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1.
Acta Vet Hung ; 72(1): 24-32, 2024 04 12.
Artigo em Inglês | MEDLINE | ID: mdl-38578702

RESUMO

Feeding costs of farmed insects may be reduced by applying alternative nitrogen sources such as urea that can partly substitute true proteins. The aim of this study was to examine the effects of different nitrogen sources on body weight (BW) and survival rate (SR) of the Jamaican field cricket (JFC, Gryllus assimilis), the house cricket (HC, Acheta domesticus), yellow mealworm larvae (YM, Tenebrio molitor) and superworm larvae (SW, Zophobas morio). Crickets were either housed individually or in groups, and larvae were group-housed. Six isonitrogenous feeds composed of 3.52% nitrogen were designed for all four insect species using four independent replicates with micellar casein: urea proportions of 100-0%, 75-25%, 50-50%, 25-75%, 0-100% and 100% extracted soybean meal. All selected insect species were able to utilise urea. However, urea as the only nitrogen source resulted in low final BW. In the HC, the JFC, and the YM on nitrogen basis urea can replace 25% of micellar casein without having any negative effects on BW and SR in comparison to the 100% micellar casein group. In the SW, a 25% urea level did not have a significant effect on final BW, but SR decreased significantly.


Assuntos
Besouros , Gryllidae , Tenebrio , Animais , Caseínas/metabolismo , Insetos , Larva/metabolismo , Tenebrio/metabolismo , Peso Corporal , Nitrogênio , Suplementos Nutricionais
2.
J Agric Food Chem ; 72(11): 6040-6052, 2024 Mar 20.
Artigo em Inglês | MEDLINE | ID: mdl-38454851

RESUMO

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.


Assuntos
Colostro , Glicoproteínas , Leite , Feminino , Gravidez , Lactente , Humanos , Animais , Colostro/metabolismo , Perilipina-2/metabolismo , Leite/metabolismo , Glicolipídeos/metabolismo , Gotículas Lipídicas/metabolismo , Proteínas do Leite/metabolismo , Caseínas/metabolismo
3.
Food Chem ; 448: 139054, 2024 Aug 01.
Artigo em Inglês | MEDLINE | ID: mdl-38552465

RESUMO

Quercetin (QUE) sufferred from poor processing adaptability and absorbability, hindering its application as a dietary supplement in the food industry. In this study, fatty acids (FAs)-sodium caseinate (NaCas) ligand complexes carriers were fabricated to improve the aqueous dispersibility, storage/thermal stability, and bioaccessibility of QUE using an ultrasound method. The results indicated that all six selected common dietary FAs formed stable hydrophilic complexes with NaCas and the FAs-NaCas complexes achieved an encapsulation efficiency greater than 90 % for QUE. Furthermore, the introduction of FAs enhanced the binding affinity between NaCas and QUE, but did not change the binding mode (static bursting) and types of intermolecular forces (mainly hydrogen bonding). In addition, a distinct improvement was discovered in the storage stability (>2.37-fold), thermal processing stability (>32.54 %), and bioaccessibility (>2.37-fold) of QUE. Therefore, the FAs-NaCas ligand complexes could effectively protect QUE to minimize degradation as fat-soluble polyphenol delivery vehicles.


Assuntos
Caseínas , Ácidos Graxos , Quercetina , Quercetina/química , Quercetina/metabolismo , Ácidos Graxos/química , Ácidos Graxos/metabolismo , Caseínas/química , Caseínas/metabolismo , Estabilidade de Medicamentos , Disponibilidade Biológica , Humanos , Interações Hidrofóbicas e Hidrofílicas , Água/química , Gorduras na Dieta/metabolismo
4.
FEMS Microbiol Lett ; 3712024 Jan 09.
Artigo em Inglês | MEDLINE | ID: mdl-38479791

RESUMO

Lactic acid bacteria (LAB) have evolved into fastidious microorganisms that require amino acids from environmental sources. Some LAB have cell envelope proteases (CEPs) that drive the proteolysis of high molecular weight proteins like casein in milk. CEP activity is typically studied using casein as the predominant substrate, even though CEPs can hydrolyze other protein sources. Plant protein hydrolysis by LAB has rarely been connected to the activity of specific CEPs. This study aims to show the activity of individual CEPs using LAB growth in a minimal growth medium supplemented with high molecular weight casein or potato proteins. Using Lactococcus cremoris MG1363 as isogenic background to express CEPs, we demonstrate that CEP activity is directly related to growth in the protein-supplemented minimal growth media. Proteolysis is analyzed based on the amino acid release, allowing a comparison of CEP activities and analysis of amino acid utilization by L. cremoris MG1363. This approach provides a basis to analyze CEP activity on plant-based protein substrates as casein alternatives and to compare activity of CEP homologs.


Assuntos
Lactococcus lactis , Peptídeo Hidrolases , Animais , Peptídeo Hidrolases/metabolismo , Caseínas/metabolismo , Peso Molecular , Endopeptidases/química , Lactococcus lactis/metabolismo , Aminoácidos/metabolismo
5.
Int J Biol Macromol ; 265(Pt 1): 130948, 2024 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-38503374

RESUMO

A D-optimal design was employed to optimize the microencapsulation (MEC) of basil essential oil (BEO) within a biopolymer matrix using the complex coacervation technique. BEO microcapsules (BEO-MCs) obtained under the optimal conditions exhibited high yield and efficiency with 80.45 ± 0.01 % and 93.10 ± 0.18 %, respectively. The successful MEC of BEO with an average particle size of 4.81 ± 2.86 µm was confirmed by ATR-FTIR, X-RD, and SEM analyses. Furthermore, the thermal stability of BEO-MCs was assessed using TGA-DSC analysis, which provided valuable insights into the MC's thermal stability. Furthermore, the proposed model, with a high R2 value (0.99) and low RMSE (1.56 %), was the most suitable one among the tested models for the controlled release kinetics of the optimal BEO-MCs under simulated gastrointestinal conditions. The successful optimization of BEO MEC using biopolymers through the D-optimal design could be a promising avenue for food and pharmaceutical industries, providing new strategies for the development of effective products.


Assuntos
Ocimum basilicum , Óleos Voláteis , Pectinas , Caseínas , Preparações de Ação Retardada
6.
Clin Exp Dent Res ; 10(1): e817, 2024 02.
Artigo em Inglês | MEDLINE | ID: mdl-38345511

RESUMO

OBJECTIVE: This study assessed whether combining photobiomodulation therapy (PBMT) with casein phosphopeptide-amorphous calcium phosphate fluoride (CPP-ACPF) paste can effectively reduce post-home whitening tooth sensitivity (TS) without compromising shade change. METHODS: Fifty participants were selected and assigned to one of four groups: (1) PLACEBO group-received a placebo paste and PBMT simulation; (2) PBMT group-received a placebo paste + PBMT; (3) CPP-ACPF group-received CPP-ACPF paste and PBMT simulation; (4) CPP-ACPF + PBMT group-received both CPP-ACPF paste and PBMT. The participants used whitening trays containing 22% carbamide peroxide for 2 h a day for 21 days. TS was measured daily using a visual analog scale, while shade change was assessed using a spectrophotometer: before bleaching treatment (T0), after the first (T1), second (T2), and third (T3) weeks of treatment, and 30 days (T4) after completing the whitening treatment. RESULTS: Intragroup analysis revealed that the PLACEBO group had the highest increase in sensitivity during the whitening treatment. The CPP-ACPF and PBMT groups showed no significant difference tooth whitening (TW) between weeks regarding aesthetic change. The CPP-ACPF and PBMT group exhibited a significant reduction in TS between the first and third and between the second and third weeks TW, but not between the first and second. Conversely, the PLACEBO group showed a higher sensitivity than the other groups (p < .05). The CPP-ACPF and PBMT groups did not differ from each other. Furthermore, the CPP-ACPF and PBMT group showed a greater decrease in sensitivity than the PLACEBO group at T1, T2, and T3 (p < .01), and was significantly differed from CPP-ACPF and PBMT groups only at T2 and T3. All groups confirmed TW effectiveness. Student's and paired t-test did not reveal any significant difference between groups (p > .05). CONCLUSION: Therefore, PBMT associated with CPP-ACPF paste can reduce TS without compromising the efficacy of TW.


Assuntos
Fosfatos de Cálcio , Sensibilidade da Dentina , Terapia com Luz de Baixa Intensidade , Humanos , Fluoretos/uso terapêutico , Sensibilidade da Dentina/prevenção & controle , Caseínas/uso terapêutico , Fosfopeptídeos , Ensaios Clínicos Controlados Aleatórios como Assunto
7.
Quintessence Int ; 55(2): 148-158, 2024 Feb 28.
Artigo em Inglês | MEDLINE | ID: mdl-38224103

RESUMO

OBJECTIVES: White spot lesions are more susceptible to staining agents due to their porous structure. This study examines the impact of white spot lesion treatments on discoloration caused by pediatric supplements. METHOD AND MATERIALS: Three treatments (fluoride, casein phosphopeptide-amorphous calcium phosphate [CPP-ACP], resin infiltration), a control, and their respective syrup-based subgroups (iron and black elderberry syrups) were established, each with eight teeth. Artificial white spot lesions were induced, and weekly applications of fluoride varnish, daily applications of CPP-ACP paste, or a single resin infiltration procedure were performed on the white spot lesions within the treatment groups over 4 weeks. Simultaneously, samples were exposed daily to iron or black elderberry syrups. Spectrophotometer measurements were taken at baseline, after demineralization (T0), and after 1 (T1), 2 (T2), and 4 weeks (T4). ΔE00 values were calculated. Statistical analysis was conducted using a three-way mixed-design ANOVA, with the significance level set at P = .05. RESULTS: At T4, ΔE00 values from all groups exceeded the clinical acceptability limit of 1.8. At T2 and T4, the ΔE00 values obtained from the black elderberry syrup subgroups were significantly higher (P < .001). At T4, the highest ΔE00 values were seen in the CPP-ACP groups (P < .001). The lowest ΔE00 values at T2 and T4 were observed in the resin infiltration groups (P < .05). CONCLUSIONS: Supplements containing ferrous sulfate and black elderberry extract caused color changes in white spot lesions that exceeded the clinical acceptability limit. Resin infiltration of white spot lesions provides advantages over remineralization treatments, particularly in minimizing discoloration induced by pediatric supplements.


Assuntos
Cárie Dentária , Fluoretos , Humanos , Criança , Fluoretos/farmacologia , Fluoretos/uso terapêutico , Caseínas/farmacologia , Caseínas/uso terapêutico , Esmalte Dentário , Remineralização Dentária/métodos , Ferro/farmacologia , Ferro/uso terapêutico
8.
Food Res Int ; 176: 113845, 2024 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-38163735

RESUMO

How different dietary fibers including pectin, cellulose and lignin affect casein digestibility was studied using in vitro static protocols. Peptides' profile, free amino acids (AAs) content, casein-DF interactions and their influences on enzymatic activities of proteolytic enzymes were studied using combined techniques. Under gastric and intestinal digestive conditions, while pectin could reduce casein digestibility (with an averaged decrease of 12.15% and 7.83, respectively) through both depletion flocculation and hydrogen-binding interactions, lignin inhibited the digestion of casein straightly through reducing the enzymatic activity of proteolytic enzymes, thereby altering the production of free AAs. Although cellulose showed the least detrimental effects, it still significantly reduced the content of Thr, Glu, Val, Leu, Phe, Lys, and no Arg was released. Deeper insight into casein-DF interactions and their influences on casein digestibility improves the development of more effective forms of DF for improving AA homeostasis in individuals.


Assuntos
Caseínas , Lignina , Humanos , Caseínas/metabolismo , Ração Animal/análise , Digestão , Aminoácidos/metabolismo , Fibras na Dieta/metabolismo , Celulose/farmacologia , Pectinas/farmacologia , Peptídeo Hidrolases/farmacologia
9.
Food Chem ; 441: 138340, 2024 May 30.
Artigo em Inglês | MEDLINE | ID: mdl-38176146

RESUMO

This present study investigated the masking effect of high methoxyl pectin, xanthan gum, and gum Arabic on the astringency of the traditional herbal formula Triphala and further examined the mechanism of polysaccharide reducing astringency. Results of sensory evaluation and electronic tongue illustrated that 0.6 % pectin, 0.3 % xanthan gum, and 2 % gum Arabic had a substantial deastringent effect. The polyphenols in Triphala are basically hydrolysable tannins, which with high degree of gallic acylation may be the main astringent component of Triphala. Moreover, the three polysaccharides can combine with ß-casein through CO and NH groups to form soluble binary complexes and decrease the secondary structure of ß-casein. When polysaccharides were added to the Triphala-protein system, polyphenol-protein precipitation was also diminished, and they were capable of forming soluble ternary complexes. Consequently, the competition between polysaccharides and polyphenols for binding salivary proteins and the formation of ternary complexes help decrease the astringency of Triphala.


Assuntos
Caseínas , Goma Arábica , Extratos Vegetais , Goma Arábica/química , Polissacarídeos/química , Pectinas/química , Polifenóis , Adstringentes
10.
J Oral Sci ; 66(1): 60-65, 2024.
Artigo em Inglês | MEDLINE | ID: mdl-38233156

RESUMO

PURPOSE: To investigate the surface topography and nickel content of nickel-titanium (NiTi) archwires exposed to either routine oral hygiene or a prophylactic regimen with casein phosphopeptide-amorphous calcium phosphate (CPP-ACP) during orthodontic treatment. METHODS: This in vivo study involved 40 orthodontic patients with fixed appliances, who were randomly assigned to either a routine oral hygiene group or a CPP-ACP supplementary regimen group. Twenty new NiTi archwires served as controls. All archwires underwent scanning electron microscopy and energy-dispersive spectroscopy to evaluate their surface topography and elemental composition. The nickel content was quantified as a percentage of total weight and the Ni/Ti ratio, and statistical comparisons were made using pairwise tests. RESULTS: Wires exposed to fluoride toothpaste showed signs of pitting corrosion, deep grooves, and corrosion debris. In contrast, wires exposed to supplementary CPP-ACP exhibited smooth surface areas interspersed with microdefects and deposits. Statistically significant differences in nickel content were found between the new and retrieved archwires, as well as between wires exposed to routine oral hygiene and CPP-ACP (P < 0.001). The archwires exposed to CPP-ACP had the lowest nickel content (P < 0.001). CONCLUSION: The use of CPP-ACP holds promise for application as a safe anticariogenic agent with possible protective properties during orthodontic treatment.


Assuntos
Fosfatos de Cálcio , Caseínas , Fosfopeptídeos , Humanos , Níquel/química , Titânio/química , Ligas Dentárias/química , Aparelhos Ortodônticos Fixos , Propriedades de Superfície , Teste de Materiais
11.
J Am Vet Med Assoc ; 262(3): 1-5, 2024 Mar 01.
Artigo em Inglês | MEDLINE | ID: mdl-38171089

RESUMO

OBJECTIVE: The goal of this study was to determine whether oral administration of α-casozepine (Zylkene) supplementation decreases the risk of disease in foals, as measured through salivary cortisol levels, temperature, clinical signs of disease, and body weight before and after weaning. ANIMALS: 20 Thoroughbred foals were observed over 10 weeks, beginning 14 days prior to the time of weaning. METHODS: Experimental foals were randomly selected and given α-casozepine daily for 10 weeks, while the controls received a placebo with the same frequency as the experimental group. The average daily height and weight gain were calculated to examine the effects of α-casozepine before and after weaning. Salivary cortisol levels were also compared before versus after weaning. RESULTS: There was no statistically significant difference in average daily height/weight gain or cortisol levels between the α-casozepine group and the control before and after weaning. However, the α-casozepine group had numerically less of a decline in height and growth compared to the control. This suggests that with further study Zylkene may decrease losses in foal growth rate. CLINICAL RELEVANCE: The weaning process is one of the largest stressors in a young horse's life. This abrupt process can contribute to an increased risk of disease and even morbidity. Other major stressors including separation from the mare, diet change, and new social groups can also lead to animal health and welfare concerns, as well as economic losses in weanling foals. However, further study is required to determine the benefits of α-casozepine on equine stress and health.


Assuntos
Caseínas , Hidrocortisona , Fragmentos de Peptídeos , Aumento de Peso , Animais , Cavalos , Feminino , Desmame , Suplementos Nutricionais
12.
Biol Trace Elem Res ; 202(3): 1126-1139, 2024 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-37393387

RESUMO

Protein diets are required for the normal development of the reproductive system and their inadequacy or deficiency might have hazardous functional complications during maturational and developmental stages. The study was carried out to evaluate the effect of selenium (Se) and zinc (Zn) supplementation on the male and female reproductive organs of rats with postnatal protein malnutrition. Male and female weanling rats were randomly assigned to six groups respectively. The adequate protein diet rats were fed with 16% casein diet while the protein malnourished diet (PMD) rats were fed with 5% casein diet. After the 8th week of feeding, Se (sodium selenite; Na2SeO3) and Zn (zinc sulfate; ZnSO4·7H2O) were supplemented for 3 weeks. The growth curve of body weights, lipid profile, testosterone and progesterone level, Na+-K+-ATPase activity, oxidative stress, and antioxidant status were evaluated. The results showed that PMD reduced the body weights of male and female rats. It also reduced the activities of catalase and glutathione peroxidase in the testes, but reductions in superoxide dismutase and glutathione-S-transferase activities, glutathione, vitamins C and E, testosterone, and progesterone levels were observed in both the testes and ovaries. Furthermore, PMD increased the nitric oxide level in both organs and altered the plasma lipid profiles in both sexes. Se and Zn supplementation, however, restored almost all the alterations observed in all the parameters analyzed. In conclusion, Se and Zn supplementation protects the male and female reproductive organs of rats against postnatal protein malnutrition.


Assuntos
Desnutrição , Selênio , Feminino , Ratos , Masculino , Animais , Selênio/farmacologia , Zinco/farmacologia , Caseínas , Progesterona , Antioxidantes/farmacologia , Antioxidantes/metabolismo , Suplementos Nutricionais , Glutationa/metabolismo , Glutationa Peroxidase/metabolismo , Peso Corporal , Desnutrição/tratamento farmacológico , Testosterona , Lipídeos
13.
Br J Nutr ; 131(1): 17-26, 2024 01 14.
Artigo em Inglês | MEDLINE | ID: mdl-37485899

RESUMO

Breast milk is known to contain bioactive peptides that are released during digestion, being a major source of bioactive peptides to the new-born, some of which act against invading pathogens. However, the formation of bioactive peptides during digestion of human colostrum remains largely uninvestigated. This study aimed to investigate the formation of peptides during simulated digestion of human colostrum from adult women and to prospect antimicrobial peptides. For this purpose, we used high-resolution MS to monitor the release of peptides during in vitro digestion. Bioinformatics was used for the prospection of antimicrobial activity of peptides. During simulated digestion (oral, gastric and duodenal phases), 2318 peptide sequences derived from 112 precursor proteins were identified. At the end of simulated digestion, casein-derived peptide sequences were the most frequently observed. Among precursors, some proteins were seen for the first time in this study. The resulting peptides were rich in proline, glutamine, valine and leucine residues, providing characteristic traits of antimicrobial peptides. From bioinformatics analysis, seven peptides showed potentially high antimicrobial activity towards bacteria, viruses and fungi, from which the latter was the most prominent predicted activity. Antimicrobial peptides released during digestion may provide a defence platform with controlled release for the new-born.


Assuntos
Anti-Infecciosos , Colostro , Adulto , Gravidez , Humanos , Feminino , Proteólise , Colostro/química , Espectrometria de Massas em Tandem , Peptídeos/química , Leite Humano/metabolismo , Cromatografia Líquida , Caseínas/metabolismo , Peptídeos Antimicrobianos , Proteômica/métodos , Anti-Infecciosos/farmacologia , Anti-Infecciosos/análise , Anti-Infecciosos/metabolismo , Digestão
14.
Int J Biol Macromol ; 256(Pt 2): 128064, 2024 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-37967606

RESUMO

This study developed a combination method between protein-polysaccharide complex coacervation and freezing drying for the preparation of green coffee oil (GCO) encapsulated powders. Different combinations of soy protein isolate, sodium caseinate, sodium carboxymethylcellulose, and sodium alginate were utilised as wall materials. The occurrence of complexation between the biopolymers were compared to the final emulsion of the individual protein and confirmed by fourier transform infrared spectrometry and X-ray diffraction. The mean diameter and estimated PDI of GCO microcapsules were 72.57-295.00 µm and 1.47-2.02, respectively. Furthermore, the encapsulation efficiency of GCO microcapsules was between 61.47 and 90.01 %. Finally, oxidation kinetics models of GCO and its microcapsules demonstrated that the zero-order model of GCO microcapsules was found to have a higher fit, which could better reflect the quality changes of GCO microcapsules during storage. Different combinations of proteins and polysaccharides exhibited effective oxidative stability against single proteins because of polysaccharide addition. This research revealed that soy protein isolate, sodium caseinate combined with polysaccharides can be used as a promising microencapsulating agent for microencapsulation of GCO, especially with sodium carboxymethylcellulose and sodium alginate, and provided useful information for the potential use of GCO in the development of powder food.


Assuntos
Caseínas , Proteínas de Soja , Caseínas/química , Proteínas de Soja/química , Café , Cápsulas/química , Carboximetilcelulose Sódica , Composição de Medicamentos/métodos , Polissacarídeos/química , Alginatos/química
15.
Curr Opin Clin Nutr Metab Care ; 27(1): 31-39, 2024 01 01.
Artigo em Inglês | MEDLINE | ID: mdl-38085662

RESUMO

PURPOSE OF REVIEW: Casein glycomacropeptide (CGMP) is a milk-derived bioactive sialyated phosphorylated peptide with distinctive nutritional and nutraceutical properties, produced during the cheese making process. It comprises 20-25% of total protein in whey products. CGMP is low in phenylalanine (Phe) and provides an alternative to Phe-free amino acids as a source of protein equivalent for patients with phenylketonuria (PKU). The amino acid sequence of CGMP is adapted by adding the amino acids histidine, leucine, tyrosine, arginine and tryptophan to enable its suitability in PKU. CGMP has potential antibacterial, antioxidative, prebiotic, remineralizing, digestion /metabolism and immune-modulating properties. The aim of this review is to assess the evidence for the role of CGMP in the management of PKU. RECENT FINDINGS: In PKU, there is no agreement concerning the amino acid composition of CGMP protein substitutes and consequently the nutritional composition varies between products. Although there is evidence in patients or animal models that CGMP has possible beneficial effects on gut microbiota and bone health, the results are inconclusive. Data on kinetic advantage is limited. Most studies report an increase in blood Phe levels with CGMP. Appropriate adaptations and reduction of dietary Phe intake should be made to compensate for the residual Phe content of CGMP, particularly in children. Data from short term studies indicate improved palatability of CGMP when compared to Phe-free amino acids. SUMMARY: In PKU, CGMP with supplementary amino acids, offers a safe low Phe nitrogen source. Current scientific evidence is unconvincing about its bioactive advantage in PKU. Further longitudinal research is necessary.


Assuntos
Caseínas , Fenilcetonúrias , Criança , Animais , Humanos , Suplementos Nutricionais , Aminoácidos , Fenilcetonúrias/tratamento farmacológico , Fenilcetonúrias/metabolismo , Fenilalanina/metabolismo
16.
Poult Sci ; 103(2): 103327, 2024 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-38128455

RESUMO

A study was conducted to evaluate the P digestibility in soybean meal (SBM) using the regression method with different basal diet that varied in protein sources. The treatments were organized in a 4 × 3 factorial arrangement, where 4 semipurified diets were formulated with varying source of protein (no protein supplement, or added casein, potato protein isolate (PPI), or dried egg albumen (DEA) at 60 g/kg) and 3 dietary levels of SBM (290, 370, or 450 g/kg). The study was a randomized complete block design with 8 replicate cages of 6 birds per cage. The experimental diets were fed from d 19 to 22 posthatching, excreta samples were collected from d 20 to 22, and ileal digesta samples were collected on d 22. Data were analyzed as a 2-way ANOVA using the GLM procedure. The digestibility and total tract utilization of DM, P, Ca, and N were affected by protein source (P < 0.05). Diets with casein presented the highest (P < 0.05) digestibility of N. Increasing SBM level in all dietary protein sources reduced (P < 0.001) the digestibility and total tract utilization of DM. The regression-derived ileal digestibility of P in SBM was 57.8 (SE = 3.78), 63.2 (SE = 5.02), 58.8 (SE = 4.53), and 35.3% (SE = 5.27) for diets without protein supplement, with casein, PPI, or DEA, respectively; the corresponding P retention were 52.2 (SE = 11.09), 83.4 (SE = 14.89), 42.6 (SE = 15.88), and 51.9% (SE = 14.67). The protein source affected (P < 0.05) the slope and intercept of P digestibility in SBM. A comparison of the coefficients using confidence intervals demonstrated that the ileal digestibility of P in SBM determined in diets with DEA was lower (P < 0.05) than the other protein sources, which did not differ from one another. These results indicate that the selection of dietary protein supplements may affect P digestibility assays using the regression method.


Assuntos
Fósforo na Dieta , Fósforo , Animais , Fósforo/metabolismo , Fósforo na Dieta/metabolismo , Galinhas/metabolismo , Digestão , Caseínas , Farinha , Dieta/veterinária , Íleo/metabolismo , Ração Animal/análise , Fenômenos Fisiológicos da Nutrição Animal
17.
Sci Rep ; 13(1): 19943, 2023 11 15.
Artigo em Inglês | MEDLINE | ID: mdl-37968448

RESUMO

Single amino acid (AA) supplementations in foods are increasing, however their potential nutritional and physiological impacts are not fully understood. This study examined the effects of L-lysine (Lys) supplementation on protein quality of diets, serum AA concentrations and associations between the ratio of supplemental Lys to dietary protein (X) with body weight gain (BWG) in Sprague-Dawley male rats. Rats were fed one of 10 diets containing either 7% or 20% casein and supplemented with 0% (Control), 1.5%, 3%, 6% Lys or 6% Lys + 3% L-arginine (Arg) (8 rats/diet group) for 1 week. Lys supplementation reduced the protein quality of the casein-based diets (p < 0.01). BWG was reduced by supplemental Lys when X > 0.18. Free Lys supplementation dose-dependently increased serum Lys levels (p < 0.01), while increased protein-bound Lys (1.4% vs 0.52%) had little effect on serum Lys (p > 0.05). In the 7% casein diets, ≥ 1.5% supplemental Lys reduced serum alanine, asparagine, glycine, isoleucine, leucine, serine, tyrosine, valine, carnitine, ornithine, and increased urea. Supplementation of ≥ 3% Lys additionally reduced tryptophan and increased histidine, methionine and α-aminoadipic acid (α-AAA) compared to the Control (p < 0.05). In the 20% casein diets, addition of ≥ 1.5% Lys reduced serum asparagine and threonine, and ≥ 3% Lys reduced leucine, proline, tryptophan, valine, and ornithine, and 6% Lys reduced carnitine, and increased histidine, methionine, and α-AAA. Overall, this study showed that free Lys supplementation in a Lys-sufficient diet reduced the protein quality of the diets and modified the serum concentrations of many amino acids. Excess free Lys intake adversely affected growth and utilization of nutrients due to AA imbalance or antagonism. Overall lower protein intake increases susceptibility to the adverse effects of Lys supplementation.


Assuntos
Lisina , Triptofano , Masculino , Animais , Ratos , Lisina/farmacologia , Leucina , Caseínas/farmacologia , Histidina , Asparagina , Ratos Sprague-Dawley , Suplementos Nutricionais , Aminoácidos/farmacologia , Dieta , Metionina , Proteínas Alimentares/farmacologia , Aumento de Peso , Valina , Racemetionina , Carnitina , Ornitina
18.
J Med Food ; 26(12): 911-918, 2023 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-37971778

RESUMO

The health benefits of soy foods are attributed to the high-quality protein and the bioactive compounds such as isoflavones. We previously reported that feeding obese (fa/fa) Zucker rats soy protein concentrates (SPCs) with low isoflavone (LIF) and high isoflavone (HIF) for 9 weeks significantly reduced liver steatosis compared to a casein control (C) diet. The current study extended the dietary treatments to 18 weeks to investigate the long-term effect of LIF and HIF SPC diets. 6-week-old male lean (L, n = 21) and obese (O, n = 21) Zucker rats were fed a casein C diet, LIF and HIF SPC diets for 18 weeks and body weight (BW) was recorded twice weekly. Rats were killed after 18 weeks to measure liver steatosis and serum aspartate aminotransferase and alanine aminotransferase. Obese rats had significantly greater final BW, liver weight, liver weight as the percentage of BW, and steatosis score compared to lean rats in all three dietary groups. The obese high-isoflavones (OHIF) group had significantly higher BW compared to obese control (OC) group (P < .0001) and obese low-isoflavones (OLIF) group (P = .01). OC group had significantly greater liver weight, liver weight as the percentage of BW, and liver steatosis score compared to OLIF (P = .0077, P < .0001 and P < .0001, respectively) and OHIF (P = .0094, P < .0001, and P < .0001, respectively) groups. Taken together, long-term feeding of SPC diets protected against liver steatosis regardless of isoflavone levels.


Assuntos
Fígado Gorduroso , Isoflavonas , Masculino , Ratos , Animais , Proteínas de Soja , Caseínas/farmacologia , Isoflavonas/farmacologia , Ratos Zucker , Fígado Gorduroso/prevenção & controle , Fígado/metabolismo , Obesidade/metabolismo
19.
J Agric Food Chem ; 71(43): 16184-16193, 2023 Nov 01.
Artigo em Inglês | MEDLINE | ID: mdl-37853551

RESUMO

Leucine, a kind of branched-chain amino acid, plays a regulatory role in the milk production of mammalian mammary glands, but its regulatory functions and underlying molecular mechanisms remain unknown. This work showed that a leucine-enriched mixture (LEUem) supplementation increased the levels of milk protein and milk fat synthesis in primary bovine mammary epithelial cells (BMECs). RNA-seq of leucine-treated BMECs indicated alterations in lipid metabolism, translation, ribosomal structure and biogenesis, and inflammatory response signaling pathways. Meanwhile, the supplementation of leucine resulted in mTOR activation and increased the expression of BCKDHA, FASN, ACC, and SCD1. Interestingly, the expression of PPARα was independently correlated with the leucine-supplemented dose. PPARα activated by WY-14643 caused significant suppression of lipogenic genes expression. Furthermore, WY-14643 attenuated leucine-induced ß-casein synthesis and enhanced the level of BCKDHA expression. Moreover, promoter analysis revealed a peroxisome-proliferator-response element (PPRE) site in the bovine BCKDHA promoter, and WY-14643 promoted the recruitment of PPARα onto the BCKDHA promoter. Together, the present data indicate that leucine promotes the synthesis of ß-casein and fatty acid and that PPARα-involved leucine catabolism is the key target.


Assuntos
Caseínas , PPAR alfa , Bovinos , Animais , Caseínas/genética , Caseínas/metabolismo , Leucina/farmacologia , Leucina/metabolismo , PPAR alfa/genética , PPAR alfa/metabolismo , Glândulas Mamárias Animais/metabolismo , Ácidos Graxos/metabolismo , Células Epiteliais/metabolismo , Mamíferos/metabolismo
20.
Food Funct ; 14(17): 7992-8007, 2023 Aug 29.
Artigo em Inglês | MEDLINE | ID: mdl-37580964

RESUMO

Procyanidin-amino acid interactions during transmembrane transport cause changes in the structural and physical properties of peptides, which limits further absorption of oligopeptide-advanced glycation end products (AGEs). In this study, glycated casein hydrolysates (GCSHs) were employed to investigate the structure and interaction mechanism of GCSH with lotus seedpod oligomeric procyanidin (LSOPC) complexes in an intestinal environment. LSOPC can interact with GCSH under certain conditions to form hydrogen bonds and hydrophobic interactions to form GCSH-LSOPC complexes. Results showed that procyanidin further leads to the transformation of a GCSH secondary structure and the increase of surface hydrophobicity (H0). The strongest non-covalent interaction between GCSH and (-)-epigallocatechin gallate (EGCG) was due to the polyhydroxy structure of EGCG. Binding site analysis showed that EGCG binds to the internal cavity of P1 to maintain the relative stability of the binding conformation. The antioxidant capacity of GCSH was remarkably elevated by GCSH-LSOPC. This study will provide a new reference for the accurate control of oligopeptide-AGEs absorption by LSOPC in vivo.


Assuntos
Catequina , Lotus , Proantocianidinas , Caseínas/análise , Extratos Vegetais/química , Proantocianidinas/química , Lotus/química , Antioxidantes/análise , Catequina/química , Produtos Finais de Glicação Avançada/metabolismo , Sementes/química , Digestão
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