Studies on the specificity of Candida rugosa lipase catalyzed esterification reactions in organic media
In this study, the feasibility of the synthesis of various flavor esters catalyzed by a commercial lipase from Candida rugosa was investigated and the process parameters were optimized. Lipase from C. rugosa successfully catalyzed the synthesis of 19 esters. The highest yields, of more than 90 % aft...
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Serbian Chemical Society
2006-01-01
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doaj-cae99806d4cc42d9a7f08ecb21f53a342020-11-24T20:55:54ZengSerbian Chemical Society Journal of the Serbian Chemical Society0352-51392006-01-017113141Studies on the specificity of Candida rugosa lipase catalyzed esterification reactions in organic mediaDEJAN BEZBRADICAIVANA KARALAZICNEVENA OGNJANOVICDUSAN MIJINSLAVICA SILER-MARINKOVICZORICA KNEZEVICIn this study, the feasibility of the synthesis of various flavor esters catalyzed by a commercial lipase from Candida rugosa was investigated and the process parameters were optimized. Lipase from C. rugosa successfully catalyzed the synthesis of 19 esters. The highest yields, of more than 90 % after 20 h, were observed in the synthesis of short-chain esters, pentyl propanoate, isopentyl butanoate, and butyl butanoate. Increasing the number of carbon atoms of both substrates above 8 caused a significant decrease of the initial reaction rates and the final yields. The enzyme showed surprisingly low affinity towards pentanoic acid and hexanoic acid, compared with the higher homologues, octanoic acid and decanoic acid. In addition to the number of carbon atoms, the structure of the substrates had a significant influence on the enzyme activity. Namely, the activity of the enzyme towards isopropanol was significantly lower compared with n-propanol. Additionally, cis-9-octadecenoic acid was a better substrate than octadecanoic acid, its saturated analogue.http://www.shd.org.yu/HtDocs/SHD/Vol71/No1/JSCS_V71_No1-04.pdflipaseCandida rugosaesterificationspecificity |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
DEJAN BEZBRADICA IVANA KARALAZIC NEVENA OGNJANOVIC DUSAN MIJIN SLAVICA SILER-MARINKOVIC ZORICA KNEZEVIC |
spellingShingle |
DEJAN BEZBRADICA IVANA KARALAZIC NEVENA OGNJANOVIC DUSAN MIJIN SLAVICA SILER-MARINKOVIC ZORICA KNEZEVIC Studies on the specificity of Candida rugosa lipase catalyzed esterification reactions in organic media Journal of the Serbian Chemical Society lipase Candida rugosa esterification specificity |
author_facet |
DEJAN BEZBRADICA IVANA KARALAZIC NEVENA OGNJANOVIC DUSAN MIJIN SLAVICA SILER-MARINKOVIC ZORICA KNEZEVIC |
author_sort |
DEJAN BEZBRADICA |
title |
Studies on the specificity of Candida rugosa lipase catalyzed esterification reactions in organic media |
title_short |
Studies on the specificity of Candida rugosa lipase catalyzed esterification reactions in organic media |
title_full |
Studies on the specificity of Candida rugosa lipase catalyzed esterification reactions in organic media |
title_fullStr |
Studies on the specificity of Candida rugosa lipase catalyzed esterification reactions in organic media |
title_full_unstemmed |
Studies on the specificity of Candida rugosa lipase catalyzed esterification reactions in organic media |
title_sort |
studies on the specificity of candida rugosa lipase catalyzed esterification reactions in organic media |
publisher |
Serbian Chemical Society |
series |
Journal of the Serbian Chemical Society |
issn |
0352-5139 |
publishDate |
2006-01-01 |
description |
In this study, the feasibility of the synthesis of various flavor esters catalyzed by a commercial lipase from Candida rugosa was investigated and the process parameters were optimized. Lipase from C. rugosa successfully catalyzed the synthesis of 19 esters. The highest yields, of more than 90 % after 20 h, were observed in the synthesis of short-chain esters, pentyl propanoate, isopentyl butanoate, and butyl butanoate. Increasing the number of carbon atoms of both substrates above 8 caused a significant decrease of the initial reaction rates and the final yields. The enzyme showed surprisingly low affinity towards pentanoic acid and hexanoic acid, compared with the higher homologues, octanoic acid and decanoic acid. In addition to the number of carbon atoms, the structure of the substrates had a significant influence on the enzyme activity. Namely, the activity of the enzyme towards isopropanol was significantly lower compared with n-propanol. Additionally, cis-9-octadecenoic acid was a better substrate than octadecanoic acid, its saturated analogue. |
topic |
lipase Candida rugosa esterification specificity |
url |
http://www.shd.org.yu/HtDocs/SHD/Vol71/No1/JSCS_V71_No1-04.pdf |
work_keys_str_mv |
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