Effect of ethyleneoxide groups of anionic surfactants on lipase activity

Abstract

The use of enzymes in laundry and dish detergent products is growing. Such tendency implies dedicated studies to understand surfactant-enzyme interactions. The interactions between surfactants and enzymes and their impact on the catalytic efficiency represent a central problem and were here evaluated using circular dichroism, dynamic light scattering, and enzyme activity determinations. This work focuses on this key issue by evaluating the role of the ethyleneoxide (EO) groups of anionic surfactants on the structure and activity of a commercial lipase, and by focusing on the protein/surfactant interactions at a molecular level. The conformational changes and enzymatic activity of the protein were evaluated in the presence of sodium dodecyl sulfate (SDS also denoted as SLE S) and of sodium lauryl ether sulfate with two EO units (SLE S). The results strongly suggest that the presence of EO units in the surfactant polar headgroup determines the stability and the activity of the enzyme. While SDS promotes enzyme denaturation and consequent loss of activity, SLE S preserves the enzyme structure and activity. The data further highlights that the electrostatic interactions among the protein groups are changed by the presence of the adsorbed anionic surfactants being such absorption mainly driven by hydrophobic interactions. © 2016 American Institute of Chemical Engineers Biotechnol. Prog., 32:1276-1282, 2016.

Decellularized liver transplant could be recellularized in rat partial hepatectomy model

“…Hence, the lower molecular size of SDS makes it harsh and strong, and increasing its absorption and distribution into lipid bilayers of the cell membrane results in its solubilizing and destruction (Lichtenberg, Ahyayauch, & Goñi, ). Lower surface activity is another reason that makes SLES less irritant because of reduced critical micelle concentration (CMC) that refers to the EO units (Magalhães et al, ). Moreover, water solubility of SLES due to longer polar headgroup is more than SDS (Kronberg, Holmberg, & Lindman, ), which causes SLES to pass easier throughout the blood vessel networks with lesser harm to ECM component.…”

Phospholipase D encapsulated into metal-surfactant nanocapsules for enhancing biocatalysis in a two-phase system

“…This is because the metal ions acted as an activator and could enhance the activity of the enzyme 26 while NaDC as the surfactant could also promote enzyme activity. 27 Encapsulated PLD in MSNCs formed from Ca 2+ displayed the highest specic enzyme activity of 10.51 U g À1 protein with PC as a substrate for the biosynthesis of PS, displaying 133.6% of the enzyme activity of free PLD (7.87 U g À1 protein); this was higher than the activities of PLD@MSNC prepared using other divalent metal ions. The amount of encapsulated PLD in PLD@MSNC was 85 mg g À1 .…”

Recent advances on sources and industrial applications of lipases

“…Generally, the chelating agents in commercial detergents leads to enzyme inactivation, however in case of lipase from B. licheniformis , the addition of calcium chloride to the enzyme‐detergent complex, helped in restoring the activity . Similarly, from one of the recent studies on anionic surfactants, it is noted that the stability and activity of lipase was retained in the presence of sodium lauryl ether sulfate with two ethylene oxide units . Lipases form a crucial functional compound in the formulation of detergents and about 32% of the total lipases produced have been used in the detergent industry .…”