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Purification of a Thermostable Lipase Geobacillus thermodenitrificans nr68 (Lip.nr-68) with Potential for Enzymatic Deinking

Nik Raikhan Nik Him
Bioprocess Engineering Department, Faculty of Chemical Engineering, Universiti Teknologi MARA (UiTM), 40450 Shah Alam, Selangor, Malaysia

Abstract—Lipase from Geobacillus thermodenitrificans nr68 (Lip.nr-68) has shown great enzymatic bio-deinking activity towards a laser jet printed paper with deinkability brightness test of 55%, a value that was slightly lower than the value showed by a commercial lipase from Sigma (63%). In regards of this quality, Lip.nr-68 was purified and characterized to obtain the pure biological characteristic of this catalyst. Airlift fermenter system was used with optimum parameters of 65°C, pH of 6.8, and air flow rate of 1.00 L/min and inoculum size at 7.0% (v/v) in a cultivation medium containing; glucose of 1.25% (w/v); yeast extract of 1.25% (w/v); NaCl 0.75% (w/v) and olive oil of 0.10% (v/v) for 24 hours. The extracted extracellular crude lipase was purified to homogeneity by using four-step procedures: acetone precipitation, Sephadex G-100 filtration chromatography and twice of DEAE Sefarose CL-6B anion exchange chromatography by 22.1 times with a final yield of 25%. The molecular weight of the purified enzyme was estimated to be 33.5 kDa after SDS-PAGE analysis.

Index Terms—lipase, enzymatic deinking, Geobacillus thermodenitrificans

Cite: Nik Raikhan Nik Him, "Purification of a Thermostable Lipase Geobacillus thermodenitrificans nr68 (Lip.nr-68) with Potential for Enzymatic Deinking," Journal of Life Sciences and Technologies, vol. 4, no. 2, pp. 70-74, December 2016. doi: 10.18178/jolst.4.2.70-74
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