Synthesis of structured phospholipids by immobilized phospholipase A2 catalyzed acidolysis

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Synthesis of structured phospholipids by immobilized phospholipase A2 catalyzed acidolysis. / Vikbjerg, Anders Falk; Mu, Huiling; Xu, Xuebing.

In: Journal of Biotechnology, Vol. 128, No. 3, 2007, p. 545-54.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Vikbjerg, AF, Mu, H & Xu, X 2007, 'Synthesis of structured phospholipids by immobilized phospholipase A2 catalyzed acidolysis', Journal of Biotechnology, vol. 128, no. 3, pp. 545-54. https://doi.org/10.1016/j.jbiotec.2006.11.006

APA

Vikbjerg, A. F., Mu, H., & Xu, X. (2007). Synthesis of structured phospholipids by immobilized phospholipase A2 catalyzed acidolysis. Journal of Biotechnology, 128(3), 545-54. https://doi.org/10.1016/j.jbiotec.2006.11.006

Vancouver

Vikbjerg AF, Mu H, Xu X. Synthesis of structured phospholipids by immobilized phospholipase A2 catalyzed acidolysis. Journal of Biotechnology. 2007;128(3):545-54. https://doi.org/10.1016/j.jbiotec.2006.11.006

Author

Vikbjerg, Anders Falk ; Mu, Huiling ; Xu, Xuebing. / Synthesis of structured phospholipids by immobilized phospholipase A2 catalyzed acidolysis. In: Journal of Biotechnology. 2007 ; Vol. 128, No. 3. pp. 545-54.

Bibtex

@article{582ba14537464651b00720fcd65bd700,
title = "Synthesis of structured phospholipids by immobilized phospholipase A2 catalyzed acidolysis",
abstract = "Acyl modification of the sn-2 position in phospholipids (PLs) was conducted by acidolysis reaction using immobilized phospholipase A(2) (PLA(2)) as the catalyst. In the first stage we screened different carriers for their ability to immobilize PLA(2). Several carriers were able to fix the enzyme and maintain catalytic activity; however, the final choice of carrier for the continued work was a non-ionic weakly polar macroreticular resin. Response surface methodology was applied to evaluate the influence of substrate ratio, reaction temperature, and water addition during acidolysis reaction between caprylic acid and soybean phosphatidylcholine (PC). Reaction temperature and water addition had significant effect on acidolysis reaction, however no effect was observed for substrate ratio (mol caprylic acid/mol PC) in range tested. In general an inverse relationship between incorporation of caprylic acid and PC recovery was observed. Highest incorporation obtained during acidolysis reactions was 36%. Such incorporation could be obtained under reaction temperature, 45 degrees C; substrate ratio, 9mol/mol caprylic acid/PC; water addition of 2%; 30wt.% immobilized enzyme; and reaction time, 48h. The yield under these conditions was however only 29%. Lysophosphatidylcholine (LPC) was the major by-product formed during the reaction. Incorporation of acyl donor into LPC was very low (",
author = "Vikbjerg, {Anders Falk} and Huiling Mu and Xuebing Xu",
year = "2007",
doi = "10.1016/j.jbiotec.2006.11.006",
language = "English",
volume = "128",
pages = "545--54",
journal = "Journal of Biotechnology",
issn = "0168-1656",
publisher = "Elsevier",
number = "3",

}

RIS

TY - JOUR

T1 - Synthesis of structured phospholipids by immobilized phospholipase A2 catalyzed acidolysis

AU - Vikbjerg, Anders Falk

AU - Mu, Huiling

AU - Xu, Xuebing

PY - 2007

Y1 - 2007

N2 - Acyl modification of the sn-2 position in phospholipids (PLs) was conducted by acidolysis reaction using immobilized phospholipase A(2) (PLA(2)) as the catalyst. In the first stage we screened different carriers for their ability to immobilize PLA(2). Several carriers were able to fix the enzyme and maintain catalytic activity; however, the final choice of carrier for the continued work was a non-ionic weakly polar macroreticular resin. Response surface methodology was applied to evaluate the influence of substrate ratio, reaction temperature, and water addition during acidolysis reaction between caprylic acid and soybean phosphatidylcholine (PC). Reaction temperature and water addition had significant effect on acidolysis reaction, however no effect was observed for substrate ratio (mol caprylic acid/mol PC) in range tested. In general an inverse relationship between incorporation of caprylic acid and PC recovery was observed. Highest incorporation obtained during acidolysis reactions was 36%. Such incorporation could be obtained under reaction temperature, 45 degrees C; substrate ratio, 9mol/mol caprylic acid/PC; water addition of 2%; 30wt.% immobilized enzyme; and reaction time, 48h. The yield under these conditions was however only 29%. Lysophosphatidylcholine (LPC) was the major by-product formed during the reaction. Incorporation of acyl donor into LPC was very low (

AB - Acyl modification of the sn-2 position in phospholipids (PLs) was conducted by acidolysis reaction using immobilized phospholipase A(2) (PLA(2)) as the catalyst. In the first stage we screened different carriers for their ability to immobilize PLA(2). Several carriers were able to fix the enzyme and maintain catalytic activity; however, the final choice of carrier for the continued work was a non-ionic weakly polar macroreticular resin. Response surface methodology was applied to evaluate the influence of substrate ratio, reaction temperature, and water addition during acidolysis reaction between caprylic acid and soybean phosphatidylcholine (PC). Reaction temperature and water addition had significant effect on acidolysis reaction, however no effect was observed for substrate ratio (mol caprylic acid/mol PC) in range tested. In general an inverse relationship between incorporation of caprylic acid and PC recovery was observed. Highest incorporation obtained during acidolysis reactions was 36%. Such incorporation could be obtained under reaction temperature, 45 degrees C; substrate ratio, 9mol/mol caprylic acid/PC; water addition of 2%; 30wt.% immobilized enzyme; and reaction time, 48h. The yield under these conditions was however only 29%. Lysophosphatidylcholine (LPC) was the major by-product formed during the reaction. Incorporation of acyl donor into LPC was very low (

U2 - 10.1016/j.jbiotec.2006.11.006

DO - 10.1016/j.jbiotec.2006.11.006

M3 - Journal article

C2 - 17150274

VL - 128

SP - 545

EP - 554

JO - Journal of Biotechnology

JF - Journal of Biotechnology

SN - 0168-1656

IS - 3

ER -

ID: 44090433