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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Main Authors: Castro H.F., Silva M.L.C.P., Silva G.L.J.P
Format: Article
Language:English
Published: Brazilian Society of Chemical Engineering 2000-01-01
Series:Brazilian Journal of Chemical Engineering
Subjects:
Online Access:http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322000000400048
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spelling 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
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