Production and immobilization of partially purified lipase from Penicillium chrysogenum

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 immo...

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Bibliographic Details
Published in:Malaysian Journal of Microbiology 2010-12, Vol.6 (2), p.196-202
Main Authors: Shafei, M. S., Allam, R. F.
Format: Article
Language:English
Subjects:
Alginate
Immobilization
k-carrageenan
Lipase
Penicillium chrysogenum
Polyacrylamide
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Summary: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.
ISSN:2231-7538
1823-8262
2231-7538
DOI:10.21161/mjm.17609