Direct visualization of the dynamic hydrolysis process of an L-DPPC monolayer catalyzed by phospholipase D at the air/water interface

Qiang He, Xiuhong Zhai, Junbai Li

Research output: Contribution to journalArticlepeer-review

17 Scopus citations

Abstract

The hydrolysis reaction of L-α-dipalmitoylphosphatidylcholine (L-DPPC) catalyzed by cabbage phospholipase D (PLD) at the air/water interface has been studied by Brewster angle microscopy (BAM) and film balance technique. The curves of surface pressure versus time show that the hydrolysis reaction depends on the initial state of the lipid monolayer. The BAM images display that the hydrolysis reaction preferentially occurs in the liquid-expanded phase where PLD has a maximum activity. In the coexistence region of liquid-expanded and liquid-condensed phases, a "lotus-like" domain of the monolayer was observed, indicating that the hydrolysis product 1,2-dipalmitoylphosphatidic acid (DPPA) created a new phase, which inhibited the reaction rate of hydrolysis.

Original languageEnglish (US)
Pages (from-to)473-476
Number of pages4
JournalJournal of Physical Chemistry B
Volume108
Issue number1
StatePublished - Jan 8 2004

Fingerprint Dive into the research topics of 'Direct visualization of the dynamic hydrolysis process of an L-DPPC monolayer catalyzed by phospholipase D at the air/water interface'. Together they form a unique fingerprint.

Cite this