Search results for "Lipase"

Chemoselective Removal of Protecting Groups from O-Glycosyl Amino Acid and Peptide (Methoxyethoxy)ethyl Esters Using Lipases and Papain

1996

The selective C-terminal deprotection of O-glycopeptide (methoxyethoxy)ethyl esters is achieved under mild conditions (pH 6.6, 37 degrees C) by enzymatic hydrolysis using papain or lipase M from Mucor javanicus to give building blocks useful for chain-extending glycopeptide synthesis. On the other hand, the selective removal of acetyl protecting groups from the saccharide portion of glycopeptides is accomplished by alternative enzymatic hydrolysis with lipase WG from wheat germ to furnish model substrates for enzymatic glycosyl transfer reactions in order to extend the carbohydrate side chain of these conjugates.

Enzyme-mediated enantioselective acylation of secondary amines in organic solvents

1991

Abstract Porcine pancreatic lipase (PPL) and lipase Amano P catalyze the enantioselective acylation of cyclic 1,2- and 1,3-amino alcohol derivatives in organic solvents. The enatiomeric excesses (ee′s) were shown to depend on the enzyme, reaction time, temperature and type of substrate.

ChemInform Abstract: Comparative Lipase-Catalyzed Hydrolysis of Ethylene Glycol Derived Esters. The 2-Methoxyethyl Ester as a Protective Group in Pep…

2010

ChemInform Abstract: Chemoselective Removal of Protecting Groups from O-Glycosyl Amino Acid and Peptide (Methoxyethoxy)ethyl Esters Using Lipases and…

2010

The selective C-terminal deprotection of O-glycopeptide (methoxyethoxy)ethyl esters is achieved under mild conditions (pH 6.6, 37 degrees C) by enzymatic hydrolysis using papain or lipase M from Mucor javanicus to give building blocks useful for chain-extending glycopeptide synthesis. On the other hand, the selective removal of acetyl protecting groups from the saccharide portion of glycopeptides is accomplished by alternative enzymatic hydrolysis with lipase WG from wheat germ to furnish model substrates for enzymatic glycosyl transfer reactions in order to extend the carbohydrate side chain of these conjugates.

Effects of free fatty acids, lysophosphatides and phospholipase treatment on lipid peroxidation of myocardial homogenates and membrane fractions

1987

The effects of various free fatty acids, lysophosphatides and phospholipase treatments on the enzymatic and the non-enzymatic lipid peroxidation capacities in the heart homogenates and subcellular fractions were studied. The results showed a dose related inhibition of both the enzymatic and non-enzymatic lipid peroxidation with free fatty acids. A significant inhibition occurred as early as at the concentration of 25–50 μM of several fatty acids both in homogenates and in organelle fractions. In general, the inhibition was greatest with cis-unsaturated, long-chain fatty acids. The inhibition was also induced by the pretreatment of the homogenates with phospholipase A2 but not with phospholi…

ChemInform Abstract: Dysidotronic Acid, a New and Selective Human Phospholipase A2 Inhibitor from the Sponge Dysidea sp.

2010

Abstract A new bioactive sesquiterpenoid, named dysidotronic acid 1, with a rearranged drimane skeleton has been isolated from the sponge Dysidea sp. from Vanuatu islands, along with bolinaquinone 2. The chemical structure of 1 was determined on the basis of spectroscopic data. Dysidotronic acid significantly inhibited human synovial phospholipase A2 (PLA2) at 10 μM, with an IC50 value of 2.6 μM and a higher selectivity and potency towards this enzyme than the reference inhibitor manoalide.

Dysidotronic acid, a new and selective human phospholipase A2 inhibitor from the sponge Dysidea sp.

2000

Abstract A new bioactive sesquiterpenoid, named dysidotronic acid 1, with a rearranged drimane skeleton has been isolated from the sponge Dysidea sp. from Vanuatu islands, along with bolinaquinone 2. The chemical structure of 1 was determined on the basis of spectroscopic data. Dysidotronic acid significantly inhibited human synovial phospholipase A2 (PLA2) at 10 μM, with an IC50 value of 2.6 μM and a higher selectivity and potency towards this enzyme than the reference inhibitor manoalide.

Study of a lipase from Candida rugosa Diddens and Lodder

1993

Lipasic system of Candida rugosa (CBS 613) strain was studied. The enzyme was purified in one step by hydrophobic chromatography. The properties of this lipase were determined. It is an oligomeric enzyme composed of five identical monomers of 46 kg · mol−1. Its optimum reaction conditions are pH = 7 and temperature = 40°C. This enzyme presents a rapid thermal denaturation and then a more stable form. It is a cell-bound lipase which is induced by triacyl glycerols. This enzyme presents a high specificity for external positions on glycerol. Unterschung einer Lipase aus Candida rugosa Diddens und Lodder Die Reinigung einer Lipase aus Candida rugosa (CBS 613) wurde in einer einzigen Stufe durch…

Differential behaviour of Pseudomonas sp. 42A2 LipC, a lipase showing greater versatility than its counterpart LipA

2009

Abstract Growth of Pseudomonas sp. 42A2 on oleic acid releases polymerized hydroxy-fatty acids as a result of several enzymatic conversions that could involve one or more lipases. To test this hypothesis, the lipolytic system of strain Pseudomonas sp. 42A2 was analyzed, revealing the presence of at least an intracellular carboxylesterase and a secreted lipase. Consensus primers derived from a conserved region of bacterial lipase subfamilies I.1 and I.2 allowed isolation of two secreted lipase genes, lipA and lipC, highly homologous to those of Pseudomonas aeruginosa PAO1. Homologous cloning of the isolated lipA and lipC genes was performed in Pseudomonas sp. 42A2 for LipA and LipC over-expr…

Trapping of Different Lipase Conformers in Water-Restricted Environments

1996

Based on a recently reported strategy to rationally activate lipolytic enzymes for use in nonaqueous media [Mingarro, I., et al. (1995) Proc. Natl. Acad. Sci. U.S.A. 92, 3308-3312], we compared the behavior in water-restricted environments of activated vs nonactivated forms of different lipases toward their natural substrates, triacylglycerols. To this end, nine lipases from varied origins (mammalian, fungal, and bacterial) were assayed using simple acidolyses as nonaqueous model reactions. The experimental results for several (though not all) lipases, discussed in the light of current structural and functional information, were collectively consistent with a model where, depending on the "…