Lipase catalysis on monolayers at the air/water interface. 2. Diffusion-controlled kinetics on quasi-two-dimension

Keiji Tanaka, Steven P. Mecca, Hyuk Yu

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Homogeneous exoplasmic leaflets of biomembrane are mimicked by lipid monolayers at the air/water interface. The reaction rates of lipase (Pseudomonas cepacia) catalyzed hydrolysis of a substrate (umbelliferone stearate) on L-α-dilauroylphosphatidylcholine/cholesterol mixed monolayers at the air/water interface are examined as a function of cholesterol composition, which is to vary the dynamics of the system. Lateral mobility as a measure of dynamics of phospholipids and adsorbed lipase molecules are probed with the technique of fluorescence recovery after photobleaching. Upon correlating the lateral diffusion coefficients of a probe lipid and lipase with the interfacial hydrolysis kinetics, we show for the first time that the catalytic reactions on the monolayers are diffusion-controlled. Moreover, our results are in a quantitative agreement with the two-dimensional reaction dynamics theory of Torney and McConnell.

Original languageEnglish
Pages (from-to)2672-2676
Number of pages5
JournalLangmuir
Volume16
Issue number6
DOIs
Publication statusPublished - Mar 21 2000
Externally publishedYes

Fingerprint

Lipases
Lipase
Catalysis
catalysis
Monolayers
7-hydroxycoumarin
Cholesterol
cholesterol
Lipids
Kinetics
lipids
hydrolysis
Water
Hydrolysis
air
kinetics
Air
water
Stearates
Photobleaching

All Science Journal Classification (ASJC) codes

  • Materials Science(all)
  • Condensed Matter Physics
  • Surfaces and Interfaces
  • Spectroscopy
  • Electrochemistry

Cite this

Lipase catalysis on monolayers at the air/water interface. 2. Diffusion-controlled kinetics on quasi-two-dimension. / Tanaka, Keiji; Mecca, Steven P.; Yu, Hyuk.

In: Langmuir, Vol. 16, No. 6, 21.03.2000, p. 2672-2676.

Research output: Contribution to journalArticle

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