Paenibacillus lactis
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA52659 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| Other | ||||
| SRR24886677_1.fastq.gz | Fastqsanger.gz | |||
| SRR24886677_2.fastq.gz | Fastqsanger.gz |
Items per page: 5 1 - 3 of 3 |
Similar Datasets
Project description:Lactic acid bacterium involved in cheese and fermented food production
| PRJNA52799 | ENA
Project description:Paenibacillus lactis 154 genome sequencing project
| PRJNA50329 | ENA
Project description:Paenibacillus larvae, the causal agent of American Foulbrood disease (AFB), affects honeybee health worldwide. The present study investigates the transcriptional response of this Gram-positive, endospore-forming bacterium to bodily fluids from honeybee larvae. Four different conditions were evaluated with a loop design: sampling of in vitro grown P. larvae cultures one or four hours after addition of larval fluids or BHIT-broth (C1, T1, C4, T4).
2014-12-22 | GSE37481 | GEO
Project description:Bioremediation of a common product of food processing by a human gut bacterium
2019-08-27 | MSV000084239 | MassIVE
Project description:Purpose: Lactococcus lactis is the primary constituent of many industrial starter cultures used in food fermentations. However, this bacterium is exposed to several stressful conditions during the industrial process. L. lactis TOMSC161 has been shown to resist better to freeze-drying and storage when cells are harvested at the late stationary compared to the early stationary phase. Methods: In this work, the physiological changes that occur during growth (early and late stationary phases) were studied using transcriptomic, proteomic and cytometric approaches in order to elucidate the cell mechanisms involved in the stress tolerance of L. lactis TOMSC161 to freeze-drying and storage processes. Results: The majority of altered abundances for genes determined by transcriptomic analysis indicated a slowdown at the late stationary phase in general metabolism and in the incomplete reduction of O2 leading to reactive oxygen species (ROS), in comparison to the early stationary phase. Furthermore, the expression of genes involved in general and oxidative stress responses was over-expressed at the late stationary phase when compared to the early stationary phase, thus explaining the better resistance to freeze-drying and the storage of cells harvested after six hours of stationary phase. Superoxide anion detection was performed by flow cytometry and related to the ROS production of starters. Superoxide anion concentration was lower for cells harvested at the late stationary phase when compared to cells harvested at the early stationary phase. Conclusions: L. lactis TOMSC161 was thus able to develop an oxidative stress “pre-adaptation” during the stationary phase making it possible to better resist freeze-drying and storage stresses and especially oxidative stress.
2018-10-30 | GSE74554 | GEO
Project description:Background- The plant growth promoting rhizobacterium Paenibacillus riograndensis SBR5 is a promising candidate to serve as crop inoculant. Despite its potential regarding environmental and economic benefits, the species P. riograndensis is poorly characterized. Here, we performed for the first time a detailed transcriptome analysis of P. riograndensis SBR5 using RNAseq technology. Results- Sequence analysis of the library enriched in 5’-ends of the primary transcripts was used to identify 1,082 TSS belonging to novel transcripts and allowed us to determine a promoter consensus sequence and regulatory sequences in 5’ untranslated regions including riboswitches Conclusions- Our RNAseq analysis provides insight into the P. riograndensis SBR5 transcriptome at the systems level and will be a valuable basis for differential RNAseq analysis of this bacterium.
2017-10-25 | GSE98766 | GEO
Project description:Paenibacillus lactis CIP 108827 genome sequence
| PRJEB286 | ENA
Project description:Research backgroundCellulose is an ingredient of waste materials that can be converted to other valuable substances. This is possible provided that the polymer molecule is degraded to smaller particles and used as a carbon source by microorganisms. Because of the frequently applied methods of pretreatment of lignocellulosic materials, the cellulases derived from thermophilic microorganisms are particularly desirable.Experimental approachWe were looking for cellulolytic microorganisms able to grow at 50 °C and we described their morphological features and biochemical characteristics based on carboxymethyl cellulase (CMCase) activity and the API® ZYM system. The growth curves during incubation at 50 °C were examined using the BioLector® microbioreactor.Results and conclusionsForty bacterial strains were isolated from fermenting hay, geothermal karst spring, hot spring and geothermal pond at 50 °C. The vast majority of the bacteria were Gram-positive and rod-shaped with the maximum growth temperature of at least 50 °C. We also demonstrated a large diversity of biochemical characteristics among the microorganisms. The CMCase activity was confirmed in 27 strains. Hydrolysis capacities were significant in bacterial strains: BBLN1, BSO6, BSO10, BSO13 and BSO14, and reached 2.74, 1.62, 1.30, 1.38 and 8.02 respectively. Rapid and stable growth was observed, among others, for BBLN1, BSO10, BSO13 and BSO14. The strains fulfilled the selection conditions and were identified based on the 16S rDNA sequences. BBLN1, BSO10, BSO13 were classified as Bacillus licheniformis, whereas BSO14 as Paenibacillus lactis.Novelty and scientific contributionWe described cellulolytic activity and biochemical characteristics of many bacteria isolated from hot environments. We are also the first to report the cellulolytic activity of thermotolerant P. lactis. Described strains can be a source of new thermostable cellulases, which are extremely desirable in various branches of circular bioeconomy.
| S-EPMC8542176 | biostudies-literature
Project description:This study aimed to isolate thermostable, alkaliphilic, and detergent-tolerant amylase-producing bacteria. Pure isolates from environmental samples were screened on a starch-based medium (pH 11), and selected isolates were identified using cultural and molecular techniques. Product optimization studies were conducted, and secreted amylase was partially purified using 40% (w/v) saturation ammonium sulfate at 4 °C. The wash performance of concentrated amylase was analyzed. A novel isolate, Paenibacillus lactis OPSA3, was selected for further studies. The isolate produced amylase optimally when grown on banana peels and soybean extracts, which are agro-wastes. Optimization by Response surface Methodology resulted in a 2.1-fold increase in alkaliphilic amylase production. A 2.46-fold purification was achieved, with an enzyme activity yield of 79.53% and specific activity of 26.19 Umg-1. Wash performance analysis using the amylase supplemented with boiled commercial detergent (kiln®) showed good cleaning efficiency. The amylase has the potential for application as a component of green detergent.
| S-EPMC10388169 | biostudies-literature
Project description:Oleanane-type ginsenosides are a class of compounds with remarkable pharmacological activities. However, the lack of effective preparation methods for specific rare ginsenosides has hindered the exploration of their pharmacological properties. In this study, a novel glycoside hydrolase PlGH3 was cloned from Paenibacillus lactis 154 and heterologous expressed in Escherichia coli. Sequence analysis revealed that PlGH3 consists of 749 amino acids with a molecular weight of 89.5 kDa, exhibiting the characteristic features of the glycoside hydrolase 3 family. The enzymatic characterization results of PlGH3 showed that the optimal reaction pH and temperature was 8 and 50 °C by using p-nitrophenyl-β-D-glucopyranoside as a substrate, respectively. The Km and kcat values towards ginsenoside Ro were 79.59 ± 3.42 µM and 18.52 s-1, respectively. PlGH3 exhibits a highly specific activity on hydrolyzing the 28-O-β-D-glucopyranosyl ester bond of oleanane-type saponins. The mechanism of hydrolysis specificity was then presumably elucidated through molecular docking. Eventually, four kinds of rare oleanane-type ginsenosides (calenduloside E, pseudoginsenoside RP1, zingibroside R1, and tarasaponin VI) were successfully prepared by biotransforming total saponins extracted from Panax japonicus. This study contributes to understanding the mechanism of enzymatic hydrolysis of the GH3 family and provides a practical route for the preparation of rare oleanane-type ginsenosides through biotransformation. KEY POINTS: • The glucose at C-28 in oleanane-type saponins can be directionally hydrolyzed. • Mechanisms to interpret PlGH3 substrate specificity by molecular docking. • Case of preparation of low-sugar alternative saponins by directed hydrolysis.
| S-EPMC10995091 | biostudies-literature