Mucin- and carbohydrate-stimulated adhesion and subproteome changes of the probiotic bacterium Lactobacillus acidophilus NCFM

2017 ◽  
Vol 163 ◽  
pp. 102-110 ◽  
Author(s):  
Hasan Ufuk Celebioglu ◽  
Sita Vaag Olesen ◽  
Kennie Prehn ◽  
Sampo J. Lahtinen ◽  
Susanne Brix ◽  
...  
Keyword(s):  
Lactobacillus Acidophilus ◽  
Probiotic Bacterium ◽  
Lactobacillus Acidophilus Ncfm

Viability of Lactobacillus acidophilus NCFM Howaru Dophilus during storage at refrigeration temperatures

2015 ◽  
Vol 8 (1) ◽  
pp. 17-21 ◽  
Author(s):  
Tatiana Mančušková ◽  
Alžbeta Medved’ová ◽  
Ľubomír Valík
Keyword(s):  
Lactobacillus Acidophilus ◽  
Average Rate ◽  
Probiotic Bacterium ◽  
Positive Health ◽  
Stable Temperature ◽  
Viable Cells ◽  
The Media ◽  
Lactobacillus Acidophilus Ncfm ◽  
Unstable Temperature ◽  
Mrs Broth

Abstract A strain Lactobacillus acidophilus NCFM Howaru Dophilus is a probiotic bacterium available in dairy products and dietary supplements since 1970s. Its positive health effects have been proved by many studies. This work deals with the examination of NCFM strain’s viability during its storage at stable and unstable temperature in MRS broth and ultra-pasteurized milk. In nutritionally rich environment, Lb. acidophilus NCFM was able to survive and to metabolize the media. The relevant decrease of viable cells was observed in MRS broth about 30 days after inoculation, and in milk after 21 to 45 days at both stable and unstable temperatures, respectively. The average rate of decrease of viable cells was approximately two to three times higher in experiments at unstable temperature (GrMRS,unst = −0.149 log CFU.ml−1.d−1 in MRS broth, Grmilk,unst = 0.030 log CFU.ml−1.d−1 in milk) compared with that at stable temperature (GrMRS,st = −0.079 log CFU.ml−1.d−1 in MRS broth, Grmilk,st = 0.009 log CFU.ml−1.d−1 in milk). In the MRS broth exhausted by overnight cultivation of NCFM strain the decrease of viable cells started practically immediately (Grovernigh,unst = −0.137 log CFU.ml−1.d−1). Maintenance of the culture in milk at stable temperature was proved to be the most appropriate form of its storage.

scholarly journals An NAD+–dependent sirtuin depropionylase and deacetylase (Sir2La) from the probiotic bacterium Lactobacillus acidophilus NCFM

2018 ◽  
Author(s):  
Sita V. Olesen ◽  
Nima Rajabi ◽  
Birte Svensson ◽  
Christian A. Olsen ◽  
Andreas S. Madsen
Keyword(s):  
Lactobacillus Acidophilus ◽  
Probiotic Bacterium ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Steady State Kinetics ◽  
Chain Acyl ◽  
Bona Fide ◽  
Lactobacillus Acidophilus Ncfm ◽  
Hydrolysis Of

ABSTRACTSirtuins—a group of NAD+-dependent deacylases—have emerged as key in the connection between NAD+ metabolism and aging. This class of enzymes hydrolyze a range of ε-N-acyllysine PTMs and determining the repertoire of catalyzed deacylation reactions is of high importance to fully elucidate the roles of a given sirtuin. Here we have identified and produced two potential sirtuins from the probiotic bacterium Lactobacillus acidophilus NCFM and screening more than 80 different substrates, covering 26 acyl groups on five peptide scaffolds, showed that one of the investigated proteins—Sir2La—is a bona fide NAD+-dependent sirtuin, catalyzing hydrolysis of acetyl‐, propionyl‐, and butyryllysine. Further substantiating the identity as a sirtuin, known sirtuin inhibitors nicotinamide and suramin as well as a thioacetyllysine compound inhibit the deacylase activity in a concentration-dependent manner. Based on steady-state kinetics Sir2La showed a slight preference for propionyllysine over acetyllysine and butyryllysine, driven both by KM (14 μM vs 21 μM and 15 μM) and kcat (4.4·10−3 s−1vs 2.5·10−3 s−1 and 1.21·10−3 s−1). Moreover, while NAD+ is a prerequisite for Sir2La-mediated deacylation, Sir2La has very high KM for NAD+ compared to the expected levels of the dinucleotide in L. acidophilus. Sir2La is the first sirtuin from Lactobacillales and of the Gram-positive bacterial subclass of sirtuins to be functionally characterized. The ability to hydrolyze propionyl‐ and butyryllysine emphasizes the relevance of further exploring the role of other short-chain acyl moieties as PTMs.

scholarly journals An NAD+-Dependent Sirtuin Depropionylase and Deacetylase (Sir2La) from the Probiotic Bacterium Lactobacillus acidophilus NCFM

Biochemistry ◽  
2018 ◽  
Vol 57 (26) ◽  
pp. 3903-3915 ◽  
Author(s):  
Sita V. Olesen ◽  
Nima Rajabi ◽  
Birte Svensson ◽  
Christian A. Olsen ◽  
Andreas S. Madsen
Keyword(s):  
Lactobacillus Acidophilus ◽  
Probiotic Bacterium ◽  
Lactobacillus Acidophilus Ncfm

scholarly journals The In Vitro Adsorption Ability of Lactobacillus acidophilus NCFM to Benzo(a)pyrene in PM2.5

2021 ◽  
Vol 2021 ◽  
pp. 1-9
Author(s):  
Lili Fu ◽  
Yan Ning ◽  
Hongfei Zhao ◽  
Junfeng Fan ◽  
Bolin Zhang
Keyword(s):  
Lactobacillus Acidophilus ◽  
Cell Concentration ◽  
Probiotic Bacterium ◽  
Organic System ◽  
Inorganic Systems ◽  
A Cell ◽  
Lactobacillus Acidophilus Ncfm ◽  
Binding Percentage

The objective of this work was to explore the ability of lactic acid bacteria strains to bind benzo(a)pyrene (B(a)P) existing in PM2.5. In this study, we examined the ability of Lactobacillus acidophilus NCFM to bind B(a)P in the simulated PM2.5 environment. Among the tested 5 strains, Lactobacillus acidophilus NCFM exhibited the best capacity to bind B(a)P, and its B(a)P binding percentage was 60.00%. Simulations of organic and inorganic systems which represent PM2.5 indicated that B(a)P could be absorbed by strain L. acidophilus NCFM. For the inorganic system of pH 5, L. acidophilus NCFM bound 92.74% B(a)P with a cell concentration of 1 × 1010 cfu/mL at 37°C for 8 hr. Regarding the organic system with pH 6, 73.00% B(a)P was bound by strain L. acidophilus NCFM after this bacterium was incubated at 37°C for 10 min. A quick B(a)P binding by this probiotic bacterium took place in the organic system. The removal of B(a)P from PM2.5 was significantly related to incubation time, cultivation temperature, pH, and cell concentration. Thus, our finding shows that long-term consumption of L. acidophilus NCFM is beneficial for the reduction of B(a)P towards the population who are exposed to PM2.5, although the ability of this bacterium to adsorb B(a)P is partly affected by the differences in the origin of PM2.5.

scholarly journals Microarray Analysis of a Two-Component Regulatory System Involved in Acid Resistance and Proteolytic Activity in Lactobacillus acidophilus

2005 ◽  
Vol 71 (10) ◽  
pp. 5794-5804 ◽  
Author(s):  
M. Andrea Azcarate-Peril ◽  
Olivia McAuliffe ◽  
Eric Altermann ◽  
Sonja Lick ◽  
W. Michael Russell ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Proteolytic Activity ◽  
Lactobacillus Acidophilus ◽  
Regulatory System ◽  
Probiotic Bacterium ◽  
Transport Systems ◽  
Logarithmic Phase ◽  
Histidine Protein Kinase ◽  
Regulatory Systems ◽  
Two Component

ABSTRACT Two-component regulatory systems are one primary mechanism for environmental sensing and signal transduction. Annotation of the complete genome sequence of the probiotic bacterium Lactobacillus acidophilus NCFM revealed nine two-component regulatory systems. In this study, the histidine protein kinase of a two-component regulatory system (LBA1524HPK-LBA1525RR), similar to the acid-related system lisRK from Listeria monocytogenes (P. D. Cotter et al., J. Bacteriol. 181:6840-6843, 1999), was insertionally inactivated. A whole-genome microarray containing 97.4% of the annotated genes of L. acidophilus was used to compare genome-wide patterns of transcription at various pHs between the control and the histidine protein kinase mutant. The expression pattern of approximately 80 genes was affected by the LBA1524HPK mutation. Putative LBA1525RR target loci included two oligopeptide-transport systems present in the L. acidophilus genome, other components of the proteolytic system, and a LuxS homolog, suspected of participating in synthesis of the AI-2 signaling compound. The mutant exhibited lower tolerance to acid and ethanol in logarithmic-phase cells and poor acidification rates in milk. Supplementation of milk with Casamino Acids essentially restored the acid-producing ability of the mutant, providing additional evidence for a role of this two component system in regulating proteolytic activity in L. acidophilus.

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