RESUMEN
Steel corrosion is a global issue that affects safety and the economy. Currently, the homopolysaccharide (HoPS) structure of a novel lactic acid bacterium (LAB) is under study, as well as its application as a green corrosion inhibitor. Weissella cibaria FMy 2-21-1 is a LAB strain capable of producing HoPS in sucrose enriched media. The isolated and purified HoPS was characterized by different spectroscopic analyses as a linear α-1,6 dextran adopting a random coil conformation, with high molecular weight and extended size in water. The polysaccharide showed a semi-crystalline organization, which is a requirement for film formation. Its biocoating showed a grainy network structure, with a slightly lesser hydrophobic role in the aqueous environment than in the ionic one. The electrochemical measurements of the steel-HoPS coating showed that the biopolymer layer acts as an anodic-type corrosion inhibitor, with high resistance to corrosion by water and with chloride ions which prevent pitting, a corrosion process typical of bare steel. Few reports have cited the application of LAB HoPS as corrosive coating inhibitors. This work is the first to explore the influence of a structurally characterized dextran from Weissella cibaria strain as a potential steel corrosion inhibitor in ionic environments.
Asunto(s)
Dextranos , Weissella , Corrosión , Dextranos/química , Acero/química , Agua , Weissella/químicaRESUMEN
Homopolysaccharides (HoPS) produced by lactic acid bacteria (LAB) are highly versatile, biocompatible and safe compounds. In this work, six HoPS from different species of Weisella and Leuconostoc were identified as thermally stable dextrans, with endothermic crystalline deformations between 214 and 239 °C. These dextrans proved to have greater solubility and capacities to retain water and oil than similar polymers in other reports. Furthermore, a surface morphology study presented cubic grumps, stratify mesh with irregular grumps, and highly compact filaments. Assays in vitro revealed moderate antioxidant, browning and foaming activities as well as technological properties, such as anti-syneresis, emulsifying and flocculating activities, even at low concentrations. Taking into account bipolymers' microstructure, functionalities and performance in both, aqueous and hydrophobic matrixes, plus their capacity to maintain themselves at elevated temperatures, we consider these HoPS beneficial and natural food additives.
Asunto(s)
Aditivos Alimentarios/química , Lactobacillales/química , Polisacáridos/química , Emulsiones , Aditivos Alimentarios/metabolismo , Interacciones Hidrofóbicas e Hidrofílicas , Lactobacillales/metabolismo , Solubilidad , Agua/químicaRESUMEN
Liberibacter asiaticus is the prevalent causative pathogen of Huanglongbing or citrus greening disease, which has resulted in a devastating crisis in the citrus industry. A thorough understanding of this pathogen's physiology and mechanisms to control cell survival is critical in the identification of therapeutic targets. YbeY is a highly conserved bacterial RNase that has been implicated in multiple roles. In this study, we evaluated the biochemical characteristics of the L. asiaticus YbeY (CLIBASIA_01560) and assessed its potential as a target for antimicrobials. YbeYLas was characterized as an endoribonuclease with activity on 3' and 5' termini of 16S and 23S rRNAs, and the capacity to suppress the E. coli ΔybeY phenotype. We predicted the YbeYLas protein:ligand interface and subsequently identified a flavone compound, luteolin, as a selective inhibitor. Site-directed mutagenesis was subsequently used to identify key residues involved in the catalytic activity of YbeYLas. Further evaluation of naturally occurring flavonoids in citrus trees indicated that both flavones and flavonols had potent inhibitory effects on YbeYLas . Luteolin was subsequently examined for efficacy against L. asiaticus in Huanglongbing-infected citrus trees, where a significant reduction in L. asiaticus gene expression was observed.
Asunto(s)
Proteínas Bacterianas/antagonistas & inhibidores , Inhibidores Enzimáticos/química , Flavonoides/química , Rhizobiaceae/enzimología , Ribonucleasas/antagonistas & inhibidores , Proteínas Bacterianas/genética , Proteínas Bacterianas/metabolismo , Citrus/microbiología , Inhibidores Enzimáticos/metabolismo , Flavonoides/metabolismo , Enfermedades de las Plantas/microbiología , Rhizobiaceae/química , Rhizobiaceae/genética , Ribonucleasas/química , Ribonucleasas/genética , Ribonucleasas/metabolismoRESUMEN
The consumers' demand for food with high nutritional quality and free of chemical additives increases the need to look for new products and preservation strategies. Quinoa (Chenopodium quinoa) is an Andean pseudocereal highly appreciated because of its nutritional properties. Moreover, it is an optimal substrate for growing and production of improved amounts of antifungal compounds by Lactobacillus plantarum CRL 778. The aim of this work was to optimize a lactic ferment for packaged breads with improved nutritional value and prolonged shelf life by applying a statistical experimental design model. The addition of 30 % quinoa to the wheat semiliquid ferment (QWF) could highly improve the amino acids release (4.3 g/L) during fermentation. Moreover, this quinoa proportion was sufficient to obtain the same concentration of the antifungal compounds, phenyllactic and hydroxiphenyllactic acids (PLA and OH-PLA) as with 100 % quinoa (ca. 36 and 51 mg/L, respectively). Statistical model analysis showed that citrate and skimmed milk enhanced significantly all evaluated parameters specially PLA (ca. 71 mg/L), HO-PLA (ca. 75 mg/L), and lactate (27 g/L) with a p value <0.005. The synergic effects of higher antifungal compounds production, acid release, and pH decrease allowed lowering the amount (about 50 %) of the chemical preservative calcium propionate commonly added to bread. Moreover, these breads show increased shelf life.
Asunto(s)
Antifúngicos/metabolismo , Pan/microbiología , Chenopodium quinoa/metabolismo , Conservación de Alimentos/métodos , Lactatos/metabolismo , Lactobacillus plantarum/crecimiento & desarrollo , Lactobacillus plantarum/metabolismo , Harina , Conservantes de Alimentos/metabolismo , Concentración de Iones de Hidrógeno , Propionatos/metabolismo , Triticum/metabolismoRESUMEN
The effect of liquid (LSF) and solid state fermentation (SSF) of lentils for production of water-soluble fractions with antioxidant and antihypertensive properties was studied. LSF was performed either spontaneously (NF) or by Lactobacillus plantarum (LP) while SSF was performed by Bacillus subtilis (BS). Native lactic flora in NF adapted better than L. plantarum to fermentative broth and BS counts increased 4.0 logCFU/g up to 48 h of SSF. LSF water-soluble fractions had higher (P ≤ 0.05) free amino groups, GABA content, antioxidant and angiotensin I-converting enzyme inhibitory (ACEI) activities than SSF. In addition, GABA and ACEI activity of LSF increased in a time-dependent manner. Proteolysis by BS was limited, with slight changes in free amino groups, while GABA, total phenolic compounds and antioxidant capacity increased throughout fermentation. Higher antihypertensive potential was observed in NF (96 h) characterised by the highest GABA content (10.42 mg/g extract), ACE-inhibitory potency (expressed as IC(50)) of 0.18 mg protein/ml and antioxidant capacity of 0.26 mmol Trolox equivalents/g extract. Therefore, water-soluble fermented lentil extracts obtained by LSF are particularly promising as functional ingredients in preventing hypertension.
Asunto(s)
Antihipertensivos/metabolismo , Antioxidantes/metabolismo , Bacillus subtilis/metabolismo , Técnicas de Cultivo/métodos , Lactobacillus plantarum/metabolismo , Lens (Planta)/microbiología , Antihipertensivos/análisis , Antioxidantes/análisis , Fermentación , Lens (Planta)/química , Lens (Planta)/metabolismo , Ácido gamma-Aminobutírico/análisis , Ácido gamma-Aminobutírico/metabolismoRESUMEN
Lactic acid bacteria (LAB) isolated from soy milk were used to produce a multifunctional fermented food. Seven isolates were screened for their ability to produce peptides and free isoflavones in soy milk. The antihypertensive, antioxidant, and anti-inflammatory properties of the resulting fermented soy milks were evaluated in vitro using biochemical assays. Isolates 1-5 were found to be producers of fermented soy milk with angiotensin I converting enzyme inhibitory activity (ACEI). Isolate 3 was found to be a producer of free isoflavones that increased the antioxidant and anti-inflammatory potential of fermented soy milk. LAB isolates 2-5 were submitted to genetic profiling and a characterization scheme. These isolates were identified as Enterococcus faecium , and none of them contained virulence determinants or resistance to antibiotics. In conclusion, this study shows that the application of E. faecium isolate 3 for multifunctional food production from soy milk could be a promising strategy in the prevention therapy against cardiovascular disease.
Asunto(s)
Enterococcus faecium/metabolismo , Fermentación , Alimentos Funcionales/microbiología , Leche de Soja/química , Leche de Soja/metabolismo , Inhibidores de la Enzima Convertidora de Angiotensina , Antiinflamatorios , Antihipertensivos , Antioxidantes , Enfermedades Cardiovasculares/prevención & control , Enterococcus faecium/aislamiento & purificación , Alimentos Funcionales/análisis , Isoflavonas/biosíntesisRESUMEN
Binding of immobilized collagen-I (Cn-I) and fibronectin (Fn) by Lactobacillus acidophilus CRL 639 depends on cell-surface proteins. Capsule formation during the stationary growth phase has a negative effect on adherence of Cn-I and Fn. However, cells from the exponential growth phase, which produce no capsule, exhibit maximal binding. Binding is sensitive to trypsin, proteinase K, pronase E, and heat. Gelatin and soluble Cn-I partially inhibit binding of Cn-I although various proteins, sugars and amino acids do not affect binding to Fn. These results indicate that protein-protein interactions mediate adhesion to extracellular matrix proteins. SDS-PAGE and Western blot analyses of surface proteins revealed that several proteins including the major 43-kDa protein of the S-layer are expressed. Monoclonal antibodies showed that Fn binds to a 15-kDa protein, while Cn-I binds to proteins of 45 and 58 kDa.