Literature DB >> 10099440

Water activity control: a way to improve the efficiency of continuous lipase esterification.

S Colombié1, R J Tweddell, J S Condoret, A Marty.   

Abstract

During continuous lipase-catalyzed oleic acid esterification by ethanol in n-hexane, the oleic acid conversion, initially at 95%, decreases to 20% after 2 h. This decrease is caused by the accumulation of the water produced in the course of the reaction in the packed-bed reactor (PBR). In order to improve the PBR efficiency, it is necessary to evacuate the water produced. In this study, different approaches have been tested to control the water content in the PBR during continuous esterification. The first approach consisted in improving the water solubility by increasing the reaction medium polarity. The addition of polar additives to n-hexane, the use of more polar solvents, and the use of solvent-free reaction medium were tested as a means to favor the water evacuation from the PBR. First of all, the use ofn-hexane supplemented with acetone (3 M) or 2-methyl-2-propanol (1 M) enabled the conversion to be maintained at higher values than those obtained in pure n-hexane. The replacement of n-hexane by a more polar solvent, like the 5-methyl-2-hexanone, resulted in the same effect. In all cases, conversions at steady-state were always less than 95%, as obtained in pure n-hexane. This is explained by a decrease in the enzyme activity due to the increase in the medium polarity. Nevertheless, an increase in enzyme quantity allowed 90% conversion to be maintained during 1 week using 3 M acetone amended n-hexane. Good results (a steady-state conversion of about 80%) were obtained when esterification was carried out in a solvent-free reaction medium containing 2 M 2-methyl-2-propanol as a polar additive. The second approach consisted in the evaporation of the accumulated water by use of an intermittent airflow. Although this process did not enable constant esterification rate to be maintained, it did enable the initial conversion (95%) to be restored intermittently. Copyright 1998 John Wiley & Sons, Inc.

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Year:  1998        PMID: 10099440

Source DB:  PubMed          Journal:  Biotechnol Bioeng        ISSN: 0006-3592            Impact factor:   4.530


  3 in total

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2.  Displaying Candida antarctica lipase B on the cell surface of Aspergillus niger as a potential food-grade whole-cell catalyst.

Authors:  Zhi-You Pan; Zhi-Ming Yang; Li Pan; Sui-Ping Zheng; Shuang-Yan Han; Ying Lin
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3.  Production of Pentaerythritol Monoricinoleate (PEMR) by immobilized Candida antarctica lipase B.

Authors:  Manish G Yadav; Rajeshkumar N Vadgama; Monali R Kavadia; Annamma Anil Odaneth; Arvind M Lali
Journal:  Biotechnol Rep (Amst)       Date:  2019-06-16
  3 in total

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