Exemplar Abstract for Propionibacterium freudenreichii shermanii (van Niel 1928) Moore and Holdeman 1970 (Approved Lists 1980).

2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
Dorothea Taylor ◽  
George M Garrity
Keyword(s):  
Propionibacterium Freudenreichii

scholarly journals Identification of the Propionicin F Bacteriocin Immunity Gene (pcfI) and Development of a Food-Grade Cloning System for Propionibacterium freudenreichii

2007 ◽  
Vol 73 (23) ◽  
pp. 7542-7547 ◽  
Author(s):  
Dag Anders Brede ◽  
Sheba Lothe ◽  
Zhian Salehian ◽  
Therese Faye ◽  
Ingolf F. Nes
Keyword(s):  
Selection Marker ◽  
Multiple Cloning Site ◽  
Propionibacterium Freudenreichii ◽  
Expression Plasmid ◽  
Physiochemical Properties ◽  
Food Grade ◽  
Cloning System ◽  
Immunity Gene ◽  
Membrane Bound ◽  
High Level

ABSTRACT This report describes the first functional analysis of a bacteriocin immunity gene from Propionibacterium freudenreichii and its use as a selection marker for food-grade cloning. Cloning of the pcfI gene (previously orf5 [located as part of the pcfABC propionicin F operon]) rendered the sensitive host 1,000-fold more tolerant to the propionicin F bacteriocin. The physiochemical properties of the 127-residue large PcfI protein resemble those of membrane-bound immunity proteins from bacteriocin systems found in lactic acid bacteria. The high level of immunity conferred by pcfI allowed its use as a selection marker for plasmid transformation in P. freudenreichii. Electroporation of P. freudenreichii IFO12426 by use of the pcfI expression plasmid pSL102 and propionicin F selection (200 bacteriocin units/ml) yielded 107 transformants/μg DNA. The 2.7-kb P. freudenreichii food-grade cloning vector pSL104 consists of the pLME108 replicon, a multiple cloning site, and pcfI expressed from the constitutive PpampS promoter for selection. The pSL104 vector efficiently facilitated cloning of the propionicin T1 bacteriocin in P. freudenreichii. High-level propionicin T1 production (640 BU/ml) was obtained with the IFO12426 strain, and the food-grade propionicin T1 expression plasmid pSL106 was maintained by ∼91% of the cells over 25 generations in the absence of selection. To the best of our knowledge this is the first report of an efficient cloning system that facilitates the generation of food-grade recombinant P. freudenreichii strains.

scholarly journals Metabolic profiling analysis of the vitamin B 12 producer Propionibacterium freudenreichii

2021 ◽  
Vol 10 (3) ◽  
Author(s):  
Jiao Liu ◽  
Yongfei Liu ◽  
Jie Wu ◽  
Huan Fang ◽  
Zhaoxia Jin ◽  
...  
Keyword(s):  
Metabolic Profiling ◽  
Vitamin B ◽  
Propionibacterium Freudenreichii ◽  
Metabolic Profiling Analysis ◽  
Vitamin B 12 ◽  
Profiling Analysis

scholarly journals Probiotic Propionibacterium freudenreichii MJ2 Enhances Osteoblast Differentiation and Mineralization by Increasing the OPG/RANKL Ratio

2021 ◽  
Vol 9 (4) ◽  
pp. 673
Author(s):  
Jiah Yeom ◽  
Seongho Ma ◽  
Young-Hee Lim
Keyword(s):  
Signaling Pathway ◽  
Osteoblast Differentiation ◽  
Surface Proteins ◽  
Bone Morphogenetic Protein 2 ◽  
Ovariectomized Rats ◽  
Osteoblastic Cell ◽  
Enhancement Effect ◽  
Propionibacterium Freudenreichii ◽  
Alizarin Red ◽  
Osteoblastic Cell Line

Osteoblast differentiation is important for the development of bone and the maintenance of bone density. Propionibacterium freudenreichii is a probiotic with an anti-inflammatory property. The aim of this study was to investigate the enhancement effect of P. freudenreichii MJ2 (MJ2) isolated from raw milk on osteoblast differentiation, mineralization, and its signaling pathway. For in vitro and in vivo experiments, human fetal osteoblastic cell line hFOB 1.19 and an ovariectomized rat model were used, respectively. Expression levels of genes and proteins related to osteoblast differentiation and mineralization were measured by real-time polymerase chain reaction (qPCR) and Western blotting, respectively. Alizarin red S staining was performed to measure osteoblast mineralization. Heat-killed MJ2 (hkMJ2)-treated cells showed significantly increased osteoblast differentiation via an increase in the osteoprotegerin (OPG)/receptor activator of nuclear factor-κB ligand (RANKL) ratio and significantly increased osteoblast mineralization by stimulating the expression of bone morphogenetic protein 2 and runt-related transcription factor 2. Additionally, oral administration of live or heat-killed MJ2 to ovariectomized rats inhibited osteoporosis-induced bone loss. Specifically, surface proteins isolated from MJ2 promoted osteoblast differentiation and mineralization. In conclusion, MJ2 enhanced osteoblast differentiation and mineralization through the OPG/RANKL signaling pathway and the effective component of MJ2 might be its surface proteins.

Inhibition of Induced Mutagenesis in Salmonella typhimurium by the Protein of Propionibacterium freudenreichii subsp. shermanii

Anaerobe ◽  
2001 ◽  
Vol 7 (1) ◽  
pp. 37-44 ◽  
Author(s):  
Lena I. Vorobjeva ◽  
Olga V. Iljasova ◽  
Evgeni Yu. Khodjaev ◽  
Galina M. Ponomareva ◽  
Svetlana Yu. Varioukhina
Keyword(s):  
Salmonella Typhimurium ◽  
Propionibacterium Freudenreichii ◽  
Induced Mutagenesis

Reduction of linoleic acid inhibition in production of conjugated linoleic acid byPropionibacterium freudenreichiissp.shermanii

2001 ◽  
Vol 47 (8) ◽  
pp. 735-740 ◽  
Author(s):  
A Rainio ◽  
M Vahvaselkä ◽  
T Suomalainen ◽  
S Laakso
Keyword(s):  
Linoleic Acid ◽  
Conjugated Linoleic Acid ◽  
Inhibitory Effect ◽  
Propionibacterium Freudenreichii ◽  
Growth Inhibitory Effect ◽  
Sorbitan Monooleate ◽  
Whey Permeate ◽  
Growth Inhibitory ◽  
De Man ◽  
Sufficient Concentration

A method for the production of conjugated linoleic acid (CLA) from linoleic acid (LA) using growing cultures of Propionibacterium freudenreichii ssp. shermanii JS was developed. The growth inhibitory effect of LA was eliminated by dispersing it in a sufficient concentration of polyoxyethylene sorbitan monooleate detergent. For the whey permeate medium used, the optimum LA:detergent ratio was 1:15 (w/w). As a result, the cultures tolerated at least 1000 µg·mL–1LA, which was converted to CLA with 57%–87% efficiency. The cis-9, trans-11 and trans-9, cis-11 isomers constituted 85%–90% of the CLA produced. The feasibility of the method was demonstrated also in de Man – Rogosa–Sharpe (MRS) broth.Key words: conjugated linoleic acid, linoleic acid, Propionibacterium freudenreichii ssp. shermanii.

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