Penicillium cyclopium produces two lipases with different substrate specificities. Lipase I is predominantly active on triacylglycerols whereas lipase II hydrolyzes mono- and diacylglycerols but not triacylglycerols. In this study, we compared the kinetic properties of P. cyclopium lipases and human
Biochimica et biophysica acta, 659(2), 401-410 (1981-06-15)
Human pancreatic carboxylic ester hydrolase (EC 3.1.1.1), usually characterized by its activity on water-soluble substrates, is shown to catalyze reactions taking place at a lipid/water interface. The inhibition of tributyrin hydrolysis by 1-alcohols follows the pattern of a Langmuir adsorption
A novel strain of Rhizopus oryzae WPG secretes a noninduced lipase (ROLw) in the culture medium; purified ROLw is a protein of 29 kDa, the 45 N-terminal amino acid residues were sequenced, this sequence is very homologous to Rhizopus delemar
Lipids in health and disease, 10, 221-221 (2011-11-30)
Bacterial lipases received much attention for their substrate specificity and their ability to function in extreme environments (pH, temperature...). Many staphylococci produced lipases which were released into the culture medium. Reports of thermostable lipases from Staphylococcus sp. and active in
The better to characterize enzymes hydrolyzing carboxyl ester bonds (carboxyl ester hydrolases), we have compared the kinetic behavior of various lipases and esterases against solutions and emulsions of vinyl esters and TAG. Short-chain vinyl esters are hydrolyzed at comparable rates
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