2010Malaysian Journal of MicrobiologyOpen access

Production and immobilization of partially purified lipase from Penicillium chrysogenum

Mona S. Shafei, Reda F. Allam

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Abstract

An extracellular lipase from Penicillium chrysogenum produced maximal activity 225 U/mL after four days at pH 6.5.It was partially purified 4.1 fold by ammonium sulphate precipitation (70%).The enzyme was immobilized on various carriers viz.alginate, k-carrageenan and polyacrylamide gel.The immobilization yield of enzyme immobilized in kcarrageenan and polyacrylamide gel (63.41% and 48.93% respectively) was low in comparison to that immobilized with alginate (81.57%).Different concentrations of alginate were tried to study their effect on lipase production.Maximum immobilization yield was observed with 3% alginate.The optimal pH of the partially purified lipase was 7.5 and the optimum temperature was 35 ° C. At 60 ° C the immobilized enzyme retained 62.79% of its activity.Broader pH tolerance and higher heat stability could be achieved by this method.Immobilized lipase retained 72.09% relative activity after six hydrolysis cycles.

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An extracellular lipase from Penicillium chrysogenum produced maximal activity 225 U/mL after four days at pH 6.5.It was partially purified 4.1 fold by ammonium sulphate precipitation (70%).The enzyme was immobilized on various carriers viz.alginate, k-carrageenan and polyacrylamide gel.The immobilization yield of enzyme immobilized in kcarrageenan and polyacrylamide gel (63.41% and 48.93% respectively) was low in comparison to that immobilized with alginate (81.57%).Different concentrations of alginate were tried to study their effect on lipase production.Maximum immobilization yield was observed with 3% alginate.The optimal pH of the partially purified lipase was 7.5 and the optimum temperature was 35 ° C. At 60 ° C the immobilized enzyme retained 62.79% of its activity.Broader pH tolerance and higher heat stability could be achieved by this method.Immobilized lipase retained 72.09% relative activity after six hydrolysis cycles.

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Available abstract

An extracellular lipase from Penicillium chrysogenum produced maximal activity 225 U/mL after four days at pH 6.5.It was partially purified 4.1 fold by ammonium sulphate precipitation (70%).The enzyme was immobilized on various carriers viz.alginate, k-carrageenan and polyacrylamide gel.The immobilization yield of enzyme immobilized in kcarrageenan and polyacrylamide gel (63.41% and 48.93% respectively) was low in comparison to that immobilized with alginate (81.57%).Different concentrations of alginate were tried to study their effect on lipase production.Maximum immobilization yield was observed with 3% alginate.The optimal pH of the partially purified lipase was 7.5 and the optimum temperature was 35 ° C. At 60 ° C the immobilized enzyme retained 62.79% of its activity.Broader pH tolerance and higher heat stability could be achieved by this method.Immobilized lipase retained 72.09% relative activity after six hydrolysis cycles.

Key concepts: Penicillium chrysogenum, Lipase, Chemistry, Penicillium, Food science, Enzyme, Biochemistry

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