The Use of Boron Compounds for Stabilization of Lipase from Pseudomonas aeruginosa ES3 for the Detergent Industry

Abstract

This study aimed to characterize a lipase that is highly active and stable under typical washing conditions for use as a detergent ingredient by investigating the effects of various boron compounds on lipase stabilization under different conditions. In addition, the antimicrobial activity of the boron compounds used in enzyme stabilization was examined in order to obtain an effective antimicrobial detergent. A lipase-producing bacterium was isolated from kitchen wastewater samples using Rhodamine-B Agar medium and identified as Pseudomonas aeruginosa based on 16S rDNA sequence analysis. The ES3 lipase obtained from P. aeruginosa was purified, and the purified enzyme was found to have a molecular mass of 40 kDa. The enzyme showed optimal activity at pH 9.0-10.0 and 40°C and remained stable in the presence of various metal ions, surfactants and oxidizing agents. Moreover, the pH stability and thermostability of the enzyme was improved by the addition of boron compounds, which, when used as stabilizers in the incubation media, also increased the stability of the enzyme towards commercial detergents. Furthermore, the enzyme displayed properties comparable with the commercial product Lipolase Ò , which has shown excellent stability towards various commercial detergents. Finally, boron compounds used to stabilize the lipase were found to possess antimicrobial properties, suggesting that detergents incorporating these compounds will also exhibit antimicrobial activity when washing clothes and dishes. , Turkey since 2003. Her main research areas are structural biology and biomolecular NMR spectroscopy. Her current research focuses on structure-dynamics relationships in ubiquitin-like modification systems. J Surfact Deterg (2015) 18:275-285 285

Detergent Compatible Extracellular Lipase from Streptomyces cellulosae AU‐10: A Green Alternative for the Detergent Industry

“…2). The lipase maintains its activity from 30 to 50 C with the optimum temperature at around 40 C. When the temperature stability profile was taken into account, it was observed that the activity of the lipase remained more than 80% at 30, 40, and 50 C. When the optimum temperature of the studied lipase is considered, it has been observed that it is similar to the lipases previously recommended as the detergent ingredients (Boran & Ugur, 2016;Hasan et al, 2010;Sarac, Ugur, Boran, & Elgin, 2015;Saraswat, Verma, Sistla, & Bhushan, 2017). In addition, maximum activities were previously reported for extracellular lipases from Streptomyces sp.…”

“…In a study, more than 86% of the enzyme activity was detected in the existence of Ariel after 1 h incubation (Rajanikanth & Damodharam, ). In another study, Lipolase® and P. aeruginosa ES3 lipase retained 100% of their activities against Omo, Ariel, and Pril (Sarac et al, ). In the presence of Omo and Pril, the B. multivorans SB6 lipase retained 40.6% and 100% of its activity, respectively (Boran & Ugur, ).…”

“…Previously, the stability of lipase from several microorganisms in commercial detergents was reported (Boran & Ugur, ; Rathi et al, ; Sarac et al, ). The alkaline lipase from S. fungicidicus RPBS‐A4 was also stable in the presence of commercial detergents.…”

“…Similarly, Pseudomonas aeruginosa ES3 lipase retained more than 125% residual activity in the availability of 5 mM PM and BA. In addition, the lipase activity was enhanced to 131% and 140% by SM and ST, respectively, at 20 mM concentration (Sarac et al, ). In a study using BA as the enzyme stabilizer, Lipolase® showed excellent stability at 35 °C (Lenoir, ).…”

Burkholderia multivorans SB6 Lipase as a Detergent Ingredient: Characterization and Stabilization

“…Lipase-produced bacterial isolates were collected from kitchen wastewater samples using Rhodamine B agar medium [14], and their stability towards detergent was previously determined [15] using Rhodamine B agar medium containing a commercial detergent [16]. Lipase activity of isolates was assessed by inoculating nutrient broth (NB) with 2 % inoculum from an overnight culture that was then incubated for 24 h at 30°C and 130 rpm.…”