that LDsF10-EPA emulsion had the lowest lipid hydroperoxide (LHs) content, malondioxide (MDA) content and hexal concentration, which were 138.75 mmol kg-1 oil, 15.50 mmol kg-1 oil and 3.83 µmol kg-1 oil, respectively. The study provided a new idea and application values for the application of LDs in emulsion.
Subject(s)
Dextrins , Eicosapentaenoic Acid , Emulsions , Polymerization , Emulsions/chemistry , Eicosapentaenoic Acid/chemistry , Eicosapentaenoic Acid/analogs & derivatives , Dextrins/chemistry , Antioxidants/chemistry , Emulsifying Agents/chemistry , Polyethylene Glycols/chemistry , X-Ray DiffractionABSTRACT
The interaction mechanism between soybean protein isolate (SPI) and furan flavor compounds with different structures is studied using spectroscopy, molecular docking, and MD simulation methods. The order of binding ability between SPI and furan flavor compounds is 2-acetylfuran>furfural>5-methylfurfural. The structural differences (position and quantity of methyl groups) of three furan flavor compounds are key factors leading to the different adsorption abilities of SPI for furan flavor compounds. The findings from spectroscopy analyses suggest that the interaction between SPI and furan flavor compounds involves both static and dynamic quenching mechanisms, with static quenching being the main factor. Molecular docking and MD simulations reveal the atomic-level mechanisms underlying the stable binding for SPI and furan flavor compounds at spatiotemporal multiscale. This study provides a theoretical framework for the production and adjustment of meat essence formula in the production of soybean protein-based meat products.
Subject(s)
Flavoring Agents , Furans , Molecular Docking Simulation , Soybean Proteins , Soybean Proteins/chemistry , Adsorption , Furans/chemistry , Flavoring Agents/chemistry , Glycine max/chemistry , Meat Products/analysis , Molecular Dynamics SimulationABSTRACT
Poor storage stability limits the application of liquid diabetes formula food for special medical purposes (L-D-FSMP) in maintaining blood sugar stability in diabetic patients. This work aims to improve the stability of L-D-FSMP by adjusting the ratio of xanthan gum (XG) and carrageenan (CG) in casein (CA)-XG-CG ternary complex. The centrifugal sedimentation rate results showed that the compound ratio of XG and CG had a greater impact on L-D-FSMP storage stability. Transmission electron microscopy (TEM) results showed that the combination of CA, XG and CG occurred. Fourier transform infrared spectroscopy (FTIR) results showed that CA, XG and CG were mainly combined through hydrogen bonds and ionic bonds to form a CA-XG-CG ternary complex. When the ratio of XG and CG was 1:1, the number of disulfide bonds was the largest. The results of three-phase contact angle and emulsifying ability confirmed that when the ratio of XG and CG was 1:1, CA-XG-CG had the strongest emulsifying ability. The particle size distribution and zeta-potential results showed that when the ratio of XG and CG was 1:1, L-D-FSMP had the narrowest particle size distribution range and the strongest stability. These results may provide valuable information for the production of stable L-D-FSMP.
Subject(s)
Carrageenan , Caseins , Polysaccharides, Bacterial , Caseins/chemistry , Polysaccharides, Bacterial/chemistry , Carrageenan/chemistry , Diabetes Mellitus/drug therapy , Food, Formulated , Humans , Particle Size , Spectroscopy, Fourier Transform InfraredABSTRACT
In this study, the purpose was to investigate the effects with different concentrations of carrageenan (CG, 0-0.30%) on the gel properties and freeze-thaw stability of soy protein isolate (SPI, 8%) cold-set gels. LF-NMR, MRI, and rheology revealed that CG promoted the formation of SPI-CG cold-set gel dense three-dimensional network structures and increased gel network cross-linking sites. As visually demonstrated by microstructure observations, CG contributed to the formation of stable SPI-CG cold-set gels with uniform and compact network structures. The dense gel network formation was caused when the proportion of disulfide bonds in the intermolecular interaction of SPI-CG cold-set gels increased, and the particle size and zeta potential of SPI-CG aggregates increased. SG20 (0.20% CG) had the densest gel network in all samples. It effectively hindered the migration and flow of water, which decreased the damage of freezing to the gel network. Therefore, SG20 exhibited excellent gel strength, water holding capacity, freeze-thaw stability, and steaming stability. This was beneficial for the gel having a good quality after freeze-thaw, which provided a valuable reference for the development of freeze-thaw-resistant SPI cold-set gel products.
ABSTRACT
Nanomedicine has a profound impact on various research domains including drug delivery, diagnostics, theranostics, and regenerative medicine. Nevertheless, the clinical translation of nanomedicines for solid cancer remains limited due to the abundant physiological and pathological barriers in tumor that hinder the intratumoral penetration and distribution of these nanomedicines. In this article, we review the dynamic remodeling of tumor extracellular matrix during the tumor progression, discuss the impact of biophysical obstacles within tumors on the penetration and distribution of nanomedicines within the solid tumor and collect innovative approaches to surmount these obstacles for improving the penetration and accumulation of nanomedicines in tumor. Furthermore, we dissect the challenges and opportunities of the respective approaches, and propose potential avenues for future investigations. The purpose of this review is to provide a perspective guideline on how to effectively enhance the penetration of nanomedicines within tumors using promising methods.
Subject(s)
Antineoplastic Agents , Nanoparticles , Neoplasms , Humans , Nanomedicine , Neoplasms/drug therapy , Neoplasms/pathology , Drug Delivery Systems , Extracellular Matrix/pathology , Antineoplastic Agents/pharmacology , Antineoplastic Agents/therapeutic useABSTRACT
The primary significance of this work is that the commercial yeast proteins particles were successfully used to characterize the high internal phase Pickering emulsions (HIPPEs). The different sonication time (0,3,7,11,15 min) was used to modulate the structure and interface characteristics of yeast proteins (YPs) that as Pickering particles. Immediately afterward, the influence of YPs particles prepared at different sonication time on the rheological behavior and coalescence mechanism of HIPPEs was investigated. The results indicate that the YPs sonicated for 7 min exhibited a more relaxed molecular structures and conformation, the smallest particle size, the highest H0 and optimal amphiphilicity (the three-phase contact (θ) was 88.91°). The transition from extended to compact conformations of YPs occurred when the sonication time exceeded 7 min, resulting in an augmentation of size of YPs particles, a reduction in surface hydrophobicity (H0), and an elevation in hydrophilicity. The HIPPEs stabilized by YPs particles sonicated for 7 min exhibited the highest adsorption interface protein percentage and a more homogeneous three-dimensional (3D) protein network, resulting in the smallest droplet size and the highest storage (G'). The HIPPEs sample that stabilized by YPs particles sonicated for 15 min showed the lowest adsorption protein percentage. This caused a reduction in the thickness of its interface protein layer and an enlargement in the droplet diameter (D [3,2]). It was prone to droplet coalescence according to the equation used to evaluate the coalescence probability of droplets (Eq (2)). And the non-adsorbed YPs particles form larger aggregation structures in the continuous phase and act as "structural agents" in 3D protein network. Therefore, mechanistically, the interface protein layer formed by YPs particles sonicated 7 min contributed more to HIPPEs stability. Whereas the "structural agents" contributed more to HIPPEs stability when the sonication time exceeded 7 min. The present results shed important new light on the application of commercial YPs in the functional food fields, acting as an available and effective alternative protein.
Subject(s)
Fungal Proteins , Sonication , Emulsions/chemistry , Hydrophobic and Hydrophilic Interactions , Particle SizeABSTRACT
Recently, MLCTs have attracted considerable attention as a potential alternative to traditional oils due to their suppressive effect on fat accumulation and insulin sensitivity. In this study, the microcapsules of MLCTs with superior performance were fabricated through different homogenization processes to overcome the limitations of ω-3 medium- and long- chain triacylglycerols (MLCTs), including poor stability and prone oxidation. Additionally, the impact of various homogenization techniques, namely, high-pressure, ultrasound, and cavitation jet, on the particle structure, encapsulation efficiency, and oxidation stability of microcapsules (MLCTs) was investigated. The MLCTs microcapsules fabricated through high-pressure homogenization had a smaller particle size of 295.12 nm, lower PDI of 0.24, and a higher zeta-potential absolute value of 32.65, which significantly improved their dispersion and encapsulation efficiency, reaching 94.56 % after the spray-drying process. Furthermore, the low moisture content and superior storage stability of MLCTs microcapsules have the potential to serve as carriers of liposoluble actives.
Subject(s)
Fatty Acids, Omega-3 , Soybean Proteins , Capsules/chemistry , Fatty Acids, Omega-3/chemistry , Oxidation-Reduction , TriglyceridesABSTRACT
At present, there have been many research articles reporting that plant-based protein Pickering particles from different sources are used to stabilize Pickering emulsions, but the reports of corresponding review articles are still far from sufficient. This study focuses on the research hotspots and related progress on plant-based protein Pickering particles in the past five years. First, the article describes the mechanism by which Pickering emulsions are stabilized by different types of plant-based protein Pickering particles. Then, the extraction, preparation, and modification methods of various plant-based protein Pickering particles are highlighted to provide a reference for the development of greener and more efficient plant-based protein Pickering particles. The article also introduces some of the most promising applications of Pickering emulsions stabilized by plant-based protein Pickering particles in the food field. Finally, the paper also discusses the potential applications and challenges of plant-based protein Pickering particles in the food industry.
ABSTRACT
Exopolysaccharides (EPS) yield and added concentration of lactic acid bacteria can greatly affect the processing characteristics of fermented milk. In order to investigate the effects and mechanisms of EPS yield and added concentration on fermented milk, researchers extracted EPS from 50 strains of Lactobacillus helvedicus (L. helvedicus) and selected the two strains with the largest difference in EPS yield (L. helvedicus LH18 and L. helvetigus LH33) for subsequent experiments. The physicochemical properties of EPS-LH18 and EPS-LH33 were analyzed. The gel characteristics and protein conformation of fermented milk were studied by means of texture analyzer, rheometer, scanning electron microscopy, nuclear magnetic resonance machine, fluorescence spectrophotometer and circular dichroism. The results indicate that the monosaccharide compositions of EPS-LH18 and EPS-LH33 are the same and have good thermal stability. The texture and rheological properties of L. helveticus LH18 fermented milk are significantly superior to other fermented milk. The reason is that L. helveticus LH18 EPS has the highest yield, which leads to a denser gel structure, lower surface hydrophobicity and free sulfhydryl content of its fermented milk. According to circular dichroism analysis, ß- sheet and random coil are the internal factors leading to the difference in fermented milk gel. In addition, the fermented milk improved even more favorably as the concentration of the two EPS additions increased. As described above, L. helveticus LH18 has the potential to be an excellent yogurt starter, and both of the above EPS can be used as probiotic stabilizer alternatives for fermented dairy products.
Subject(s)
Cultured Milk Products , Lactobacillus helveticus , Probiotics , Animals , Milk/chemistry , Lactobacillus helveticus/metabolism , Fermentation , Cultured Milk Products/microbiology , Yogurt/microbiologyABSTRACT
The interactions between carboxymethyl cellulose sodium and proteins can regulate the interfacial and rheological properties of HIPEs, which plays a leading role in the stabilities of HIPEs. This article prepared various ratios of soluble soy protein isolate/carboxymethyl cellulose sodium (SPI/CMC) complexes in different proportions and examined the impact of various ratios of complexes on the structure and interface properties of complexes systems. Additionally, it explored the co-emulsification mechanism of HIPEs using SPI and CMC. At appropriate ratios of SPI/CMC, SPI and CMC mainly combine through non covalent binding and form complexes with smaller particle sizes and stronger electrostatic repulsion. The interfacial properties indicated that adding appropriate CMC increased the pliability and reduced the interfacial tension, while also enhancing the wettability of SPI/CMC complexes. At the ratio of 2:1, the SPI/CMC complexes-stabilized HIPPEs exhibited smaller oil droplets size, tighter droplet packing, and thicker interfacial film through the bridging of droplets and the generation of stronger gel-like network structures to prevent the coalescence/flocculation of droplets. These results suggested that the appropriate ratios of SPI/CMC can improve the physical stability of HIPEs by changing the structure and interface characteristics of the SPI/CMC complexes. This work provided theoretical support for stable HIPEs formed with protein-polysaccharide complexes.
Subject(s)
Carboxymethylcellulose Sodium , Soybean Proteins , Soybean Proteins/chemistry , Emulsions/chemistry , Wettability , Particle Size , SodiumABSTRACT
This research explored microwave treatment impact on the structuro-functional aspects of oxidized soy protein aggregates (OSPI). Data showed that oxidative treatment promoted the formation of high molecular weight aggregates through hydrophobic interactions, thereby disrupting the structure of natural soy protein isolates (SPI). Microwave treatment for an appropriate time (≤30 s) caused the molecular structure of OSPI to open up and reduction in molecular weight and disulfide bond content, while absolute zeta potential increased. These modifications increased emulsifying capacity of OSPI, as well as the interfacial adsorption of protein. Longer microwave treatment times (>30 s) caused OSPI to exhibit a tendency to aggregate in TEM and CLSM images. It indicated the appropriate microwave electromagnetic field effect and microwave heating effect could coordinatively regulate soy protein functional properties by modifying their aggregation behavior. The results provided new ideas for reducing resource waste, and further expanding soy protein application in the food industry.
ABSTRACT
Native soy protein isolate (N-SPI) has a low denaturation point and low solubility, limiting its industrial application. The influence of different industrial modification methods (heat (H), alkaline (A), glycosylation (G), and oxidation (O)) on the structure of SPI, the properties of the gel, and the gel properties of soy protein isolate (SPI) in myofibril protein (MP) was evaluated. The study found that four industrial modifications did not influence the subunit composition of SPI. However, the four industrial modifications altered SPI's secondary structure and disulfide bond conformation content. A-SPI exhibits the highest surface hydrophobicity and I850/830 ratio but the lowest thermal stability. G-SPI exhibits the highest disulfide bond content and the best gel properties. Compared with MP gel, the addition of H-SPI, A-SPI, G-SPI, and O-SPI components significantly improved the properties of the gel. Additionally, MP-ASPI gel exhibits the best properties and microstructure. Overall, the four industrial modification effects may impact SPI's structure and gel properties in different ways. A-SPI could be a potential functionality-enhanced soy protein ingredient in comminuted meat products. The present study results will provide a theoretical basis for the industrialized production of SPI.
ABSTRACT
The protein conformation of soymilk is the key to affecting the instant solubility of soymilk flour. This study aimed to evaluate the effect of cavitation jet treatment time (0, 2, 4, 6, and 8 min) on the instant solubility of soymilk flour based on the conformational changes of protein in soymilk. The results showed that the cavitation jet treatment for 0-4 min significantly unfolded the protein structure of soymilk and increased the content of soluble protein, which reduced the particle size and increased the electrostaticrepulsion and the viscosity of soymilk. This was beneficial for soymilk droplets fully atomized and repolymerized in the spray drying tower, forming soymilk flour particles with large size, smooth surface, and uniform distribution. When the cavitation jet treatment time was 4 min, the wettability (from 127.3 ± 2.5 s to 84.7 ± 2.1 s), dispersibility (from 70.0 ± 2.0 s to 55.7 ± 2.1 s), and solubility (from 56.54% to 78.10%) of soymilk flour were significantly improved. However, when the time of the cavitation jet treatment was extended to 8 min, the protein of soymilk aggregated and the stability of soymilk decreased, which reduced the particle size and hurt the surfacecharacteristics of soymilk flour after spraydrying. It resulted in a decrease in the instant solubility of soymilk flour. Therefore, the cavitationjet treatment with proper time increases the instant solubility of soymilk flour by improving the protein conformation of soymilk.
Subject(s)
Flour , Soy Milk , Solubility , Chemical Phenomena , Soy Milk/chemistry , Protein ConformationABSTRACT
A simple model of alternative microbiota in the developing intestinal environment has been highly desirable for the study of health and disease in the gut. The pattern of antibiotic depletion of natural gut microbes is necessary for this model. However, the effects and loci of antibiotic deletion of gut microbes remain unclear. In this study, a mixture of three proven broad-spectrum antibiotics was selected to study their effects on microbial deletions in the jejunum, ileum, and colon of mice. The 16S rRNA sequencing results showed that antibiotics significantly reduced colonic microbial diversity, with limited effects on the jejunum and ileum. At the level of microbial genera, only 93.38% of Burkholderia-Caballeronia-Paraburkholderia and 5.89% of Enterorhabdus were present in the colon after antibiotic treatment. However, such changes were not observed in the microbial composition of the jejunum and ileum. Our results suggest that the antibiotics depleted intestinal microorganisms by acting primarily in the colon and not in the small intestine (jejunum and ileum). IMPORTANCE Many studies have applied antibiotics to delete intestinal microbes to shape pseudosterile mouse models and further used for fecal microbial transplantation. However, few studies have explored the spatial location of antibiotic action in the intestine. This study shows that the selected antibiotics effectively deleted microbiota in the colon of mice, with limited effects on microbes in the jejunum and ileum. Our study provides guidance for the application of a mouse model of antibiotic deletion of intestinal microbes.
Subject(s)
Anti-Bacterial Agents , Gastrointestinal Microbiome , Animals , Mice , Anti-Bacterial Agents/pharmacology , RNA, Ribosomal, 16S/genetics , Intestine, Small , ColonABSTRACT
A cavitation jet can enhance food proteins' functionalities by regulating solvable oxidized soybean protein accumulates (SOSPI). We investigated the impacts of cavitation jet treatment on the emulsifying, structural and interfacial features of soluble soybean protein oxidation accumulate. Findings have shown that radicals in an oxidative environment not only induce proteins to form insoluble oxidative aggregates with a large particle size and high molecular weight, but also attack the protein side chains to form soluble small molecular weight protein aggregates. Emulsion prepared by SOSPI shows worse interface properties than OSPI. A cavitation jet at a short treating time (<6 min) has been shown to break the core aggregation skeleton of soybean protein insoluble aggregates, and insoluble aggregates into soluble aggregates resulting in an increase of emulsion activity (EAI) and constancy (ESI), and a decrease of interfacial tension from 25.15 to 20.19 mN/m. However, a cavitation jet at a long treating time (>6 min) would cause soluble oxidized aggregates to reaggregate through an anti-parallel intermolecular ß-sheet, which resulted in lower EAI and ESI, and a higher interfacial tension (22.44 mN/m). The results showed that suitable cavitation jet treatment could adjust the structural and functional features of SOSPI by targeted regulated transformation between the soluble and insoluble components.
ABSTRACT
The impacts of industrial phosphorylation on the structural changes, microstructure, functional, and rheological features of soybean protein isolate (SPI) were spotlighted. The findings implied that the spatial structure and functional features of the SPI changed significantly after treatment with the two phosphates. Sodium hexametaphosphate (SHMP) promoted aggregation of SPI with a larger particle size; sodium tripolyphosphate (STP) modified SPI with smaller particle size. SDS-polyacrylamide gel electrophoresis (SDS-PAGE) results showed insignificant alterations in the structure of SPI subunits. Fourier transform infrared (FTIR) and endogenous fluorescence noted a decline in α-helix quantity, an amplification in ß-fold quantity, and an increase in protein stretching and disorder, indicating that phosphorylation treatment fluctuated the spatial structure of the SPI. Functional characterization studies showed that the solubility and emulsion properties of the SPI increased to varying degrees after phosphorylation, with a maximum solubility of 94.64% for SHMP-SPI and 97.09% for STP-SPI. Emulsifying activity index (EAI) and emulsifying steadiness index (ESI) results for STP-SPI were better than those for SHMP-SPI. Rheological results showed that the modulus of G' and Gâ³ increased and the emulsion exhibited significant elastic behavior. This affords a theoretical core for expanding the industrial production applications of soybean isolates in the food and various industries.
ABSTRACT
The gut microbiota plays an evolutionarily conserved role in host metabolism, which is influenced by diet. Here, we investigated differences in shaping the gut microbiota and regulating metabolism in cow milk-based infant formula, goat milk-based infant formula, and mix milk-based infant formula compared with pasteurized human milk. 16S rRNA results showed that goat milk-based infant formula selectively increased the relative abundance of Blautia, Roseburia, Alistites and Muribaculum in the gut compared to other infant formulas. Metabolomics identification indicated that goat milk-based infant formula mainly emphasized bile acid biosynthesis, arachidonic acid metabolism and steroid biosynthesis metabolic pathways. Metabolites associated with these metabolic pathways were positively associated with increased microorganisms in goat milk-based infant formula, particularly Alistipes. Furthermore, we found a deficiency of Akkermansia abundance in three infant formula-fed compared to pasteurizedhuman milk-fed. This study presents new insights into the improvement and application of goat milk-based infant formulas in terms of intestinal microecology.