Evaluation of inorganic matrixes as supports for immobilization of microbial lipase
Candida rugosa was immobilized by physical adsorption on several inorganic supports using hexane as coupling medium. The enzymatic activities of the different derivatives were determined by both hydrolysis of olive oil and esterification of n-butanol with butyric acid. The results were compared to p...
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Brazilian Society of Chemical Engineering
2000-01-01
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doaj-05c8e924bbc54146bf20088e956f034a2020-11-24T20:58:50ZengBrazilian Society of Chemical EngineeringBrazilian Journal of Chemical Engineering0104-66321678-43832000-01-01174-7849858Evaluation of inorganic matrixes as supports for immobilization of microbial lipaseCastro H.F.Silva M.L.C.P.Silva G.L.J.PCandida rugosa was immobilized by physical adsorption on several inorganic supports using hexane as coupling medium. The enzymatic activities of the different derivatives were determined by both hydrolysis of olive oil and esterification of n-butanol with butyric acid. The results were compared to previous data obtained by using a controlled porous silica matrix. The goal was to contribute in searching inexpensive supports for optimum lipase performance. All supports examined exhibited good properties for binding the enzyme lipase. Zirconium phosphate was the best support, giving the highest percentage of protein fixation (86%) and the highest retention of lipase activity after immobilization (34%). The operational stability performance for niobium oxide derivative was improved by previously activated the support with silane and glutaraldehyde. Thermal stabilities were also examined by thermal gravimetric analysis (TG).http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322000000400048Inorganic matrixeslipaseimmobilizationesterificationoperational stabilitythermal stability |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Castro H.F. Silva M.L.C.P. Silva G.L.J.P |
spellingShingle |
Castro H.F. Silva M.L.C.P. Silva G.L.J.P Evaluation of inorganic matrixes as supports for immobilization of microbial lipase Brazilian Journal of Chemical Engineering Inorganic matrixes lipase immobilization esterification operational stability thermal stability |
author_facet |
Castro H.F. Silva M.L.C.P. Silva G.L.J.P |
author_sort |
Castro H.F. |
title |
Evaluation of inorganic matrixes as supports for immobilization of microbial lipase |
title_short |
Evaluation of inorganic matrixes as supports for immobilization of microbial lipase |
title_full |
Evaluation of inorganic matrixes as supports for immobilization of microbial lipase |
title_fullStr |
Evaluation of inorganic matrixes as supports for immobilization of microbial lipase |
title_full_unstemmed |
Evaluation of inorganic matrixes as supports for immobilization of microbial lipase |
title_sort |
evaluation of inorganic matrixes as supports for immobilization of microbial lipase |
publisher |
Brazilian Society of Chemical Engineering |
series |
Brazilian Journal of Chemical Engineering |
issn |
0104-6632 1678-4383 |
publishDate |
2000-01-01 |
description |
Candida rugosa was immobilized by physical adsorption on several inorganic supports using hexane as coupling medium. The enzymatic activities of the different derivatives were determined by both hydrolysis of olive oil and esterification of n-butanol with butyric acid. The results were compared to previous data obtained by using a controlled porous silica matrix. The goal was to contribute in searching inexpensive supports for optimum lipase performance. All supports examined exhibited good properties for binding the enzyme lipase. Zirconium phosphate was the best support, giving the highest percentage of protein fixation (86%) and the highest retention of lipase activity after immobilization (34%). The operational stability performance for niobium oxide derivative was improved by previously activated the support with silane and glutaraldehyde. Thermal stabilities were also examined by thermal gravimetric analysis (TG). |
topic |
Inorganic matrixes lipase immobilization esterification operational stability thermal stability |
url |
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322000000400048 |
work_keys_str_mv |
AT castrohf evaluationofinorganicmatrixesassupportsforimmobilizationofmicrobiallipase AT silvamlcp evaluationofinorganicmatrixesassupportsforimmobilizationofmicrobiallipase AT silvagljp evaluationofinorganicmatrixesassupportsforimmobilizationofmicrobiallipase |
_version_ |
1716784363069243392 |