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image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao European Journal of ...arrow_drop_down
image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao
European Journal of Lipid Science and Technology
Article . 2010 . Peer-reviewed
License: Wiley Online Library User Agreement
Data sources: Crossref
image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao
Lipid Technology
Article . 2011 . Peer-reviewed
License: Wiley Online Library User Agreement
Data sources: Crossref
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Enzymatic degumming

Authors: Albert J. Dijkstra;

Enzymatic degumming

Abstract

AbstractThe first enzymatic degumming process to be used industrially was the EnzyMax® process that was launched in 1992; it used porcine phospholipase A2 (PLA2). Subsequently, various microbial phospholipases (PLases) with different specificities have been developed. They have the advantages of being kosher/halal and of having a non‐limited availability and lower cost.The first of these microbial enzymes were the phospholipases A1 (Lecitase® Novo and Ultra) and more recently, a phospholipase C (Purifine®) and a lipid acyl transferase (LysoMax®) with PLA2 acitivity have also become available in commercial quantities. These enzymes have different specificities. The Lecitases® and the LysoMax® enzymes catalyse the hydrolysis of all common phosphatides and differ in this respect from the Purifine® enzyme, which is specific for phosphatidyl choline and phosphatidyl ethanolamine. These phosphatides are hydrolysed to oil‐soluble diacylglycerol and water‐soluble phosphate esters. Since these diacylglycerols remain in the oil during refining, they contribute to the oil yield. That also holds for the sterol and stanol fatty esters formed as a consequence of the phosphatide hydrolysis catalysed by the LysoMax® enzyme. In addition, all enzymes cause less oil to be retained by the gums by decreasing the amount of gums and/or their oil retention, which also contributes to an improved oil yield.On the other hand and contrary to common belief, the enzymes are incapable of catalysing the hydrolysis of non‐hydratable phosphatides (alkaline earth salts of phosphatidic acid) under industrial conditions. Consequently, the industrial enzymatic degumming step has to be preceded by a chemical degumming step to arrive at a degummed oil with a sufficiently low residual phosphorus content that can be physically refined. Accordingly, it might well be preferable to limit the oil treatment to said chemical degumming and produce oil with a low residual phosphorus content and gums, and then treat the gums separately to recover their fatty matter, whereby this recovery can be enzymatic or chemical.

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selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
112
Top 1%
Top 1%
Top 10%
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