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1.
Foods ; 13(9)2024 May 03.
Artículo en Inglés | MEDLINE | ID: mdl-38731777

RESUMEN

The history of probiotics and fermented products has evolved over millennia [...].

2.
Int J Biol Macromol ; 263(Pt 1): 130098, 2024 Apr.
Artículo en Inglés | MEDLINE | ID: mdl-38342264

RESUMEN

The aim of this study was to investigate the prebiotic properties of the almond polysaccharide AP-1 on intestinal microorganisms by using an in vitro fecal fermentation method and its anti-inflammatory effect on lipopolysaccharide (LPS)-induced RAW264.7 cells. The results showed that during the in vitro fermentation of AP-1, the pH value of the fermentation broth decreased obviously, while the concentration of short-chain fatty acids (SCFAs) increased significantly, especially acetic acid and butyric acid. In genus level, the number of Clostridium and Megamonas increased markedly in the AP-1 group after 24 h of fermentation. After 48 h of fermentation, there was a noticeable increase in the number of beneficial genera Lactobacillaceae and Bifidobacteriaceae, and a considerable decrease in the number of pro-inflammatory genera. In addition, we found that AP-1 had no toxic effect on RAW264.7 cells. In the LPS-induced inflammation model of RAW264.7 cells, AP-1 could effectively inhibit the release of NO, regulate the level of reactive oxides (ROS), and effectively down-regulate the mRNA expression of TNF-α, IL-1ß, IL-6 and iNOS. In conclusion, the almond polysaccharide AP-1 may be a functional active substance aimed at promoting intestinal health and exerting anti-inflammatory effects.


Asunto(s)
Microbioma Gastrointestinal , Prunus dulcis , Prunus , Animales , Ratones , Lipopolisacáridos/farmacología , Factor de Transcripción AP-1 , Polisacáridos/química , Células RAW 264.7 , Antiinflamatorios/farmacología , Antiinflamatorios/química
3.
Int J Biol Macromol ; 264(Pt 2): 130684, 2024 Apr.
Artículo en Inglés | MEDLINE | ID: mdl-38460647

RESUMEN

The impact of recrystallization conditions and drying temperatures on the crystallization and digestibility of native waxy maize (Zea mays L.) starch (NWMS) was explored. This study involved subjecting NWMS to concurrent debranching and crystallization at 50 °C for up to 7 days. Samples were collected by oven-drying at 40, 60, and 80 °C for 24 h. This simultaneous debranching and crystallization process increased the resistant starch (RS) content by approximately 48 % compared to the native starch. The drying temperatures significantly influenced the RS content, with samples dried at 60 °C exhibiting the lowest digestibility. X-ray diffraction (XRD) analysis revealed that most crystals demonstrated a characteristic A-type arrangement. Debranching and crystallization processes enhanced the crystallinity of the samples. The specific crystal arrangement (A- or B-type) depended on the crystallization conditions. A 15 min heating of NWMS in a boiling water bath increased the digestible fraction to over 90 %, while the samples subjected to debranching and crystallization showed an increase to only about 45 %. A linear correlation between starch fractions and enthalpy was also observed.


Asunto(s)
Amilopectina , Zea mays , Temperatura , Zea mays/química , Cristalización , Difracción de Rayos X , Amilopectina/química , Almidón/química , Almidón Resistente
4.
J Agric Food Chem ; 72(6): 3210-3217, 2024 Feb 14.
Artículo en Inglés | MEDLINE | ID: mdl-38291649

RESUMEN

This study aimed to explore the differences in milk fat globule membrane (MFGM) proteins between human milk (HM) and porcine milk (PM) using a label-free quantitative proteomic approach. A total of 3920 and 4001 MFGM proteins were identified between PM and HM, respectively. Among them, 3520 common MFGM proteins were detected, including 956 significant differentially expressed MFGM proteins (DEPs). Gene ontology (GO) enrichment analysis showed that the DEPs were highly enriched in the lipid metabolic process and intrinsic component of membrane. Kyoto Encyclopedia of Genes and Genomes pathways suggested that protein processing in the endoplasmic reticulum was the most highly enriched pathway, followed by peroxisome, complement, and coagulation cascades. This study reflects the difference in the composition of MFGM proteins between HM and PM and provides a scientific and systematic reference for the development of MFGM protein nutrition.


Asunto(s)
Glicoproteínas , Proteínas de la Membrana , Proteómica , Humanos , Animales , Porcinos , Proteínas de la Membrana/genética , Proteínas de la Membrana/metabolismo , Proteínas de la Leche/metabolismo , Glucolípidos/metabolismo , Leche Humana/metabolismo , Gotas Lipídicas/metabolismo
5.
J Agric Food Chem ; 72(2): 1405-1417, 2024 Jan 17.
Artículo en Inglés | MEDLINE | ID: mdl-38181196

RESUMEN

Donkey milk fat globule membrane (MFGM) proteins are a class of membrane-bound secreted proteins with broad-spectrum biofunctional activities; however, their site-specific O-glycosylation landscapes have not been systematically mapped. In this study, an in-depth MFGM O-glycoproteome profile of donkey milk during lactation was constructed based on an intact glycopeptide-centered, label-free glycoproteomics pipeline, with 2137 site-specific O-glycans from 1121 MFGM glycoproteins and 619 site-specific O-glycans from 217 MFGM glycoproteins identified in donkey colostrum and donkey mature milk, respectively. As lactation progressed, the number of site-specific O-glycans from three glycoproteins significantly increased, whereas that of 11 site-specific O-glycans from five glycoproteins significantly decreased. Furthermore, donkey MFGM O-glycoproteins with core-1 and core-2 core structures and Lewis and sialylated branch structures may be involved in regulating apoptosis. The findings of this study reveal the differences in the composition of donkey MFGM O-glycoproteins and their site-specific O-glycosylation modification dynamic change rules during lactation, providing a molecular basis for understanding the complexity and biological functions of donkey MFGM protein O-glycosylation.


Asunto(s)
Calostro , Proteoma , Animales , Femenino , Embarazo , Calostro/química , Equidae/metabolismo , Glucolípidos/química , Glicoproteínas/química , Glicosilación , Gotas Lipídicas/química , Proteínas de la Membrana/metabolismo , Proteínas de la Leche/química , Polisacáridos/metabolismo , Proteoma/metabolismo , Espectrometría de Masas en Tándem
6.
J Agric Food Chem ; 72(11): 6040-6052, 2024 Mar 20.
Artículo en Inglés | MEDLINE | ID: mdl-38454851

RESUMEN

One type of large and intricate post-translational modification of milk proteins that has significant biological implications is phosphorylation. The characterization of phosphoproteins found in the bovine milk fat globule membrane (MFGM) is still mostly unknown. Here, label-free phosphoproteomics was used to identify 94 phosphorylation sites from 54 MFGM phosphoproteins in bovine colostrum (BC) and 136 phosphorylation sites from 91 MFGM phosphoproteins in bovine mature milk (BM). αs1-Casein and ß-casein were the most phosphorylated proteins in bovine colostrum. In bovine mature milk, perilipin-2 was the protein with the greatest number of phosphorylation sites. The results show that bovine colostrum MFGM phosphoproteins were mainly involved in immune function, whereas bovine mature MFGM phosphoproteins were mainly involved in metabolic function. Plasminogen and osteopontin were the most strongly interacting proteins in colostrum, whereas perilipin-2 was the most strongly interacting protein in bovine mature milk. This work demonstrates the unique alterations in the phosphorylation manner of the bovine MFGM protein during lactation and further expands our knowledge of the site characteristics of bovine MFGM phosphoproteins. This result confirms the value of MFGM as a reference ingredient for infant formula during different stages.


Asunto(s)
Calostro , Glicoproteínas , Leche , Femenino , Embarazo , Lactante , Humanos , Animales , Calostro/metabolismo , Perilipina-2/metabolismo , Leche/metabolismo , Glucolípidos/metabolismo , Gotas Lipídicas/metabolismo , Proteínas de la Leche/metabolismo , Caseínas/metabolismo
7.
Food Chem ; 445: 138651, 2024 Jul 01.
Artículo en Inglés | MEDLINE | ID: mdl-38359565

RESUMEN

Endogenous peptides and their parent proteins are important nutritional components with diverse biological functions. The objective of this study was to analyze and compare endogenous peptides and parent proteins found in human colostrum (HC) and human mature milk (HM) using a 4D label-free technique. In total, 5162 and 940 endogenous peptides derived from 258 parent proteins were identified in human milk by database (DB) search and de novo, respectively. Among these peptides, 2446 differentially expressed endogenous peptides with various bioactivities were identified. The Gene Ontology analysis unveiled the cellular components, biological processes, and molecular functions associated with these parent proteins. Metabolic pathway analysis suggested that neutrophil extracellular trap formation had the greatest significance with 24 parent proteins. These findings will offer a fresh perspective on the development of infant formula powder, highlighting the potential for incorporating these changes to enhance its nutritional composition and benefits.


Asunto(s)
Calostro , Proteínas de la Leche , Femenino , Embarazo , Lactante , Humanos , Calostro/metabolismo , Proteínas de la Leche/química , Espectrometría de Masas en Tándem , Leche Humana/química , Proteínas/metabolismo , Péptidos/metabolismo , Proteómica
8.
Foods ; 13(1)2024 Jan 02.
Artículo en Inglés | MEDLINE | ID: mdl-38201179

RESUMEN

Functional dyspepsia (FD) is a common functional gastrointestinal disorder. The pathophysiology remains poorly understood; however, alterations in the small intestinal microbiome have been observed. Current treatments for FD with drugs are limited, and there are certain safety problems. A class of active probiotic bacteria can control gastrointestinal homeostasis, nutritional digestion and absorption, and the energy balance when taken in certain dosages. Probiotics play many roles in maintaining intestinal microecological balance, improving the intestinal barrier function, and regulating the immune response. The presence and composition of intestinal microorganisms play a vital role in the onset and progression of FD and serve as a critical factor for both regulation and potential intervention regarding the management of this condition. Thus, there are potential advantages to alleviating FD by regulating the intestinal flora using probiotics, targeting intestinal microorganisms. This review summarizes the research progress of probiotics regarding improving FD by regulating intestinal flora and provides a reference basis for probiotics to improve FD.

9.
Food Funct ; 15(13): 7161-7173, 2024 Jul 01.
Artículo en Inglés | MEDLINE | ID: mdl-38888609

RESUMEN

Proteins and peptides play vital roles in different biological processes in vivo. As a dynamic hydrolysis system, milk is rich in proteins and proteases and provides a constant supply of endogenous bioactive peptides to newborn mammals. Previous studies have primarily focused on researching bioactive peptides by adding exogenous enzymes to milk samples. However, such an approach overlooks the significance of endogenous peptides and parent proteins that naturally exist in milk. Herein, we analyzed and compared parent proteins and their releasing peptides in human colostrum (HC), bovine colostrum (BC), and donkey colostrum (DC). The predominant proteins and hydrolyzed peptides in the three types of milk were identified. Among them, peptides were found to possess common bioactivities, including ACE inhibitory, antioxidant, antibacterial and immunomodulatory properties in HC, BC, and DC. Furthermore, the biological functions of these parent proteins were clarified using bioinformatics. These insights offer a novel perspective on natural bioactive peptides and the potential utilization of specific parent proteins and peptides to develop infant formulae derived from diverse milk sources.


Asunto(s)
Calostro , Equidae , Proteínas de la Leche , Péptidos , Proteolisis , Calostro/química , Animales , Humanos , Bovinos , Proteínas de la Leche/metabolismo , Proteínas de la Leche/química , Péptidos/metabolismo , Péptidos/análisis , Femenino , Leche Humana/química
10.
Food Chem ; 451: 139295, 2024 Sep 01.
Artículo en Inglés | MEDLINE | ID: mdl-38729042

RESUMEN

Information regarding protein expression and phosphorylation modifications in the bovine milk fat globule membrane is scarce, particularly throughout various lactation periods. This study employed a complete proteome and phosphoproteome between bovine colostrum and mature milk. A total of 11 proteins were seen in both protein expression and phosphorylation levels. There were 400 proteins identified in only protein expression, and 104 phosphoproteins identified in only phosphorylation levels. A total of 232 significant protein characteristics were identified within the proteome and significant phosphorylation sites within 86 phosphoproteins of the phosphoproteome. Biological activities and pathways primarily exhibited associations with the immune system. Simultaneously, a comprehensive analysis of proteins and phosphorylation sites using a multi-omics approach. Hence, the data we have obtained has the potential to expand our understanding of how the bovine milk fat globule membrane might be utilized as a beneficial component in dairy products.


Asunto(s)
Glucolípidos , Glicoproteínas , Lactancia , Gotas Lipídicas , Leche , Fosfoproteínas , Proteómica , Animales , Bovinos , Glicoproteínas/química , Glicoproteínas/inmunología , Glicoproteínas/metabolismo , Gotas Lipídicas/química , Gotas Lipídicas/metabolismo , Glucolípidos/química , Glucolípidos/metabolismo , Femenino , Fosfoproteínas/química , Fosfoproteínas/metabolismo , Fosfoproteínas/genética , Fosfoproteínas/inmunología , Leche/química , Proteínas de la Leche/química , Proteínas de la Leche/metabolismo , Proteínas de la Leche/inmunología , Fosforilación , Proteoma/química , Proteoma/inmunología , Proteoma/análisis
11.
Food Chem X ; 21: 101112, 2024 Mar 30.
Artículo en Inglés | MEDLINE | ID: mdl-38268845

RESUMEN

In this study, label-free proteomic technology was applied to analyze and compare the whey proteomes of porcine colostrum and mature milk. In total, 2993 and 2906 whey proteins were detected in porcine colostrum and mature milk, respectively. A total of 2745 common proteins were identified in the two milk samples, and 280 proteins were found to be significantly differentially expressed whey proteins in porcine milk. Gene Ontology analysis demonstrated that the differentially expressed whey proteins were primarily enriched in lipid homeostasis, oxidoreductase activity, and the collagen trimer. Kyoto Encyclopedia of Genes and Genomes analysis suggested that the phagosome and endocytosis were the crucial pathways. This study provides systematic and in-depth insight into the compositions and functional properties of whey proteins in porcine milk during different periods of lactation, which may be beneficial for the development of porcine whey proteins in the future.

12.
Food Funct ; 15(16): 8182-8199, 2024 Aug 12.
Artículo en Inglés | MEDLINE | ID: mdl-39027924

RESUMEN

Lactoferrin, a multifunctional iron-binding protein found in milk and other body fluids, possesses numerous biological activities. The functional activity of lactoferrin lies not only in its iron-binding capacity but also in the molecular mechanisms by which it can affect important chemical components in the host. However, the molecular mechanisms underlying these activities remain unelucidated. In this paper, we review the structure, properties, and contents of different lactoferrin milk sources. The different biological activities, namely antibacterial, antiviral, immunomodulatory, anti-inflammatory, bone regeneration, and improved metabolic disorder bioactivities, and the associated potential mechanisms of lactoferrin are summarized with the aim of providing a reference for the development of lactoferrin-related products.


Asunto(s)
Lactoferrina , Lactoferrina/farmacología , Lactoferrina/química , Humanos , Animales , Leche/química , Antibacterianos/farmacología , Antibacterianos/química , Antiinflamatorios/farmacología , Antivirales/farmacología , Antivirales/química , Factores Inmunológicos/farmacología , Agentes Inmunomoduladores/farmacología , Agentes Inmunomoduladores/química
13.
ACS Omega ; 9(1): 1643-1655, 2024 Jan 09.
Artículo en Inglés | MEDLINE | ID: mdl-38222669

RESUMEN

Conjugated linoleic acid (CLA) holds significant application prospects due to its anticancer, anti-atherosclerosis, lipid-lowering, weight-loss, and growth-promoting functions. The key to its efficient production lies in optimizing the biocatalytic performance of linoleic acid isomerase (LAI). Here, we constructed a Propionibacterium acnes mutant library and screened positive mutants with high linoleate isomerase activity. The proteomics and metabolomics were used to explore the mechanism in the regulation of linoleic acid isomerase activity. High-throughput proteomics revealed 104 differentially expressed proteins unique to positive mutant strains of linoleic acid isomerase of which 57 were upregulated and 47 were downregulated. These differentially expressed proteins were primarily involved in galactose metabolism, the phosphotransferase system, starch metabolism, and sucrose metabolism. Differential metabolic pathways were mainly enriched in amino acid biosynthesis, including glutamate metabolism, the Aminoacyl-tRNA biosynthesis pathway, and the ABC transporter pathway. The upregulated metabolites include dl-valine and Acetyl coA, while the downregulated metabolites include Glutamic acid and Phosphoenolpyruvate. Overall, the activity of linoleic acid isomerase in the mutant strain was increased by the regulation of key proteins involved in galactose metabolism, sucrose metabolism, and the phosphotransferase system. This study provides a theoretical basis for the development of high-yield CLA food.

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