2004
DOI: 10.1016/j.molcatb.2004.01.008
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Dependency of water concentration on ethanolysis of trioleoylglycerol by lipases

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Cited by 64 publications
(39 citation statements)
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“…The excess ethanol used deactivated the Rhizomucor miehei lipase, which is known to be strongly deactivated by alcohols, 20 and in particular by ethanol. 21 The position of the active site of this lipase on the external surface of the enzyme promotes unhindered access of alcohols to the catalytic triad. In view of the previous results, Novozym 435 was the catalyst chosen for the parametric analysis described in the following sections.…”
Section: Resultsmentioning
confidence: 99%
“…The excess ethanol used deactivated the Rhizomucor miehei lipase, which is known to be strongly deactivated by alcohols, 20 and in particular by ethanol. 21 The position of the active site of this lipase on the external surface of the enzyme promotes unhindered access of alcohols to the catalytic triad. In view of the previous results, Novozym 435 was the catalyst chosen for the parametric analysis described in the following sections.…”
Section: Resultsmentioning
confidence: 99%
“…Solvents may also influence the residual water of the enzyme varying its catalytic activity. However, the Candida antarctica lipase B used in this work has been described to be still active at very low water content in the system 8 . In addition, it has also a high resistance to alcohol deactivation 9 .…”
Section: Introductionmentioning
confidence: 92%
“…Tert-pentanol is more polar than n-hexane logP hexane 3.5 and logP tert-pentanol 0.96 . Piyatheerawong et al 8 , observed that CALB was able to maintain tis active conformation after being in contact with dry ethanol. Therefore tertpentanol and solvent-free medium at high molar ratio 76:1 do not cause any activity loss despite their polarity.…”
Section: 86mentioning
confidence: 99%
“…In any case, it must be emphasized that in the literature it has been reported that lipase B from C. antarctica (CALB), of which Lipozyme 435 is an immobilized form, is a less water-sensitive lipase than others, either in its free or immobilized form [30]. Immobilized CALB dehydrated by dry ethanol was still able to retain active conformation, suggesting that essential water molecules are kept in its structure [30]. However, activity losses have been found after SC-CO 2 treatment in this study.…”
Section: Effect Of Water Content On the Residual Activitymentioning
confidence: 99%