Purification and characterization of a surfactant-compatible lipase from Aspergillus tamarii JGIF06 exhibiting energy-efficient removal of oil stains from polycotton fabric

Abstract

An extracellular lipase with 23,666.66 U/ml/min activity was produced by Aspergillus tamarii JGIF06 under submerged fermentation in mineral salt medium containing coconut oil (2.5 % v/v), tryptone (2 % w/v) and ammonium chloride (2 % w/v), with initial pH of 5 ± 0.2, incubated at 25 °C for 7 days on a rotary shaker at 120 rpm. A 7.9-fold increase in lipase-specific activity was recorded after purification by DEAE Sepharose ion exchange and Sephadex G200 column chromatography. The apparent molecular mass of this enzyme was revealed as 50 kDa by sodium dodecyl sulphate polyacrylamide gel electrophoresis. The optimal lipase activity was recorded at pH 4 and 37 °C. The enzyme revealed broad specificity towards different vegetable oils. The K m and V max of the lipase on olive oil was found to be 330.4 mg and 53,690 U/ml/min, respectively. The lipase activity was stable in the presence of surfactants such as cetrimonium bromide, sodium dodecyl sulphate and Tween 80, and metal ions and reagents such as Ca2+, Ba2+ and 2-mercaptoethanol. However, the activity was greatly reduced in the presence of organic solvents such as chloroform. The stain removal potential of the crude lipase was determined on polycotton fabric pieces stained with peanut oil. Lipase added to cold water alone significantly enhanced the removal of stain by 152 %. The addition of lipase also improved the stain removal efficiency of a commercially available detergent in the presence of either cold (25 ± 2 °C) or hot (65 ± 2 °C) water. The current findings suggest the potentiality of this enzyme for energy-efficient biocatalytic application.

Purification of lipase from Aspergillus fumigatus using Octyl Sepharose column chromatography and its characterization

“…In another study, lipase from Penicillum notatum showed the maximum activity at 40 °C . Purified lipase from Aspergillus careneus and Aspergillus tamari had maximum activity at 37 °C . In the stability pattern, lipase remained stable in the temperature range of 30–60 °C whereas activity was completely lost at higher temperature range from 60 to 80 °C when pre incubated for 1 h .…”

“…In a previous study, lipase from A. japonicus retained activity in the organic solvents such as chloroform, methanol, ethanol, and hexane except butanol but there was decrease in the enzyme activity when the concentration of the organic solvent increased . Whereas the activity was inhibhited hen the purified lipase from Aspergillus tamarii JGIF06 was treated with 2‐propanol, acetone, methanol, and ethanol . It was reported that the organic solvent (water miscible) shred water from the enzyme which resulted in the denaturation of the molecule at a much rapid rate than in pure water system .…”

“…6). Any drastic change in the pH of a medium leads to denaturation of the enzyme resulting in the loss of its activity [1]. In a previous study, purified lipase from both the wild and mutant strain of Rhizopus oligosporus and Microsporus had maximum activity in phosphate buffer at pH 8.0 of the reaction mixture [22].…”

“…Lipases (triacylglycerol acylhydrolases, EC 3.1.1.3) are enzymes that catalyze the hydrolysis of triacylglycerol to glycerol and free fatty acids . Lipases are the acyl hydrolases and the water soluble enzymes that play a role in fat digestion by cleaving triglycerides into polar lipids.…”

Purification and biochemical characterization of an organic solvent‐tolerant and detergent‐stable lipase from Staphylococcus capitis

“…The enzyme retained 57 and 47% of its original activity at 45 and 55°C, respectively, after incubation for 30 min. The probable reason for this decrease might be due to the disruption of the tertiary structure of lipase, which would have altered the configuration of the active site, thereby decreasing the enzyme substrate interaction …”