Partial Characterization of Crude Lipase from Mutant Soil Fungal Isolate

Abstract

Lipases are cluster of enzymes which cleaves oils and fats. Characterization properties of lipases have been studied in the present investigation because they play an imperative role in several industrial applications. The present lipase obtained from soil fungal strain named as EMS5%-60min exhibited optimum activity at pH 7.0 (24.90±0.25 IU/ml/min) and 37oC (20.28±0.51 IU/ml/min). In pH stability profile, the enzyme was found stable in alkaline pH range with highest activity (13.08±0.07 IU/ml/min) at pH 9.0. Lipase demonstrated considerable activity within the temperature range of 28oC to 37oC. The residual lipase activity after pre incubation for 5 h with acetone was 194.09% (27.93±0.81 IU/ml/min) as compared to 100% activity (14.39±0.21 IU/ml/min) of control. Similarly MgSO4, MnCl2, CaCl2, FeCl3, KCl and NaCl increased lipase activity by 277.48%, 195.89%, 178.04%, 177.48%, 176.02% and 110.63%, respectively as compared to control. H2O2 acted as oxidizing agent as it increased the activity from 100% (14.39±0.21 IU/ml/min) to 201.52% (29±0.35 IU/ml/min). β- mercaptoethanol drastically decline activity to 6.94% (1±0.84 IU/ml/min). Ariel (43.90%) and Patanjali (24.84%) detergents showed less inhibition on activity, therefore present lipase can be used for laundry process. The present lipase was found stable in presence of Tween-80 and xylitol. Keywords: Lipases, characterization, solvents, surfactants, EMS (ethyl methane sulfonate) Cite this Article Shreya, Arun Kumar Sharma, Vinay Sharma et al. Partial Characterization of Crude Lipase from Mutant Soil Fungal Isolate. Research & Reviews: A Journal of Microbiology and Virology . 2018; 8(3): 79–89p.