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1.
Food Sci Anim Resour ; 42(3): 426-440, 2022 May.
Artigo em Inglês | MEDLINE | ID: mdl-35611077

RESUMO

The bioactive functions of oligosaccharides from human milk have been reported by many studies. Many of oligosaccharides isolated from colostrum and/or milk of dairy animals have been reported to have similar chemical structures with those in human colostrum and/or milk. It has been proved by several studies that the oligosaccharides with similar chemical structure shared common bioactivities. Among domesticated dairy animals, bovine/cattle, caprine/goat, and ovine/sheep are the most commonly used species to isolate oligosaccharides from their colostrum and/or milk. Several studies on the oligosaccharides from goat colostrum and milk have revealed similar properties to that of human milk and possess the highest content of sialyl oligosaccharides (SOS) as compared to other ruminants. Indonesia ranks first in Association of Southeast Asian Nations (ASEAN) for goat milk production. Therefore, goat milk is the second most consumed milk in the country. The most reared dairy goat breed in Indonesia is Etawah Grade. However, oligosaccharides from Indonesia dairy animals including goat, have not been characterized. This is the first study to characterize oligosaccharides from Indonesia dairy animals. The present study was aimed to isolate and characterize oligosaccharides, specifically SOS from the colostrum of Etawah Grade goats by using proton/1H-nuclear magnetic resonance. The SOS successfully characterized in this study were: Neu5Ac(α2-3)Gal(ß1-4)Glc (3'-N-acetylneuraminyllactose), Neu5Ac(α2-6)Gal(ß1-4)Glc (6'-N-acetylneuraminyllactose), Neu5Gc(α2-3)Gal(ß1-4)Glc (3'-N-glycolylneuraminyllactose), Neu5Gc(α2-6)Gal(ß1-4)Glc (6'-N-glycolylneuraminyllactose), Neu5Ac(α2-6)Gal(ß1-4) GlcNAc (6'-N-acetylneuraminyllactosamine) and Neu5Gc(α2-6)Gal(ß1-4)GlcNAc (6'-N-glycolylneuraminyllactosamine). This finding shows that Etawah Grade, as a local dairy goat breed in Indonesia, is having significant potential to be natural source of oligosaccharides that can be utilized in the future food and pharmaceutical industries.

2.
Food Sci Anim Resour ; 42(2): 280-294, 2022 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-35310561

RESUMO

This study aimed to evaluate the effectiveness of propolis extract as a natural preservative for livestock products in term of chemical and microbiological characteristics by meta-analysis. The stages carried out in this study were identification, selection, checking suitability, and the resulting selected articles were used in the meta-analysis. The selection results obtained a total of 22 selected journal articles consisting of 9 articles for analysis of the antimicrobial activity of propolis extract and 13 articles for analysis of the chemical and mirobiological characteristics of livestock products. The articles were obtained from electronic databases, namely Science Direct and Google Scholar. The model used in this study is the random-effect model involving two groups, control and experimental. Heterogeneity and effect size values were carried out in this study using Hedge's obtained through openMEE software. Forest plot tests and data validation on publication bias was obtained using Kendall's test throught JASP 0.14.1 software. The results showed that there is a significant relationship between propolis extract with the results of the antimicrobial activity (p<0.05). In addition, the results of the application of propolis extract on the livestock products for the test microbes and the value of thiobarbituric acid reactive substances (TBARs) showed significant results (p<0.05). Conclusion based on the random-effect model on the effectiveness of antimicrobial activity of propolis extract and their apllication as a natural preservative of the chemical and microbiological characteristics of livestock products is valid by Kendall's test (p>0.05). Propolis in this case effectively used as natural preservatives in livestock products.

3.
Cell Stress Chaperones ; 26(2): 377-386, 2021 03.
Artigo em Inglês | MEDLINE | ID: mdl-33247372

RESUMO

FKBP22 of a psychrophilic bacterium, Shewanella sp. SIB1 (SIB1 FKBP22), is a member of peptidyl-prolyl cis-trans isomerase (PPIase) and consists of N- and C-domains responsible for chaperone-like and PPIase catalytic activities, respectively. The chaperone-like activity of SIB1 FKBP22 was previously evidenced by its ability to prevent dithiothreitol (DTT)-induced insulin aggregation. Nevertheless, the mechanism by which this protein inhibits the aggregation remains unclear. To address this, the binding affinity of SIB1 FKBP22 to the native or reduced states of insulin was examined using surface plasmon resonance (SPR). The native and reduced states refer to insulin in the absence or DTT presence, respectively. The SPR sensorgram showed that SIB1 FKBP22 binds specifically to the reduced state of insulin, with a KD value of 37.31 ± 3.20 µM. This binding was facilitated by the N-domain, as indicated by the comparable KD values of the N-domain and SIB1 FKBP22. Meanwhile, the reduced state of insulin was found to have no affinity towards the C-domain. The KD value of SIB1 FKBP22 was slightly decreased by NaCl but was not severely affected by FK506, a specific FKBP inhibitor. Similarly, the prevention of DTT-induced aggregation by SIB1 FKBP22 was also modulated by the N-domain and was not affected by FK506. Further, the reduced and native states of insulin had no effect on the catalytic efficiency (kcat/KM) of SIB1 FKBP22 towards a peptide substrate. Nevertheless, the reduced state of insulin slightly reduced the catalytic efficiency towards refolding RNase T1, at up to 1.5-fold lower than in the absence of insulin. These results suggested that the binding event was mainly facilitated by hydrophobic interaction and was independent from its PPIase activity. Altogether, a possible mechanism by which SIB1 FKBP22 prevents DTT-induced insulin aggregation was proposed.


Assuntos
Insulina/metabolismo , Shewanella/metabolismo , Proteínas de Ligação a Tacrolimo/metabolismo , Proteínas de Bactérias/metabolismo , Modelos Moleculares , Chaperonas Moleculares/metabolismo , Agregação Patológica de Proteínas , Ligação Proteica , Domínios Proteicos , Dobramento de Proteína
4.
Protein Pept Lett ; 28(6): 680-686, 2021.
Artigo em Inglês | MEDLINE | ID: mdl-33231143

RESUMO

BACKGROUND: Plantaricin IIA-1A5 is a bacteriocin produced by Lactobacillus plantarum IIA-1A5, a locally isolated probiotic from Indonesia. Plantaricin IIA-1A5 exhibits antibacterial activity against wide spectrum of pathogenic bacteria, thus promising to be applied in various food products. Nevertheless, thermal stability of this bacteriocin remains to be fully investigated. OBJECTIVE: This study aims to determine thermal stability of plantaricin IIA-1A5 through kinetic and thermodynamic parameters. METHOD: To address, plantaricin IIA-1A5 was purified from Lactobacillus plantarum IIA-1A5, which was growth under whey media, using ammonium sulfate precipitation followed by ionexchange chromatography. Purified plantaricin IIA-IA5 was then subjected to analysis of its bacteriocin activity. The thermal inactivation of bacteriocin from L. plantarum IIA-1A5 was calculated by incubating the bacteriocin at different temperatures ranging from 60-80 °C for 30 to 90 min, which was then used to calculate its kinetic and thermodynamic parameters. RESULTS: The result showed the inactivation rates (k-value) were ranging from 0.008 to 0.013 min-1. Heat resistance of plantaricin IIA-1A5 (D-value) at constant heating temperature of 60, 65, 70, 75, and 80 °C were 311.6, 305.9, 294.5, 198.9, and 180.2 min, which indicated a faster inactivation at higher temperatures. D-value sensitivity for temperature changes (z-value) was calculated to be 75.76 °C. Further, thermodynamic analysis suggested that plantaricin IIA-1A5 is thermostable, with activation energy (Ea) of 29.02 kJ mol-1. CONCLUSION: This result showed that plantaricin IIA-1A5 is considerably more heat-stable than plantaricin members and promises to be applied in food industries where heat treatments are applied. Furthermore, a possible mechanism by which plantaricin IIA-1A5 maintains its stability was also discussed by referring to its thermodynamic parameters.


Assuntos
Bacteriocinas , Lactobacillus plantarum/química , Bacteriocinas/química , Bacteriocinas/isolamento & purificação , Bacteriocinas/metabolismo , Indonésia , Cinética , Estabilidade Proteica , Termodinâmica
5.
J Food Sci ; 81(11): M2761-M2769, 2016 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-27712046

RESUMO

Probiotics may be used to enhance the functionality and nutritional values of fermented sausages. This study aims to evaluate the physicochemical and sensory properties of beef sausages fermented by lactic acid bacteria of Lactobacillus plantarum IIA-2C12 and L. acidophilus IIA-2B4. These strains were isolated from beef cattle and have shown to display probiotic features. While the nutrient contents were not affected by the probiotics, the pH, texture, and color varied among the sausages. Further analysis on fatty acids showed different profiles of saturated (C14:0, C17:0, and C20:0) and unsaturated (C14:1, C18:1n9c, C18:2n6c, and C22:6n3) fatty acids in sausages with probiotics. Gas chromatography-mass spectrometry further revealed some flavor development compounds including acid, alcohols, aldehydes, aromatic, ketones, sulfur, hydrocarbons and terpenes, varied among the sausages. Hedonic test showed no difference in the preference toward aroma, texture, and color for untrained panelists.

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