title: Improved catalytic properties of Penicillium notatum lipase immobilized in nanoscale silicone polymeric films.
abstract: 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 1.19Ug-1polymers 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.
authors.affiliation: Department of Applied Chemistry, GC University, Faisalabad, Pakistan; Environmental & Material Chemistry Laboratory, Department of Chemistry, University of Agriculture, Faisalabad, Pakistan.
authors.forename: Saima
authors.initials: S
authors.lastname: Rehman
authors.affiliation: Department of Bio-products and Bio-systems Engineering, Biotechnology Institute, University of Minnesota, St Paul, MN 55108, United States.
authors.forename: Ping
authors.initials: P
authors.lastname: Wang
authors.affiliation: Environmental & Material Chemistry Laboratory, Department of Chemistry, University of Agriculture, Faisalabad, Pakistan.
authors.forename: Haq Nawaz
authors.initials: HN
authors.lastname: Bhatti
authors.affiliation: Industrial Biotechnology Laboratory, Department of Biochemistry, University of Agriculture, Faisalabad, Pakistan. Electronic address: bilaluaf@hotmail.com.
authors.forename: Muhammad
authors.initials: M
authors.lastname: Bilal
authors.affiliation: Industrial Biotechnology Laboratory, Department of Biochemistry, University of Agriculture, Faisalabad, Pakistan.
authors.forename: Muhammad
authors.initials: M
authors.lastname: Asgher
mesh_terms: D055162:Biocatalysis; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry / Q000378:metabolism; D005110:Extracellular Space / Q000201:enzymology; D006863:Hydrogen-Ion Concentration; D008049:Lipase / Q000737:chemistry* / Q000378:metabolism*; D049329:Nanostructures / Q000737:chemistry*; D010408:Penicillium chrysogenum / Q000166:cytology / Q000201:enzymology*; D011108:Polymers / Q000737:chemistry*; D012828:Silicones / Q000737:chemistry*; D013696:Temperature
chemical_list: D004800:Enzymes, Immobilized; D011108:Polymers; D012828:Silicones; D008049:Lipase
keywords: Catalytic stability; Immobilization; Lipase; Penicillium notatum; Reusability; Silicon polymers