Immobilization and stability studies of a lipase from thermophilic Bacillus sp: The effect of process parameters on immobilization of enzyme

A thermostable lipase was partially purified from the culture supernatant of a thermophilic Bacillus sp. The enzyme is optimally active at 60ºC and pH 8.0. The enzyme showed enhancement in activity in presence of benzene or hexane (30% v/v each). The activity (assayed by determining the rel...

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Autores principales:	Nawani,Neerupma, Singh,Rajvinder, Kaur,Jagdeep
Lenguaje:	English
Publicado:	Pontificia Universidad Católica de Valparaíso 2006
Materias:	esterification immobilization lipase thermostability
Acceso en línea:	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582006000500011
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spelling	oai:scielo:S0717-345820060005000112007-01-04Immobilization and stability studies of a lipase from thermophilic Bacillus sp: The effect of process parameters on immobilization of enzymeNawani,NeerupmaSingh,RajvinderKaur,Jagdeep esterification immobilization lipase thermostability A thermostable lipase was partially purified from the culture supernatant of a thermophilic Bacillus sp. The enzyme is optimally active at 60ºC and pH 8.0. The enzyme showed enhancement in activity in presence of benzene or hexane (30% v/v each). The activity (assayed by determining the release of pNP from pNP laurate) was stimulated up to 60% of these solvents in enzyme reaction mixture. The catalytic properties of this thermostable enzyme can be further improved via the use of different immobilization techniques and reaction conditions. Enzyme was immobilized on different solid supports and their enzyme activity and stability was compared. The enzyme was adsorbed on silica and HP-20 beads followed by cross-linking with gluteraldehyde on HP-20, which improved the thermostability of enzyme. The optimum pH (pH 8.5) was nearly same for aqueous and immobilized enzyme while optimum temperature was nearly 5ºC higher in case of immobilized enzyme. The immobilized/cross linked enzyme was more thermostable at 70 and 80ºC in comparison to aqueous and surface adsorbed lipase on silica and HP-20. The optimum temperature for esterification reactions was determined to be 60-65ºC. Half-life of immobilized lipase was nearly 2.5 x higher than the aqueous enzyme at 70ºC. Esterification of methanol and oleic acid to methyl oleate by immobilized enzyme was studied in detail.info:eu-repo/semantics/openAccessPontificia Universidad Católica de ValparaísoElectronic Journal of Biotechnology v.9 n.5 20062006-10-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582006000500011en
institution	Scielo Chile
collection	Scielo Chile
language	English
topic	esterification immobilization lipase thermostability
spellingShingle	esterification immobilization lipase thermostability Nawani,Neerupma Singh,Rajvinder Kaur,Jagdeep Immobilization and stability studies of a lipase from thermophilic Bacillus sp: The effect of process parameters on immobilization of enzyme
description	A thermostable lipase was partially purified from the culture supernatant of a thermophilic Bacillus sp. The enzyme is optimally active at 60ºC and pH 8.0. The enzyme showed enhancement in activity in presence of benzene or hexane (30% v/v each). The activity (assayed by determining the release of pNP from pNP laurate) was stimulated up to 60% of these solvents in enzyme reaction mixture. The catalytic properties of this thermostable enzyme can be further improved via the use of different immobilization techniques and reaction conditions. Enzyme was immobilized on different solid supports and their enzyme activity and stability was compared. The enzyme was adsorbed on silica and HP-20 beads followed by cross-linking with gluteraldehyde on HP-20, which improved the thermostability of enzyme. The optimum pH (pH 8.5) was nearly same for aqueous and immobilized enzyme while optimum temperature was nearly 5ºC higher in case of immobilized enzyme. The immobilized/cross linked enzyme was more thermostable at 70 and 80ºC in comparison to aqueous and surface adsorbed lipase on silica and HP-20. The optimum temperature for esterification reactions was determined to be 60-65ºC. Half-life of immobilized lipase was nearly 2.5 x higher than the aqueous enzyme at 70ºC. Esterification of methanol and oleic acid to methyl oleate by immobilized enzyme was studied in detail.
author	Nawani,Neerupma Singh,Rajvinder Kaur,Jagdeep
author_facet	Nawani,Neerupma Singh,Rajvinder Kaur,Jagdeep
author_sort	Nawani,Neerupma
title	Immobilization and stability studies of a lipase from thermophilic Bacillus sp: The effect of process parameters on immobilization of enzyme
title_short	Immobilization and stability studies of a lipase from thermophilic Bacillus sp: The effect of process parameters on immobilization of enzyme
title_full	Immobilization and stability studies of a lipase from thermophilic Bacillus sp: The effect of process parameters on immobilization of enzyme
title_fullStr	Immobilization and stability studies of a lipase from thermophilic Bacillus sp: The effect of process parameters on immobilization of enzyme
title_full_unstemmed	Immobilization and stability studies of a lipase from thermophilic Bacillus sp: The effect of process parameters on immobilization of enzyme
title_sort	immobilization and stability studies of a lipase from thermophilic bacillus sp: the effect of process parameters on immobilization of enzyme
publisher	Pontificia Universidad Católica de Valparaíso
publishDate	2006
url	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582006000500011
work_keys_str_mv	AT nawanineerupma immobilizationandstabilitystudiesofalipasefromthermophilicbacillussptheeffectofprocessparametersonimmobilizationofenzyme AT singhrajvinder immobilizationandstabilitystudiesofalipasefromthermophilicbacillussptheeffectofprocessparametersonimmobilizationofenzyme AT kaurjagdeep immobilizationandstabilitystudiesofalipasefromthermophilicbacillussptheeffectofprocessparametersonimmobilizationofenzyme
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Immobilization and stability studies of a lipase from thermophilic Bacillus sp: The effect of process parameters on immobilization of enzyme

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