Effects of polyelectrolyte complex micelles and their components on the enzymatic activity of lipase

Saskia Lindhoud, W Norde, M A C Stuart

Research output: Contribution to journalArticle

28 Citations (Scopus)

Abstract

The enzymatic activity of Hi-lipase embedded in complexes of poly-2-methylvinylpyridinium-co-poly(ethylene oxide) (P2MVP(41)-PEG(205)) and poly(acrylic acid)(PAA(139)) is studied as a function of the PAA(139) + P2MVP(41) - PEO205 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) - PEO205 is more active than lipase without this additive.
Original languageEnglish
Pages (from-to)9802-9808
Number of pages7
JournalLangmuir
Volume26
Issue number12
DOIs
Publication statusPublished - 15 Jun 2010

Fingerprint

Lipases
Micelles
Polyelectrolytes
Lipase
micelles
carbopol 940
Ionic strength
Polyethylene oxides
Polyethylene glycols
Acrylics
acrylic acid
ethylene oxide
Acids
Substrates
Chemical analysis

Cite this

Effects of polyelectrolyte complex micelles and their components on the enzymatic activity of lipase. / Lindhoud, Saskia; Norde, W; Stuart, M A C.

In: Langmuir, Vol. 26, No. 12, 15.06.2010, p. 9802-9808.

Research output: Contribution to journalArticle

Lindhoud, Saskia ; Norde, W ; Stuart, M A C. / Effects of polyelectrolyte complex micelles and their components on the enzymatic activity of lipase. In: Langmuir. 2010 ; Vol. 26, No. 12. pp. 9802-9808.
@article{2f08fc74c46e46aa9dc1c0c2dc21aaf4,
title = "Effects of polyelectrolyte complex micelles and their components on the enzymatic activity of lipase",
abstract = "The enzymatic activity of Hi-lipase embedded in complexes of poly-2-methylvinylpyridinium-co-poly(ethylene oxide) (P2MVP(41)-PEG(205)) and poly(acrylic acid)(PAA(139)) is studied as a function of the PAA(139) + P2MVP(41) - PEO205 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) - PEO205 is more active than lipase without this additive.",
author = "Saskia Lindhoud and W Norde and Stuart, {M A C}",
year = "2010",
month = "6",
day = "15",
doi = "10.1021/la1000705",
language = "English",
volume = "26",
pages = "9802--9808",
journal = "Langmuir",
issn = "0743-7463",
publisher = "American Chemical Society",
number = "12",

}

TY - JOUR

T1 - Effects of polyelectrolyte complex micelles and their components on the enzymatic activity of lipase

AU - Lindhoud, Saskia

AU - Norde, W

AU - Stuart, M A C

PY - 2010/6/15

Y1 - 2010/6/15

N2 - The enzymatic activity of Hi-lipase embedded in complexes of poly-2-methylvinylpyridinium-co-poly(ethylene oxide) (P2MVP(41)-PEG(205)) and poly(acrylic acid)(PAA(139)) is studied as a function of the PAA(139) + P2MVP(41) - PEO205 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) - PEO205 is more active than lipase without this additive.

AB - The enzymatic activity of Hi-lipase embedded in complexes of poly-2-methylvinylpyridinium-co-poly(ethylene oxide) (P2MVP(41)-PEG(205)) and poly(acrylic acid)(PAA(139)) is studied as a function of the PAA(139) + P2MVP(41) - PEO205 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) - PEO205 is more active than lipase without this additive.

UR - http://www.scopus.com/inward/record.url?scp=77956075422&partnerID=8YFLogxK

UR - http://dx.doi.org/10.1021/la1000705

U2 - 10.1021/la1000705

DO - 10.1021/la1000705

M3 - Article

VL - 26

SP - 9802

EP - 9808

JO - Langmuir

JF - Langmuir

SN - 0743-7463

IS - 12

ER -