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1.
Microbiologyopen ; 10(2): e1183, 2021 03.
Article in English | MEDLINE | ID: mdl-33970536

ABSTRACT

In recent years, the fermented milk product kefir has been intensively studied because of its health benefits. Here, we evaluated the microbial consortia of two kefir samples, from Escarcega, Campeche, and Campeche (México). We considered a functional comparison between both samples, including fungal and bacterial inhibition; second, we applied shotgun metagenomics to assess the structure and functional diversity of the communities of microorganisms. These two samples exhibited antagonisms against bacterial and fungal pathogens. Bioactive polyketides and nonribosomal peptides were identified by LC-HRMS analysis. We also observed a high bacterial diversity and an abundance of Actinobacteria in both kefir samples, and a greater abundance of Saccharomyces species in kefir of Escarcega than in the Campeche kefir. When the prophage compositions were evaluated, the Campeche sample showed a higher diversity of prophage sequences. In Escarcega, we observed a prevalence of prophage families that infect Enterobacteria and Lactobacillus. The sequences associated with secondary metabolites, such as plipastatin, fengycin, and bacillaene, and also bacteriocins like helveticin and zoocin, were also found in different proportions, with greater diversity in the Escarcega sample. The analyses described in this work open the opportunity to understand the microbial diversity in kefir samples from two distant localities.


Subject(s)
Anti-Infective Agents/metabolism , Anti-Infective Agents/pharmacology , Bacteria/drug effects , Fungi/drug effects , Kefir/microbiology , Metagenome , Animals , Bacteria/classification , Biodiversity , Cultured Milk Products/microbiology , DNA, Bacterial , DNA, Fungal , Fermentation , Food Microbiology , Fungi/classification , Metagenomics/methods , Mexico , Microbiota , Milk/microbiology , Peptides/pharmacology , Polyketides/pharmacology , Prophages/genetics , Secondary Metabolism
2.
Article in English | MEDLINE | ID: mdl-18678934

ABSTRACT

The PyrR transcriptional regulator is widely distributed in bacteria. This RNA-binding protein is involved in the control of genes involved in pyrimidine biosynthesis, in which uridyl and guanyl nucleotides function as effectors. Here, the crystallization and preliminary X-ray diffraction analysis of two crystal forms of Bacillus halodurans PyrR are reported. One of the forms belongs to the monoclinic space group P2(1) with unit-cell parameters a = 59.7, b = 87.4, c = 72.1 A, beta = 104.4 degrees , while the other form belongs to the orthorhombic space group P22(1)2(1) with unit-cell parameters a = 72.7, b = 95.9, c = 177.1 A. Preliminary X-ray diffraction data analysis and molecular-replacement solution revealed the presence of four and six monomers per asymmetric unit; a crystallographic tetramer is formed in both forms.


Subject(s)
Bacillus/chemistry , Bacterial Proteins/chemistry , Pentosyltransferases/chemistry , Repressor Proteins/chemistry , Bacterial Proteins/genetics , Bacterial Proteins/isolation & purification , Base Sequence , Chromatography, Gel , Cloning, Molecular , Crystallography, X-Ray , DNA Primers , Electrophoresis, Polyacrylamide Gel , Models, Molecular , Pentosyltransferases/genetics , Pentosyltransferases/isolation & purification , Protein Conformation , Repressor Proteins/genetics , Repressor Proteins/isolation & purification
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