Influence of the pH of glutaraldehyde and the use of dextran aldehyde on the preparation of cross-linked enzyme aggregates (CLEAs) of lipase from Burkholderia cepacia

The preparation of cross-linked enzyme aggregates (CLEAs) of lipase has been a challenge due the low amount of lysine residues that lipases have on their surface. The results show that CLEAs prepared using dextran aldehyde (100-200KDa) have a higher hydrolysis activity and particle size (activities...

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Autores principales:	Caballero Valdés,Eduardo, Wilson Soto,Lorena, Aroca Arcaya,Germán
Lenguaje:	English
Publicado:	Pontificia Universidad Católica de Valparaíso 2011
Materias:	albumin dextran aldehyde glutaraldehyde immobilisation lipase
Acceso en línea:	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582011000300010
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spelling	oai:scielo:S0717-345820110003000102011-09-23Influence of the pH of glutaraldehyde and the use of dextran aldehyde on the preparation of cross-linked enzyme aggregates (CLEAs) of lipase from Burkholderia cepaciaCaballero Valdés,EduardoWilson Soto,LorenaAroca Arcaya,Germán albumin dextran aldehyde glutaraldehyde immobilisation lipase The preparation of cross-linked enzyme aggregates (CLEAs) of lipase has been a challenge due the low amount of lysine residues that lipases have on their surface. The results show that CLEAs prepared using dextran aldehyde (100-200KDa) have a higher hydrolysis activity and particle size (activities between 3186 Â± 21 U/g of CLEA and 4800 Â± 30 U/g of CLEA and particle sizes between 52.6 Â± 18.7 Âµm and 126.2 Â± 53.5 Âµm) than CLEAs prepared with glutaraldehyde (0.1 KDa) (activities between 894 Â± 16 U/g of CLEA and 2874 Â± 20 U/g of CLEA and particle sizes between 21.2 Â± 5.1 Âµm and 83.4 Â± 24.9 Âµm); Thermal stability assays of bioctalysts at 60ÂºC at pH 7.0 using phosphate buffer 25 mM showed that CLEAs prepared with dextran aldehyde have lower residual activity after 50 hrs (maximum residual activity of 46.8% in the CLEA) than CLEAs prepared with glutaraldehyde (maximum residual activity of 70.2% in CLEA). When considering hydrolysis activity, thermal stability and residual activity of CLEAs as a criteria for selecting the best preparation conditions, it has been found that the best condition for CLEAs preparation are to use glutaraldehyde as cross-linking reagent at pH 9.5, at a concentration of 3.5 g/l, and an enzyme/albumin ratio of 15.info:eu-repo/semantics/openAccessPontificia Universidad Católica de ValparaísoElectronic Journal of Biotechnology v.14 n.3 20112011-05-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582011000300010en
institution	Scielo Chile
collection	Scielo Chile
language	English
topic	albumin dextran aldehyde glutaraldehyde immobilisation lipase
spellingShingle	albumin dextran aldehyde glutaraldehyde immobilisation lipase Caballero Valdés,Eduardo Wilson Soto,Lorena Aroca Arcaya,Germán Influence of the pH of glutaraldehyde and the use of dextran aldehyde on the preparation of cross-linked enzyme aggregates (CLEAs) of lipase from Burkholderia cepacia
description	The preparation of cross-linked enzyme aggregates (CLEAs) of lipase has been a challenge due the low amount of lysine residues that lipases have on their surface. The results show that CLEAs prepared using dextran aldehyde (100-200KDa) have a higher hydrolysis activity and particle size (activities between 3186 Â± 21 U/g of CLEA and 4800 Â± 30 U/g of CLEA and particle sizes between 52.6 Â± 18.7 Âµm and 126.2 Â± 53.5 Âµm) than CLEAs prepared with glutaraldehyde (0.1 KDa) (activities between 894 Â± 16 U/g of CLEA and 2874 Â± 20 U/g of CLEA and particle sizes between 21.2 Â± 5.1 Âµm and 83.4 Â± 24.9 Âµm); Thermal stability assays of bioctalysts at 60ÂºC at pH 7.0 using phosphate buffer 25 mM showed that CLEAs prepared with dextran aldehyde have lower residual activity after 50 hrs (maximum residual activity of 46.8% in the CLEA) than CLEAs prepared with glutaraldehyde (maximum residual activity of 70.2% in CLEA). When considering hydrolysis activity, thermal stability and residual activity of CLEAs as a criteria for selecting the best preparation conditions, it has been found that the best condition for CLEAs preparation are to use glutaraldehyde as cross-linking reagent at pH 9.5, at a concentration of 3.5 g/l, and an enzyme/albumin ratio of 15.
author	Caballero Valdés,Eduardo Wilson Soto,Lorena Aroca Arcaya,Germán
author_facet	Caballero Valdés,Eduardo Wilson Soto,Lorena Aroca Arcaya,Germán
author_sort	Caballero Valdés,Eduardo
title	Influence of the pH of glutaraldehyde and the use of dextran aldehyde on the preparation of cross-linked enzyme aggregates (CLEAs) of lipase from Burkholderia cepacia
title_short	Influence of the pH of glutaraldehyde and the use of dextran aldehyde on the preparation of cross-linked enzyme aggregates (CLEAs) of lipase from Burkholderia cepacia
title_full	Influence of the pH of glutaraldehyde and the use of dextran aldehyde on the preparation of cross-linked enzyme aggregates (CLEAs) of lipase from Burkholderia cepacia
title_fullStr	Influence of the pH of glutaraldehyde and the use of dextran aldehyde on the preparation of cross-linked enzyme aggregates (CLEAs) of lipase from Burkholderia cepacia
title_full_unstemmed	Influence of the pH of glutaraldehyde and the use of dextran aldehyde on the preparation of cross-linked enzyme aggregates (CLEAs) of lipase from Burkholderia cepacia
title_sort	influence of the ph of glutaraldehyde and the use of dextran aldehyde on the preparation of cross-linked enzyme aggregates (cleas) of lipase from burkholderia cepacia
publisher	Pontificia Universidad Católica de Valparaíso
publishDate	2011
url	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582011000300010
work_keys_str_mv	AT caballerovaldeseduardo influenceofthephofglutaraldehydeandtheuseofdextranaldehydeonthepreparationofcrosslinkedenzymeaggregatescleasoflipasefromburkholderiacepacia AT wilsonsotolorena influenceofthephofglutaraldehydeandtheuseofdextranaldehydeonthepreparationofcrosslinkedenzymeaggregatescleasoflipasefromburkholderiacepacia AT arocaarcayagerman influenceofthephofglutaraldehydeandtheuseofdextranaldehydeonthepreparationofcrosslinkedenzymeaggregatescleasoflipasefromburkholderiacepacia
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Influence of the pH of glutaraldehyde and the use of dextran aldehyde on the preparation of cross-linked enzyme aggregates (CLEAs) of lipase from Burkholderia cepacia

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