Improved catalytic properties of Penicillium notatum lipase immobilized in nanoscale silicone polymeric films

Saima Rehman, Ping Wang, Haq Nawaz Bhatti, Muhammad Bilal, Muhammad Asgher

Research output: Contribution to journalArticlepeer-review

35 Scopus citations


Lipases are one of the most proficient biocatalysts having enormous biotechnological prospective. Immobilization offers a potential solution to improve the stability and recycling characteristics of lipases. An extracellular lipase from Penicillium notatum (PNL) was immobilized in silicon polymers (SiP) through entrapment, and subsequently coated this matrix on the network of fibers in the sponges. The silicone polymers-immobilized lipase (SiP-lipase) displayed highest apparent activity and entrapment efficiency of 1.19 U g−1 polymers and 92.3%, respectively. It also exhibited greater catalytic activity in broad-working pHs and higher temperature than equivalent free-state of enzyme. Immobilization caused an improvement in thermo-stability of the lipase with an increase in energy of activation. The recycling potential of SiP-lipase was investigated. After reusing the sponge pieces for ten reaction cycles, the SiP preserved its structure without leakage of enzyme, and retained around 90% of its original activity. The SiP surface analysis was envisaged by scanning electron microscopy that further confirmed the recycling efficiency of SiP-lipase. Overall, SiP-lipase displayed a number of useful properties that make it a promising candidate for future applications in different chemical processes.

Original languageEnglish (US)
Pages (from-to)279-286
Number of pages8
JournalInternational Journal of Biological Macromolecules
StatePublished - Apr 1 2017

Bibliographical note

Publisher Copyright:
© 2017 Elsevier B.V.


  • Catalytic stability
  • Immobilization
  • Lipase
  • Penicillium notatum
  • Reusability
  • Silicon polymers


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