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• W2164283307 abstract "Rhizopus cohnii lipase was immobilized by adsorption on porous chitosan polyphosphate beads. The obtained preparation, active against fatty acids esters of p-nitrophenol and against olive oil, was characterised and compared with the free enzyme. Both lipase forms displayed the highest activity at pH 8—9. The optimum activity temperature of free and immobilized lipase was 37iC and 30iC, respectively. Immobilization did not significantly change the thermal stability of lipase in comparison with the free enzyme. Both forms of the enzyme were stable at 30iC, they lost half of their activity within 45—50 min at 50iC, and at 60iC they were fully inactivated within 10 min. Affinity to p-nitrophenylpalmitate (pNPP) for both the free and immobilized lipase was identical and amounted Km=0.2 mmol/L. With the use of HPLC, enzymatic hydrolysis of olive oil by the free and immobilized lipase was compared with the chemical hydrolysis of this substrate. It was found that both forms of the enzyme were active only against emulsified substrate, and the chromatograms of products of reactions catalysed by free and immobilized lipase showed no qualitative differences. Among the products of olive oil degradation by both forms of the enzyme, fractions identified as palmitic and linoleic acids were detected, whereas oleic acid, normally generated in the largest amount after chemical hydrolysis, was not detected." @default.
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• W2164283307 date "2003-01-01" @default.
• W2164283307 modified "2023-09-27" @default.
• W2164283307 title "Properties of immobilized and free lipase from Rhizopus cohnii" @default.
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