Partial Characterization of Crude Lipase from Mutant Soil Fungal Isolate

Shreya .; Arun Kumar Sharma; Vinay Sharma; Jyoti Saxena

doi:10.37591/rrjomv.v8i3.334

Abstract

Lipases are cluster of enzymes which cleaves oils and fats. Characterization properties oflipases have been studied in the present investigation because they play an imperative role inseveral industrial applications. The present lipase obtained from soil fungal strain named asEMS5%-60min exhibited optimum activity at pH 7.0 (24.90±0.25 IU/ml/min) and 37ºC (20.28±0.51IU/ml/min). In pH stability profile, the enzyme was found stable in alkaline pH range withhighest activity (13.08±0.07 IU/ml/min) at pH 9.0. Lipase demonstrated considerable activitywithin the temperature range of 28ºC to 37ºC. The residual lipase activity after pre incubationfor 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 NaClincreased 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 activityfrom 100% (14.39±0.21 IU/ml/min) to 201.52% (29±0.35 IU/ml/min). β- mercaptoethanoldrastically 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 forlaundry 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 ArticleShreya, 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.