Strategies for lipase-catalyzed production and the purification of structured phospholipids

2006 ◽  
Vol 108 (10) ◽  
pp. 802-811 ◽  
Author(s):  
Anders F. Vikbjerg ◽  
Jean-Yves Rusig ◽  
Gunnar Jonsson ◽  
Huiling Mu ◽  
Xuebing Xu
Keyword(s):  
Structured Phospholipids

Acyl chain that matters: introducing sn-2 acyl chain preference to a phospholipase D by protein engineering

2019 ◽  
Vol 32 (1) ◽  
pp. 1-11 ◽  
Author(s):  
Jasmina Damnjanović ◽  
Hideo Nakano ◽  
Yugo Iwasaki
Keyword(s):  
Protein Engineering ◽  
Phospholipase D ◽  
Enzymatic Synthesis ◽  
Acyl Chain ◽  
Saturation Mutagenesis ◽  
Structure Model ◽  
Streptomyces Antibioticus ◽  
In The Wild ◽  
Structured Phospholipids ◽  
Experimental Findings

AbstractPhospholipase D (PLD) is an enzyme widely used for enzymatic synthesis of structured phospholipids (PLs) with modified head groups. These PLs are mainly used as food supplements and liposome ingredients. Still, there is a need for an enzyme that discriminates between PLs and lysoPLs, for specific detection of lysoPLs in various specimens and enzymatic synthesis of certain PLs from a mixed substrate. To meet this demand, we aimed at altering sn-2 acyl chain recognition of a PLD, leading to a variant enzyme preferably reacting on lysoPLs, by protein engineering. Based on the crystal structure of Streptomyces antibioticus PLD, W166 was targeted for saturation mutagenesis due to its strong interaction with the sn-2 acyl chain of the PL. Screening result pointed at W166R and W166K PLDs to selectively react on lysophosphatidylcholine (lysoPC), while not on PC. These variants showed a negative correlation between activity and sn-2 chain length of PL substrates. This behavior was not observed in the wild-type (WT)-PLD. Kinetic analysis revealed that the W166R and W166K variants have 7–10 times higher preference to lysoPC compared to the WT-PLD. Additionally, W166R PLD showed detectable activity toward glycero-3-phosphocholine, unlike the WT-PLD. Applicability of the lysoPC-preferring PLD was demonstrated by detection of lysoPC in the mixed PC/lysoPC sample and by the synthesis of cyclic phosphatidic acid. Structure model analyses supported the experimental findings and provided a basis for the structure model-based hypothesis on the observed behavior of the enzymes.

Production of structured phospholipids by lipase-catalyzed acidolysis: optimization using response surface methodology

2002 ◽  
Vol 31 (4) ◽  
pp. 523-532 ◽  
Author(s):  
Lifeng Peng ◽  
Xuebing Xu ◽  
Huiling Mu ◽  
Carl-Erik Høy ◽  
Jens Adler-Nissen
Keyword(s):  
Response Surface Methodology ◽  
Response Surface ◽  
Structured Phospholipids

scholarly journals Synthesis of structured phospholipids by immobilized phospholipase A2 catalyzed acidolysis

2007 ◽  
Vol 128 (3) ◽  
pp. 545-554 ◽  
Author(s):  
Anders Falk Vikbjerg ◽  
Huiling Mu ◽  
Xuebing Xu
Keyword(s):  
Phospholipase A2 ◽  
Structured Phospholipids

scholarly journals Preparation of Structured Phospholipids

Oleoscience ◽  
2002 ◽  
Vol 2 (1) ◽  
pp. 13-17,12 ◽  
Author(s):  
Setsuko HARA ◽  
Yoichiro TOTANI
Keyword(s):  
Structured Phospholipids
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