Effects of polyelectrolyte complex micelles and their components on the enzymatic activity of lipase.
The enzymatic activity of Hl-lipase embedded in complexes of poly-2-methylvinylpyridinium-co-poly(ethylene oxide) (P2MVP(41)-PEO(205)) and poly(acrylic acid)(PAA(139)) is studied as a function of the PAA(139) + P2MVP(41)-PEO(205) complex composition. The measurements revealed that there are several factors that influence the enzymatic activity. When incorporated in micelles, the activity of lipase is increased, which suggests that the micelles favor the active state. The activity may further increase because the substrate tends to accumulate to the micelles. It is found that the presence of PAA(139) alone also increases the enzymatic activity somewhat. Increasing of the ionic strength decreases the enzymatic activity in all systems. However, at ionic strengths where the micelles are disintegrated (>0.5 M), the activity of lipase in the presence of both polyelectrolytes is still higher than the activity of free lipase. At 0.7 M NaCl it was found that lipase in the presence of (just) P2MVP(41)-PEO(205) is more active than lipase without this additive.
Lindhoud
Saskia
S
Laboratory of Physical Chemistry and Colloid Science, Wageningen University, Dreijenplein 6, 6703 HB Wageningen, The Netherlands. saskia.lindhoud@gmail.com
Norde
Willem
W
Cohen Stuart
Martien A
MA
D000180:Acrylic Resins; D004573:Electrolytes; D008049:Lipase / Q000378:metabolism*; D008823:Micelles; D009994:Osmolar Concentration; D011092:Polyethylene Glycols; D011108:Polymers / Q000737:chemistry*; D014753:Vinyl Compounds
D000180:Acrylic Resins; D004573:Electrolytes; D008823:Micelles; D011108:Polymers; D014753:Vinyl Compounds; C523649:poly(N-methyl-2-vinyl pyridinium iodide)-b-poly(ethylene oxide); D011092:Polyethylene Glycols; C006903:carbopol 940; D008049:Lipase