Diacylglycerol synthesis by enzymatic glycerolysis: Screening of commercially available lipases

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

Standard

Diacylglycerol synthesis by enzymatic glycerolysis : Screening of commercially available lipases. / Kristensen, J.B.; Xu, X.; Mu, Huiling.

In: J A O C S, Vol. 82, No. 5, 01.01.2005, p. 329-334.

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

Harvard

Kristensen, JB, Xu, X & Mu, H 2005, 'Diacylglycerol synthesis by enzymatic glycerolysis: Screening of commercially available lipases', J A O C S, vol. 82, no. 5, pp. 329-334. https://doi.org/10.1007/s11746-005-1074-5

APA

Kristensen, J. B., Xu, X., & Mu, H. (2005). Diacylglycerol synthesis by enzymatic glycerolysis: Screening of commercially available lipases. J A O C S, 82(5), 329-334. https://doi.org/10.1007/s11746-005-1074-5

Vancouver

Kristensen JB, Xu X, Mu H. Diacylglycerol synthesis by enzymatic glycerolysis: Screening of commercially available lipases. J A O C S. 2005 Jan 1;82(5):329-334. https://doi.org/10.1007/s11746-005-1074-5

Author

Kristensen, J.B. ; Xu, X. ; Mu, Huiling. / Diacylglycerol synthesis by enzymatic glycerolysis : Screening of commercially available lipases. In: J A O C S. 2005 ; Vol. 82, No. 5. pp. 329-334.

Bibtex

@article{3368897cb8d948d9bf536766f8eb55d9,
title = "Diacylglycerol synthesis by enzymatic glycerolysis: Screening of commercially available lipases",
abstract = "Seven lipases were screened for their ability to synthesize DAG in the glycerolysis of rapeseed oil. In batch reactions with free glycerol, the lipase carrier was of great importance for catalysis. Catalysis did not take place in reactions with lipases having hydrophilic carriers. The best DAG yield (approx. 60 wt%) was achieved with Novozym 435 and Lipase PS-D after 7 h, and an equilibrium was obtained. Stepwise addition of glycerol allowed catalysis with Novozym CALB L (immobilized) to take place in spite of the hydrophilic carrier; however, the DAG yield was only 19 wt%. This result suggests that glycerol forms a layer around the hydrophilic lipase particles, limiting contact between the lipases and the hydrophobic oil phase. With glycerol absorbed on silica gel, all lipases catalyzed the glycerolysis reaction. Faster conversion of TAG was obtained with Lipase PS-D, Lipase AK, and Lipase F-AP15 than in reactions with free glycerol, but the DAG yield remained approximately 60-65 wt%. Nonspecific lipases yielded more 1,3-DAG early in the reaction.",
author = "J.B. Kristensen and X. Xu and Huiling Mu",
year = "2005",
month = jan,
day = "1",
doi = "10.1007/s11746-005-1074-5",
language = "English",
volume = "82",
pages = "329--334",
journal = "Oil & Soap",
issn = "0003-021X",
publisher = "Springer",
number = "5",

}

RIS

TY - JOUR

T1 - Diacylglycerol synthesis by enzymatic glycerolysis

T2 - Screening of commercially available lipases

AU - Kristensen, J.B.

AU - Xu, X.

AU - Mu, Huiling

PY - 2005/1/1

Y1 - 2005/1/1

N2 - Seven lipases were screened for their ability to synthesize DAG in the glycerolysis of rapeseed oil. In batch reactions with free glycerol, the lipase carrier was of great importance for catalysis. Catalysis did not take place in reactions with lipases having hydrophilic carriers. The best DAG yield (approx. 60 wt%) was achieved with Novozym 435 and Lipase PS-D after 7 h, and an equilibrium was obtained. Stepwise addition of glycerol allowed catalysis with Novozym CALB L (immobilized) to take place in spite of the hydrophilic carrier; however, the DAG yield was only 19 wt%. This result suggests that glycerol forms a layer around the hydrophilic lipase particles, limiting contact between the lipases and the hydrophobic oil phase. With glycerol absorbed on silica gel, all lipases catalyzed the glycerolysis reaction. Faster conversion of TAG was obtained with Lipase PS-D, Lipase AK, and Lipase F-AP15 than in reactions with free glycerol, but the DAG yield remained approximately 60-65 wt%. Nonspecific lipases yielded more 1,3-DAG early in the reaction.

AB - Seven lipases were screened for their ability to synthesize DAG in the glycerolysis of rapeseed oil. In batch reactions with free glycerol, the lipase carrier was of great importance for catalysis. Catalysis did not take place in reactions with lipases having hydrophilic carriers. The best DAG yield (approx. 60 wt%) was achieved with Novozym 435 and Lipase PS-D after 7 h, and an equilibrium was obtained. Stepwise addition of glycerol allowed catalysis with Novozym CALB L (immobilized) to take place in spite of the hydrophilic carrier; however, the DAG yield was only 19 wt%. This result suggests that glycerol forms a layer around the hydrophilic lipase particles, limiting contact between the lipases and the hydrophobic oil phase. With glycerol absorbed on silica gel, all lipases catalyzed the glycerolysis reaction. Faster conversion of TAG was obtained with Lipase PS-D, Lipase AK, and Lipase F-AP15 than in reactions with free glycerol, but the DAG yield remained approximately 60-65 wt%. Nonspecific lipases yielded more 1,3-DAG early in the reaction.

UR - http://www.scopus.com/inward/record.url?scp=25444484057&partnerID=8YFLogxK

U2 - 10.1007/s11746-005-1074-5

DO - 10.1007/s11746-005-1074-5

M3 - Journal article

AN - SCOPUS:25444484057

VL - 82

SP - 329

EP - 334

JO - Oil & Soap

JF - Oil & Soap

SN - 0003-021X

IS - 5

ER -

ID: 45482006