Evaluation of a novel thermo-alkaline Staphylococcus aureus lipase for application in detergent formulations

Abstract

An extracellular lipase of a newly isolated strain ALA1 (SAL4) was purified from the optimized culture medium. The SAL4 specific activity determined at 60 °C and pH 12 by using olive oil emulsion or TC4, reached 7215 U/mg and 2484 U/mg, respectively. The 38 NH-terminal amino acid sequence of the purified enzyme starting with two extra amino acid residues (LK) was similar to known staphylococcal lipase sequences. This novel lipase maintained almost 100% and 75% of its full activity in a pH range of 4.0-12 after a 24 h incubation or after 0.5 h treatment at 70 °C, respectively. Interestingly, SAL4 displayed appreciable stability toward oxidizing agents, anionic and non-ionic surfactants in addition to its compatibility with several commercial detergents. Overall, these interesting characteristics make this new lipase promising for its application in detergent industry.

The Role of Surface Exposed Lysine in Conformational Stability and Functional Properties of Lipase from Staphylococcus Family

“…WT, mutant K325G, and K91A/K325G were able to hydrolyse a broad range of p -nitrophenyl esters, favouring the long-chain p -nitrophenyl esters (C 10 –C 16 ). Classically, a true lipase is capable of hydrolysing long chain triglyceride (C > 10) [ 49 ], which is in agreement with our results. Staphylococcal lipases are known to exhibit a wide range of substrate preferences [ 18 ].…”

“…Staphylococcal lipases are known to exhibit a wide range of substrate preferences [ 18 ]. Similar to our results, Staphylococcus aureus strain ALA1 (SAL4) lipase efficiently hydrolyses long chain triacylglycerols [ 49 ]. On the contrary, Staphylococcus aureus lipase B56, the enzyme prefers to hydrolyse short and medium chain (C 2 –C 8 ) triacylglycerols [ 50 ].…”

Production of Industrially Important Enzymes by Thermobacilli Isolated From Hot Springs of India

“…Similar pH was also documented in thermophilic Anoxybacillus flavithermus [31] as well as in psychrophilic strain of Pseudomonas proteolytica [32]. Crude lipase was found active along a wide temperature and pH range and similar range of pH was also reported in a thermo-alkaline Staphylococcus aureus by Bacha et al [33]. Maximum stability and activity in lipase production was also recorded at suboptimal culture (40 °C temperature and 5 pH) conditions which is similar to lipase from Pseudomonas gessardii [34].…”

Realm of Thermoalkaline Lipases in Bioprocess Commodities

“…However, TA lipase from G. stearothermophilus is stable in acetone (ACE), acetonitrile (MeCN), methanol (MeOH), ethanol (EtOH), propanol (PROH), hexane (HEX), heptane (HEP), and cyclohexane (CY) up to more than 85% relative activity [ 26 ]. On the other hand, lipolytic activity of the S. aureus ALA1 lipase was enhanced by diethyl ether (Et2O), whereas nearly 100% of its catalytic activity was retained in 25% (v/v) organic solvents such as ACE, benzene, MeOH, MeCN, PROH, ETOH, or toluene (TOL) [ 24 , 51 ]. Polar solvents in particular can penetrate into the active site of lipase where the unfolding of proteins occurs due to disturbances to electrostatic charge interactions, hydrophobic interactions, hydrogen bonding, van der Waals forces, and disulfide linkages [ 2 , 27 ].…”

“…TA lipases are very stable at high temperature and alkaline environment which is the optimum condition required for maximal cleaning process. Most of them are also compatible with detergents components and resistant to inhibition [ 22 , 24 , 25 , 50 ]. TA lipases are also available in their natural free form, soluble, and readily incorporated in liquid-based detergent [ 35 , 83 ].…”