@article{scholars10721, title = {Immobilisation of candida rugosa lipase on aminated polyethylene/polypropylene microfibrous sheet modified with oxirane group}, number = {3}, note = {cited By 0}, volume = {11}, publisher = {Akademi Sains Malaysia}, journal = {ASM Science Journal}, pages = {182--200}, year = {2018}, author = {Tajudin, H. A. and Alkhatib, M. F. and Mirghani, M. E. S. and Salleh, H. M. and Nasef, M. M.}, issn = {18236782}, url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85058668989&partnerID=40&md5=53da31aaa3f6eba746023223fd6e2c83}, abstract = {An active microfibrous substrate containing aminated brush obtained by radiation-induced grafting of glycidyl methacrylate (GMA) onto a polyethylene/polypropylene (PE/PP) micro fibrous sheet followed by amination reaction was prepared and used for immobilisation of Candida rugosa lipase under various conditions. The aminated microfibrous sheet was characterised by Fourier-transform infrared spectroscopy (FTIR-ATR) and field emission scanning electron microscope (FESEM). The amine group density on the aminated microfi- brous sheet was found to be 3.33mmol/g. Response surface methodology (RSM) was applied to model and optimise the immobilisation conditions including immobilisation time (2-6 h), medium pH (pH 7-9) and enzyme/support ratio (5.0-9.0mg/cm2). The model generated from RSM was significantly correlated with the studied parameters for the residual activity of the immobilised lipase. The optimum values for immobilisation time, medium pH, and enzyme/support ratio were found to be 4.24h, pH 8, and 8.51mg/cm2 respectively. The enzymatic activity using p-nitrophenyl palmitate (pNPP) as substrate was 1.4588U/cm2 under optimum conditions. The pH endurance, storage, and thermal stability of the immobilised lipase were remarkably enhanced. The immobilised lipase can be readily recovered and more than 50 of its activity was retained following 10 cycles. The results of this study suggested that the aminated microfibrous sheet of PE/PP grafted with poly(GMA) is a promising polymer support for enzyme immobilisation with high potential for broad biocatalytic applications. {\^A}{\copyright} 2018 Akademi Sains Malaysia.} }