Optimization of conjugated linoleic acid triglycerides via enzymatic esterification in no-solvent system

Dan Yi; Xiuqin Sun; Guangyou Li; Fayi Liu; Xuezheng Lin; Jihong Shen

doi:10.1007/s00343-009-9170-7

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Optimization of conjugated linoleic acid triglycerides via enzymatic esterification in no-solvent system

Updated：2023-05-16

- Optimization of conjugated linoleic acid triglycerides via enzymatic esterification in no-solvent system
- Journal of Oceanology and Limnology Vol. 27, Issue 3, Pages: 574-577(2009)
- Affiliations：
  
  1. College of Life Sciences Ocean University of China
  2. Key Laboratory of Marine Bio-active Substance First Institute of Oceanography State Oceanic Administration
- Author bio：
- Funds：
- DOI：10.1007/s00343-009-9170-7
  CLC：
- Online First：07 November 2009，
  
  Published：2009
- Accepted：
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Yi, D., Sun, X., Li, G. et al. Optimization of conjugated linoleic acid triglycerides via enzymatic esterification in no-solvent system., Chin. J. Ocean. Limnol. 27, 574–577 (2009). https://doi.org/10.1007/s00343-009-9170-7
DOI：

Yi, D., Sun, X., Li, G. et al. Optimization of conjugated linoleic acid triglycerides via enzymatic esterification in no-solvent system., Chin. J. Ocean. Limnol. 27, 574–577 (2009). https://doi.org/10.1007/s00343-009-9170-7 DOI：

摘要

Abstract

We compared four esterifiable enzymes. The lipase Novozym 435 possessed the highest activity for the conjugated linoleic acid esterification during the synthesis of triglycerides. The triglycerides were synthesized by esterification of glycerol and conjugated linoleic acid (CLA) in a no-solvent system using lipase catalysis. We investigated the effects of temperature

enzyme concentration

water content

and time on esterification. Enzyme and water concentrations of up to 1% of the total reaction volume and a system temperature of 60°C proved optimal for esterification. Similarly

when the esterification was carried out for 24 h

the reaction ratio improved to 94.11%. The esterification rate of the rotating screen basket remained high (87.28%) when the enzyme was re-used for the 5th time. We evaluated the substrate selectivity of lipase (NOVO 435) and determined that this lipase prefers the 10

12-octadacadienoic acid to the 9

11-octadecadienoic acid.

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references

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