Enzymic hydrolysis of lecithin

Influence of Intermolecular Spacing on Enzymic Hydrolysis of Lecithin Monolayers. When snake venom phospholipase A is injected under a lecithin monolayer, it splits lecithin into lysolecithin and free fatty acid. The change in polar groups of the monolayer results in a change of surface potential. However, if prior to injection of enzyme into the subsolution, a lecithin monolayer is compressed to such a surface pressure that the active site of the enzyme is unable to penetrate the monolayer, hydrolysis does not proceed. For monolayers of dipalmitoyl, egg, soybean, and dioleoyl lecithins the threshold surface pressure values at which hydrolysis does not proceed are 20, 30, 37, and 45 dynes per cm., respectively (40). This is also the same order for area per molecule in their surface pressure-area curves, indicating that enzymic hydrolysis of lecithin monolayers is influenced by the unsaturation of the fatty acyl chains and hence the intermolecular spacing in monolayers (40). 

Enzymic hydrolysis of lecithin monolayers is strikingly influenced by the degree of unsaturation of fatty acyl chains and hence by the intermolecular spacing in monolayers. 

Enzymic hydrolysis of lecithin has not been exhaustively published in papers but rather patented. Actually, no exact data on the reaction conditions have been available, e.g., enzyme level has not been specified, as well as reaction time and temperature have varied in a wide range. On the other... 

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