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Elucidation of acyl migration during lipase‐catalyzed production of structured phospholipids
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| Zeitschriftentitel: | Journal of the American Oil Chemists' Society |
|---|---|
| Personen und Körperschaften: | , , |
| In: | Journal of the American Oil Chemists' Society, 83, 2006, 7, S. 609-614 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
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| Schlagwörter: |
| author_facet |
Vikbjerg, Anders F. Mu, Huiling Xu, Xuebing Vikbjerg, Anders F. Mu, Huiling Xu, Xuebing |
|---|---|
| author |
Vikbjerg, Anders F. Mu, Huiling Xu, Xuebing |
| spellingShingle |
Vikbjerg, Anders F. Mu, Huiling Xu, Xuebing Journal of the American Oil Chemists' Society Elucidation of acyl migration during lipase‐catalyzed production of structured phospholipids Organic Chemistry General Chemical Engineering |
| author_sort |
vikbjerg, anders f. |
| spelling |
Vikbjerg, Anders F. Mu, Huiling Xu, Xuebing 0003-021X 1558-9331 Wiley Organic Chemistry General Chemical Engineering http://dx.doi.org/10.1007/s11746-006-1246-3 <jats:title>Abstract</jats:title><jats:p>Elucidation of acyl migration was carried out in the Lipozyme RM IM (<jats:italic>Rhizomucor miehei</jats:italic>)‐catalyzed transesterification between soybean phosphatidylcholine (PC) and caprylic acid in solvent‐free media. A five‐factor response surface design was used to evaluate the influence of five major factors and their relationships. The five factors—enzyme dosage, reaction temperature, water addition, reaction time, and substrate ratio—were varied on three levels together with two star points. Enzyme dosage, reaction temperature, and reaction time showed increased effect on the acyl migration into the <jats:italic>sn</jats:italic>‐2 position of PC, whereas increased water addition and substrate ratio had no significant effect in the ranges tested. The best‐fitting quadratic response surface model was determined by regression and backward elimination. The coefficient of determination (<jats:italic>R</jats:italic><jats:sup>2</jats:sup>) was 0.84, which indicates that the fitted quadratic model has acceptable qualities in expressing acyl migration for the enzymatic transesterification. Correlation was observed between acyl donor in the <jats:italic>sn</jats:italic>‐2 position of PC and incorporation of acyl donor into the intermediate lysophosphatidylcholine. Furthermore, acyl migration into the <jats:italic>sn</jats:italic>‐2 position of PC was confirmed by TLC‐FID, as PC with caprylic acid was observed on both positions. Under certain conditions, up to 18% incorporation could be observed in the <jats:italic>sn</jats:italic>‐2 position during the lipase‐catalyzed transesterification.</jats:p> Elucidation of acyl migration during lipase‐catalyzed production of structured phospholipids Journal of the American Oil Chemists' Society |
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Journal of the American Oil Chemists' Society |
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| title |
Elucidation of acyl migration during lipase‐catalyzed production of structured phospholipids |
| title_unstemmed |
Elucidation of acyl migration during lipase‐catalyzed production of structured phospholipids |
| title_full |
Elucidation of acyl migration during lipase‐catalyzed production of structured phospholipids |
| title_fullStr |
Elucidation of acyl migration during lipase‐catalyzed production of structured phospholipids |
| title_full_unstemmed |
Elucidation of acyl migration during lipase‐catalyzed production of structured phospholipids |
| title_short |
Elucidation of acyl migration during lipase‐catalyzed production of structured phospholipids |
| title_sort |
elucidation of acyl migration during lipase‐catalyzed production of structured phospholipids |
| topic |
Organic Chemistry General Chemical Engineering |
| url |
http://dx.doi.org/10.1007/s11746-006-1246-3 |
| publishDate |
2006 |
| physical |
609-614 |
| description |
<jats:title>Abstract</jats:title><jats:p>Elucidation of acyl migration was carried out in the Lipozyme RM IM (<jats:italic>Rhizomucor miehei</jats:italic>)‐catalyzed transesterification between soybean phosphatidylcholine (PC) and caprylic acid in solvent‐free media. A five‐factor response surface design was used to evaluate the influence of five major factors and their relationships. The five factors—enzyme dosage, reaction temperature, water addition, reaction time, and substrate ratio—were varied on three levels together with two star points. Enzyme dosage, reaction temperature, and reaction time showed increased effect on the acyl migration into the <jats:italic>sn</jats:italic>‐2 position of PC, whereas increased water addition and substrate ratio had no significant effect in the ranges tested. The best‐fitting quadratic response surface model was determined by regression and backward elimination. The coefficient of determination (<jats:italic>R</jats:italic><jats:sup>2</jats:sup>) was 0.84, which indicates that the fitted quadratic model has acceptable qualities in expressing acyl migration for the enzymatic transesterification. Correlation was observed between acyl donor in the <jats:italic>sn</jats:italic>‐2 position of PC and incorporation of acyl donor into the intermediate lysophosphatidylcholine. Furthermore, acyl migration into the <jats:italic>sn</jats:italic>‐2 position of PC was confirmed by TLC‐FID, as PC with caprylic acid was observed on both positions. Under certain conditions, up to 18% incorporation could be observed in the <jats:italic>sn</jats:italic>‐2 position during the lipase‐catalyzed transesterification.</jats:p> |
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| author | Vikbjerg, Anders F., Mu, Huiling, Xu, Xuebing |
| author_facet | Vikbjerg, Anders F., Mu, Huiling, Xu, Xuebing, Vikbjerg, Anders F., Mu, Huiling, Xu, Xuebing |
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| description | <jats:title>Abstract</jats:title><jats:p>Elucidation of acyl migration was carried out in the Lipozyme RM IM (<jats:italic>Rhizomucor miehei</jats:italic>)‐catalyzed transesterification between soybean phosphatidylcholine (PC) and caprylic acid in solvent‐free media. A five‐factor response surface design was used to evaluate the influence of five major factors and their relationships. The five factors—enzyme dosage, reaction temperature, water addition, reaction time, and substrate ratio—were varied on three levels together with two star points. Enzyme dosage, reaction temperature, and reaction time showed increased effect on the acyl migration into the <jats:italic>sn</jats:italic>‐2 position of PC, whereas increased water addition and substrate ratio had no significant effect in the ranges tested. The best‐fitting quadratic response surface model was determined by regression and backward elimination. The coefficient of determination (<jats:italic>R</jats:italic><jats:sup>2</jats:sup>) was 0.84, which indicates that the fitted quadratic model has acceptable qualities in expressing acyl migration for the enzymatic transesterification. Correlation was observed between acyl donor in the <jats:italic>sn</jats:italic>‐2 position of PC and incorporation of acyl donor into the intermediate lysophosphatidylcholine. Furthermore, acyl migration into the <jats:italic>sn</jats:italic>‐2 position of PC was confirmed by TLC‐FID, as PC with caprylic acid was observed on both positions. Under certain conditions, up to 18% incorporation could be observed in the <jats:italic>sn</jats:italic>‐2 position during the lipase‐catalyzed transesterification.</jats:p> |
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| imprint_str_mv | Wiley, 2006 |
| institution | DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1 |
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| spelling | Vikbjerg, Anders F. Mu, Huiling Xu, Xuebing 0003-021X 1558-9331 Wiley Organic Chemistry General Chemical Engineering http://dx.doi.org/10.1007/s11746-006-1246-3 <jats:title>Abstract</jats:title><jats:p>Elucidation of acyl migration was carried out in the Lipozyme RM IM (<jats:italic>Rhizomucor miehei</jats:italic>)‐catalyzed transesterification between soybean phosphatidylcholine (PC) and caprylic acid in solvent‐free media. A five‐factor response surface design was used to evaluate the influence of five major factors and their relationships. The five factors—enzyme dosage, reaction temperature, water addition, reaction time, and substrate ratio—were varied on three levels together with two star points. Enzyme dosage, reaction temperature, and reaction time showed increased effect on the acyl migration into the <jats:italic>sn</jats:italic>‐2 position of PC, whereas increased water addition and substrate ratio had no significant effect in the ranges tested. The best‐fitting quadratic response surface model was determined by regression and backward elimination. The coefficient of determination (<jats:italic>R</jats:italic><jats:sup>2</jats:sup>) was 0.84, which indicates that the fitted quadratic model has acceptable qualities in expressing acyl migration for the enzymatic transesterification. Correlation was observed between acyl donor in the <jats:italic>sn</jats:italic>‐2 position of PC and incorporation of acyl donor into the intermediate lysophosphatidylcholine. Furthermore, acyl migration into the <jats:italic>sn</jats:italic>‐2 position of PC was confirmed by TLC‐FID, as PC with caprylic acid was observed on both positions. Under certain conditions, up to 18% incorporation could be observed in the <jats:italic>sn</jats:italic>‐2 position during the lipase‐catalyzed transesterification.</jats:p> Elucidation of acyl migration during lipase‐catalyzed production of structured phospholipids Journal of the American Oil Chemists' Society |
| spellingShingle | Vikbjerg, Anders F., Mu, Huiling, Xu, Xuebing, Journal of the American Oil Chemists' Society, Elucidation of acyl migration during lipase‐catalyzed production of structured phospholipids, Organic Chemistry, General Chemical Engineering |
| title | Elucidation of acyl migration during lipase‐catalyzed production of structured phospholipids |
| title_full | Elucidation of acyl migration during lipase‐catalyzed production of structured phospholipids |
| title_fullStr | Elucidation of acyl migration during lipase‐catalyzed production of structured phospholipids |
| title_full_unstemmed | Elucidation of acyl migration during lipase‐catalyzed production of structured phospholipids |
| title_short | Elucidation of acyl migration during lipase‐catalyzed production of structured phospholipids |
| title_sort | elucidation of acyl migration during lipase‐catalyzed production of structured phospholipids |
| title_unstemmed | Elucidation of acyl migration during lipase‐catalyzed production of structured phospholipids |
| topic | Organic Chemistry, General Chemical Engineering |
| url | http://dx.doi.org/10.1007/s11746-006-1246-3 |