Fluorescence microscopic imaging of hydrolysis of phospholipid monolayers by phospholipase D at the air-water interface

Tetsuya Kondo, Takashi Kakiuchi, Masatsugu Shimomura

    Research output: Contribution to journalArticlepeer-review

    12 Citations (Scopus)

    Abstract

    The enzymatic hydrolysis of phosphatidylcholine (PC) to phosphatidic acid (PA) by phospholipase D (PLD) at the air-water interface was investigated with epifluorescence microscopy. In the PC-PA mixed monolayer doped with octadecyl rhodamine B, the gel phase of PA was observed as dark domains of 2-5 μm diameter at a surface pressure above 25 mN m-1. When PC was spread over a subphase containing Streptomyces chromofuscus PLD, the assemblies of the circular dark domains whose diameter was 2-5 μm appeared at 25 mN m-1. In the case of peanut PLD, few dark domains were observed and their diameter was less than 1 μm. The observed morphological difference in the assemblies of the hydrolysis product by peanut and Streptomyces PLDs indicates that the two PLDs act differently on the monolayer, as has been suggested in the hydrolysis of the monolayer by these PLDs at the oil-water interface. The difference in the hydrolytic action of Streptomyces and plant PLDs suggests that the segregation of the product, PA, from the reaction system as a solid phase is important in efficient hydrolysis.

    Original languageEnglish
    Pages (from-to)887-889
    Number of pages3
    JournalThin Solid Films
    Volume244
    Issue number1-2
    DOIs
    Publication statusPublished - 1994 May 15

    ASJC Scopus subject areas

    • Electronic, Optical and Magnetic Materials
    • Surfaces and Interfaces
    • Surfaces, Coatings and Films
    • Metals and Alloys
    • Materials Chemistry

    Fingerprint

    Dive into the research topics of 'Fluorescence microscopic imaging of hydrolysis of phospholipid monolayers by phospholipase D at the air-water interface'. Together they form a unique fingerprint.

    Cite this