Effect of Surfactants and Polyethylene Glycol on the Activity and Stability of a Lipase from Oilseeds of Pachira aquatica

Abstract

Lipases from oilseeds have a great potential for commercial exploration as industrial enzymes. Lipases are used mixed with surfactants in cleaning and other formulated products, and accordingly, both components must be compatible with each other. This work presents the results of the effects of anionic, cationic and nonionic surfactants, polyethylene glycol and urea on the activity and stability of a lipase extracted of oilseeds from Pachira aquatica. The enzyme was purified and the spectrophotometric assays were done using p-nitrophenyl acetate (p-NPA) as substrate pH 7.5 and 25°C. The activity was significantly enhanced by the cationic surfactant CTAB. Bile salts increased the lipase activity in the tested concentration range, whereas anionic and nonionic surfactants showed an inhibitory effect. Aqueous solutions of PEG activated the lipase and maximum activation (161%) occurred in PEG 12,000. This effect on lipase that can be due to exposition of some hydrophobic residues located in the vicinity of the active site or aggregation.

Coconut oil induced production of a surfactant-compatible lipase fromAspergillus tamariiunder submerged fermentation

“…Therefore, it may be elucidated that the lipase produced by A. tamarii is surfactant-compatible. This finding is supported by Polizelli et al [20] who observed that maximum lipase activity in Pachira aquatica was obtained in the presence of CTAB.…”

Seed lipases: sources, applications and properties - a review

“…The recently discovered Panchira aquatica lipase was studied by the researchers Polizelli et al (2008) with respect to the physical-chemical characteristics of the purified enzyme. The lipase showed maximum activity at 40ºC and pH 8.0 for an incubation period of 90 min.…”

“…The versatility of lipases in catalyzing different kinds of reactions associated with their different specificities endows these enzymes with an important and vast application potential (Gandhi, 1997;Sharma et al, 2001;Pastore et al, 2003;Enujiugha et al, 2004;Hansan et al, 2006;Parques et al, 2006;Freire and Castilho, 2008;Yesiloglu and Baskurt, 2008;Isibilar et al, 2008;Polizelli et al, 2008). Lipases are excellent alternatives for classic chemical syntheses with industrial applications, such as in foods, detergents, oleochemicals, pharmaceuticals, fine chemistry, cosmetics and fragrances, paper pulp, leather, biosensors and lipidrich wastewater treatment (Gandhi, 1997;Paques et al, 2006;Freire and Castilho, 2008).…”

Kinetics of Denaturation and Effects of Surfactants and Polyethylene Glycol on Soybean Esterase (Glycine max L) Stability

“…Lipolytic enzymes obtained from seeds such as lipases and esterases, have attracted attention as biocatalysts. These enzymes have advantages when compared to animal and microbial esterases and lipases, such as: low cost and in some cases the crude extract can be used as the source of the enzyme, such characteristics making them a great alternative to the commercial exploitation of industrial enzymes [1][2][3][4].…”

“…Some authors have also reported that PEG can enhance significantly the activity and temperature stability of lipases [1,6]. Polyethylene glycol (PEG) is a synthetic polymer with low toxicity, soluble in aqueous solution and widely used in industrial biotechnological processes [8][9][10].…”