Partial Purification and Characterization of Lipase (EC 3.1.1.3) from Propionibacterium acnes

Ingham, Eileen; Holland, K. T.; Gowland, G.; Cunliffe, W. J.

doi:10.1099/00221287-124-2-393

Cited by 38 publications

(42 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…4). With optimum pH of 6.0, close to neutrality, it exhibited similar behavior to other propionic acid bacteria lipolytic enzymes [5,12,20,21]. Although it showed only 16% of its maximum activity at pH 4.0, it was considerably more active at alkaline pH, with 72 and 66% of its maximum activity at pH 8.0 and 9.0, respectively.…”

Section: Resultsmentioning

confidence: 89%

“…mol -1 for the intracellular P. shermanii lipase, as the enzyme extracellular lipase has been reported for P. acidipropionici [21]. In the case of P. acnes, Ingham et al [12] detected a major was eluted with the void volume on a Sephadex G-75 column, while a small molecular mass (6 000-8 000 g . mol -1 ) extracellular lipase of 46 770 g .…”

Section: Resultsmentioning

confidence: 99%

“…On the contrary, Dupuis and Boyaval [4], and Dupuis et al [5] reported extracellular or cell wall bound lipase and esterase activities for several Propionibacterium strains. Extracellular lipase has been also reported for P. acidipropionici [21], while the existence of extracellular lipases in the case of cutaneous propionic acid bacteria has been clearly confirmed [12,18].…”

Section: Effect Of Metal Ionsmentioning

confidence: 95%

See 2 more Smart Citations

Purification and characterization of an intracellular esterase from Propionibacterium freudenreichii ssp. freudenreichii ITG 14

Kakariari¹,

Georgalaki²,

Kalantzopoulos³

et al. 2000

Lait

View full text Add to dashboard Cite

-An intracellular esterase from Propionibacterium freudenreichii ssp. freudenreichii ITG 14 was purified by anion exchange and gel filtration chromatography. The enzyme had a molecular weight of 47 400 g . mol -1 as determined by gel filtration chromatography, with an optimum activity on α-naphthyl-acetate at pH 6.0 and at 65 °C, with K M = 1.2 mmol . L -1 . The esterase hydrolyzed synthetic substrates of low molecular weight (C2-C4), and among triglycerides only triacetin. Sulfhydryl group reagents and metal chelators had limited or no effect on enzyme activity; highest inhibition was observed with phenylmethylsulfonylfluoride (PMSF). Propionibacterium freudenreichii

show abstract

Section: Resultsmentioning

confidence: 89%

Section: Resultsmentioning

confidence: 99%

Section: Effect Of Metal Ionsmentioning

confidence: 95%

See 1 more Smart Citation

Purification and characterization of an intracellular esterase from Propionibacterium freudenreichii ssp. freudenreichii ITG 14

Kakariari¹,

Georgalaki²,

Kalantzopoulos³

et al. 2000

Lait

View full text Add to dashboard Cite

show abstract

“…The presence of lipase activity in liquid cultures was determined by a titrimetric assay measuring the release of oleic acid from triolein (Ingham et al, 1981). Assays were performed in duplicate and units of lipase activity were expressed as mean µmol oleic acid produced min − ".…”

Section: Methodsmentioning

confidence: 99%

Identification of a second lipase gene, gehD, in Staphylococcus epidermidis: comparison of sequence with those of other staphylococcal lipases The GenBank accession number for the nucleotide sequence determined in this work is AF090142.

et al. 2000

View full text Add to dashboard Cite

The identification and molecular characterization of a previously unidentified lipase, gehD, from the human cutaneous commensal Staphylococcus epidermidis is reported. A lipase-GehC-deficient but otherwise isogenic mutant of S. epidermidis 9 was constructed by allele replacement. However, the mutant was found to retain 50 % of the wild-type lipase activity in liquid culture. Rescreening of a genomic library revealed the presence of a second lipase gene, gehD, which was subsequently mapped and sequenced. In common with other staphylococcal lipases, GehD appeared to be translated as a 650-700 amino acid precursor which is processed post-translationally to an extracellular mature lipase of 360 amino acids with a size of approximately 45 kDa. Comparison of the amino acid sequence of GehD with those of other staphylococcal lipases revealed a high level of conservation between the mature lipase domains of different species. By hybridization studies, both gehC and gehD genes were found to be present in S. epidermidis isolates from both clinical and non-clinical backgrounds, but neither hybridized to DNA isolated from other staphylococcal strains. Construction of a phylogenetic tree and calculation of amino acid sequence homologies between mature lipases, however, suggested that the lipases of S. epidermidis may be more closely related to those of Staphylococcus aureus than to each other.

show abstract

“…Extracellular lipase activity in culture supernatant fluids was assayed by measuring the release of oleic acid from triolein using a modification of the method of Ingham et al (1981). In this procedure, a two-phase heptane/propan-2-ol/water system was used to extract long-chain free fatty acids released by enzyme activity.…”

Section: Determination Of P Acnes Cell Volume the Cell Volume Of Pmentioning

confidence: 99%

Interaction of Propionibacterium acnes with skin lipids in vitro

Gribbon

Cunliffe

Holland

1993

Journal of General Microbiology

Self Cite

136

View full text Add to dashboard Cite

Propionibacterium acnes is the predominant microbial resident within the pilosebaceous follicles of sebum-rich areas of human skin. This study investigated the effects of known hydrophobic components of sebum on the physiology and nutrition of this microorganism, grown anaerobically at 33 "C, under defined conditions using continuous culture techniques. The medium used was chemically defined, comprising eight amino acids, with glucose as the main carbon energy source, and the culture pH was maintained at 5.6. The range of sebum lipids assayed was based on the C,, monounsaturated fatty acid 9-cis-octadecenoic acid (oleic acid). Stock micronized solutions were aseptically pulsed into continuous cultures in the presence and absence of glucose, and nutritional effects monitored. None of the lipid substrates significantly affected P. acnes growth either in terms of maximum specific growth rate (jzmm) or final culture biomass yield. Glycerol (3mgml-') was found to be a poor carbonlenergy source in comparison to glucose. Bacterial cells did, however, adhere with varying degrees, to the Merent lipid species, with maximum adherence occurring with the free fatty acid. This observation was confirmed by preliminary uptake experiments using ['4C]oleic acid. The interactive site for cell adherence may be the lipid-fibrillar layer associated with the cell surface of P. acnes, as discerned in electron microscopical studies. The findings of this investigation suggest that one function of the P. acnes lipase may be to aid colonization within the pilosebaceous follicle, by promoting cell adherence to components such as oleic acid.

show abstract

Partial Purification and Characterization of Lipase (EC 3.1.1.3) from Propionibacterium acnes

Cited by 38 publications

References 29 publications

Purification and characterization of an intracellular esterase from Propionibacterium freudenreichii ssp. freudenreichii ITG 14

Purification and characterization of an intracellular esterase from Propionibacterium freudenreichii ssp. freudenreichii ITG 14

Identification of a second lipase gene, gehD, in Staphylococcus epidermidis: comparison of sequence with those of other staphylococcal lipases The GenBank accession number for the nucleotide sequence determined in this work is AF090142.

Interaction of Propionibacterium acnes with skin lipids in vitro

Contact Info

Product

Resources

About