Hydrolysis of Xenobiotic Fatty Acid Esters by Carboxylesterases of Human Skin

1994 ◽  
pp. 75-83
Author(s):  
Eberhard Heymann ◽  
Felicitas Noetzel ◽  
Rita Retzlaff ◽  
Gabriele Schnetgöke ◽  
Sonja Westie
Keyword(s):  
Fatty Acid ◽  
Human Skin ◽  
Fatty Acid Esters ◽  
Hydrolysis Of ◽  
Acid Esters

scholarly journals Impact of Selected Cosmetic Ingredients on Common Microorganisms of Healthy Human Skin

Cosmetics ◽  
2019 ◽  
Vol 6 (3) ◽  
pp. 45 ◽  
Author(s):  
Dorota Dobler ◽  
Thomas Schmidts ◽  
Sören Wildenhain ◽  
Ilona Seewald ◽  
Michael Merzhäuser ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Human Skin ◽  
Chain Length ◽  
Skin Diseases ◽  
Free Acid ◽  
Fatty Alcohols ◽  
Fatty Acid Esters ◽  
Bacterial Strains ◽  
Acid Esters

Human skin is a complex ecosystem and is host to a large number of microorganisms. When the bacterial ecosystem is balanced and differentiated, skin remains healthy. However, the use of cosmetics can change this balance and promote the appearance of skin diseases. The skin’s microorganisms can utilize some cosmetic components, which either promote their growth, or produce metabolites that influence the skin environment. In this study, we tested the ability of the Malassezia species and some bacterial strains to assimilate substances frequently used in dermal formulations. The growth capability of microorganisms was determined and their lipase activity was analyzed. The growth of all Malassezia spp. in the presence of free acids, free acid esters, and fatty alcohols with a fatty chain length above 12 carbon atoms was observed. No growth was observed in the presence of fatty alcohol ethers, secondary fatty alcohols, paraffin- and silicon-based substances, polymers, polyethylene glycols, quaternary ammonium salts, hydroxy fatty acid esters, or fatty acids and fatty acid esters with a fatty chain length shorter than 12 carbon atoms. The hydrolysis of esters by Malassezia lipases was detected using High Performance Thin Layer Chromatography (HPTLC). The production of free fatty acids as well as fatty alcohols was observed. The growth promotion or inhibition of bacterial strains was only found in the presence of a few ingredients. Based on these results, formulations containing microbiome inert ingredients were developed.

Hydrolysis of Fatty Acid Esters byCandida AntarcticaLipase B (Novozym 435) Dissolved in Anhydrous Triethylamine

ChemCatChem ◽  
2012 ◽  
Vol 4 (12) ◽  
pp. 2050-2054 ◽  
Author(s):  
Markus Braner ◽  
Stefan Zielonka ◽  
Julius Grzeschik ◽  
Simon Krah ◽  
Sebastian Lieb ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Esters ◽  
Novozym 435 ◽  
Hydrolysis Of ◽  
Acid Esters

Partial purification of a lipolytic enzyme from Escherichia coli

1978 ◽  
Vol 56 (5) ◽  
pp. 319-323 ◽  
Author(s):  
P. Proulx ◽  
G. Nantel ◽  
G. Baraff
Keyword(s):  
Escherichia Coli ◽  
Fatty Acid ◽  
Gel Electrophoresis ◽  
Acyl Migration ◽  
Fatty Acid Esters ◽  
Partial Purification ◽  
Lipolytic Enzyme ◽  
Phospholipase A1 ◽  
Hydrolysis Of ◽  
Acid Esters

An enzyme with phospholipase A1 activity was purified some 500-fold from Escherichia coli cell homogenates. Lipase, phospholipase A2, and lysophospholipase copurified with phospholipase A1 and the four activities displayed similar susceptibility to heat treatment. The phospholipase A and lipase activities were recovered in a single band when partially purified preparations were subjected to SDS gel electrophoresis. Phospholipase, lysophospholipase, and lipase all required Ca2+ for activity. Phosphatidylcholine, phosphatidylethanolamine, and their lyso analogues were all hydrolysed at equivalent rates and these were substantially greater than the rate of methylpalmitate or tripalmitoylglycerol hydrolyses under similar incubation conditions. Evidence for a direct but slow hydrolysis of the ester at position 2 of phosphoglyceride was obtained; however, release of fatty acid from this position is mostly indirect involving acyl migration to position 1 and subsequent release of the translocated fatty acid. Escherichia coli, therefore, appears to possess a lipolytic enzyme of broad substrate specificity acting mainly at position 1 but also at position 2 of phosphoglycerides and on triacylglycerols and methyl fatty-acid esters.

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