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Phospholipase D Activity in Relation to the Size of Substrate Micelles
Author(s) -
Dreßler Lars,
UlbrichHofmann Renate
Publication year - 2017
Publication title -
journal of the american oil chemists' society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.512
H-Index - 117
eISSN - 1558-9331
pISSN - 0003-021X
DOI - 10.1007/s11746-017-3037-4
Subject(s) - phospholipase d , micelle , substrate (aquarium) , sodium dodecyl sulfate , chemistry , triton x 100 , enzyme , sodium , phospholipase , dynamic light scattering , molar concentration , chromatography , biochemistry , biophysics , pulmonary surfactant , materials science , biology , organic chemistry , nanotechnology , ecology , aqueous solution , nanoparticle
The activity of phospholipase D (PLD) is strongly dependent on the aggregation state of its substrate. Artificial substrates, such as phosphatidyl‐ p ‐nitrophenol (P p NP), are preferably used in a mixture with Triton ® X‐100 (Serva) and sodium dodecyl sulfate (SDS) in the form of mixed micelles. In this paper the activities of PLD from cabbage (PLD cab ), which needs Ca 2+ ions for its activity, and PLD from Streptomyces sp. (PLD Str ), which is independent of Ca 2+ ions, are compared as a function of the detergent and substrate concentrations. While the variation of the Triton ® X‐100 and P p NP contents changed the activities of both enzymes in similar way, SDS showed activation effects on plant PLD but inactivation effects on microbial PLD. The activity decreased to 50% at a 7‐tenfold molar excess of Triton ® X‐100 related to P p NP. SDS induced a strong activation (up to fourfold) of PLD cab but decreased the activity of PLD Str with increasing concentration. Activity‐substrate profiles of both PLDs passed optima at 3–4 mM P p NP. In all experiments, the activity changes correlated with changes of the micelle sizes determined by dynamic light scattering. These results highlight the immense importance of the micelle structure, which is not considered in most studies.