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A column of immobilized antibodies directed against pure human pancreatic carboxylic (cholesterol) ester hydrolase was used to purify in a single step the enzyme from human pancreatic juice as well as carboxylic-ester hydrolases from other species (rat, dog). This immunoaffinity method was also used for the purification of the related bile-salt-stimulated(More)
Hydrophobins are highly tensioactive fungal proteins with a pronounced affinity for interfaces and a propensity for self-assembly. Recently, these proteins were shown to be useful in retaining different molecules on solid surfaces. This finding offers a possibility for developing new functional materials, while creating the necessity of further research at(More)
The bile-salt-stimulated lipase purified from human skim milk was modified with diisopropyl phosphofluoridate (DFP), N-ethyl-5-phenylisoxazolium-3'-sulfonate and ethoxyformic anhydride. These chemical modifications lead to the following results: (1) the inhibition of the enzyme by DFP is due to the phosphorylation of a single residue, probably a serine(More)
In the present paper, a study on the stereoselectivity of 25 lipases of animal and microbial origin towards homogeneous prochiral triglycerides is presented. All the lipases tested catalyse the hydrolysis of the chemically alike but sterically nonequivalent ester groups in trioctanoin and triolein with different degrees of stereobias, depending on the fatty(More)
Simple and reliable immobilization techniques that preserve the activity of enzymes are of interest in many technologies based on catalysis. Here, two redox enzymes, glucose oxidase from Aspergillus niger and horseradish peroxidase, were immobilized by physisorption on glassy carbon electrodes coated with Schizophyllum commune hydrophobin. Hydrophobins are(More)
In the present study, porcine pancreatic lipase, rabbit gastric lipase, and human gastric lipase stereospecificity toward enantiomeric glyceride derivatives was kinetically investigated using the monomolecular film technique. Pseudoglycerides such as enantiomeric 1(3)-alkyl-2,3(1,2)-diacyl-sn-glycerol, enantiomeric 1(3)-alkyl-2-acyl-sn-glycerol, or(More)
An enzyme-catalyzed process has been used for dioxygen monitoring. The enzymes were two different laccases (p-diphenol:dioxygen oxidoreductases), chosen as catalysts for dioxygen reduction. The laccases were immobilized in a liquid crystalline cubic phase formed with monoolein. The structures of the cubic phases, both with and without enzymes, were(More)
The stereoselectivity of dog gastric and dog pancreatic lipases was investigated both in vitro, under simulated physiological conditions, and in vivo, during the digestion of a liquid test meal. In vitro it was observed that although both lipases had a stereopreference for the sn-3 position in triglycerides, it was about three times higher in the case of(More)
In the present study, the stereoselectivity of Rhizomucor miehei lipase, lipoprotein lipase, Candida antarctica B lipase, and human gastric lipase towards racemic dicaprin spread as a monolayer at the air-water interface was investigated. For this purpose we have developed a method with which the enantiomeric excess of the residual substrate can be measured(More)