Archives of biochemistry and biophysics, 451(2), 149-159 (2006-06-20)
Chicken pancreatic lipase (CPL) was purified from delipidated pancreas. Pure CPL was obtained after ammonium sulphate fractionation, then DEAE-cellulose, Sephacryl S-200 gel filtration, and FPLC Mono-Q Sepharose columns. The pure lipase is a glycosylated monomer having a molecular mass of
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
Biochimica et biophysica acta, 1534(1), 34-44 (2001-12-26)
We have studied the enzymatic hydrolysis of solutions and emulsions of vinyl propionate, vinyl butyrate and tripropionin by lipases of various origin and specificity. Kinetic studies of the hydrolysis of short-chain substrates by microbial triacylglycerol lipases from Rhizopus oryzae, Mucor
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
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