Immobilization of Candida antarctica lipase B onto Purolite(A (R)) MN102 and its application in solvent-free and organic media esterification

The aim of this study was to develop simple and efficient method for immobilization of Candida antarctica lipase B onto hydrophobic anion exchange resin Purolite(A (R)) MN102 and to apply immobilized catalyst for the enzymatic synthesis of two valuable esters-isoamyl acetate and l-ascorbyl oleate. A...

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Published in:Bioprocess and Biosystems Engineering
Main Authors: Ćorović, Marija, Mihailović, Mladen, Banjanac, Katarina, Carević, Milica, Milivojević, Ana, Milosavić, Nenad, Bezbradica, Dejan
Format: Article in Journal/Newspaper
Language:unknown
Published: Springer, New York 2017
Subjects:
Online Access:http://TechnoRep.tmf.bg.ac.rs/handle/123456789/3655
https://doi.org/10.1007/s00449-016-1671-0
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spelling ftunivbelgradftm:oai:TechnoRep.tmf.bg.ac.rs:123456789/3655 2023-12-24T10:09:14+01:00 Immobilization of Candida antarctica lipase B onto Purolite(A (R)) MN102 and its application in solvent-free and organic media esterification Ćorović, Marija Mihailović, Mladen Banjanac, Katarina Carević, Milica Milivojević, Ana Milosavić, Nenad Bezbradica, Dejan 2017 http://TechnoRep.tmf.bg.ac.rs/handle/123456789/3655 https://doi.org/10.1007/s00449-016-1671-0 unknown Springer, New York info:eu-repo/grantAgreement/MESTD/Integrated and Interdisciplinary Research (IIR or III)/46010/RS// 1615-7591 http://TechnoRep.tmf.bg.ac.rs/handle/123456789/3655 doi:10.1007/s00449-016-1671-0 27534413 2-s2.0-84982279844 000391382800003 restrictedAccess ARR Bioprocess and Biosystems Engineering Candida antarctica lipase B Immobilization Esterification Isoamyl acetate L-Ascorbyl oleate article publishedVersion 2017 ftunivbelgradftm https://doi.org/10.1007/s00449-016-1671-0 2023-11-28T17:19:54Z The aim of this study was to develop simple and efficient method for immobilization of Candida antarctica lipase B onto hydrophobic anion exchange resin Purolite(A (R)) MN102 and to apply immobilized catalyst for the enzymatic synthesis of two valuable esters-isoamyl acetate and l-ascorbyl oleate. At optimized conditions (1 M phosphate buffer pH = 7, 7 h at 25 A degrees C, and 18.75 mg of offered proteins g(-1) of support), immobilized lipase with hydrolytic activity of 888.4 p-nitrophenyl butyrate units g(-1) was obtained. Afterwards, preparation was applied for the solvent-free synthesis of isoamyl acetate from triacetin and isoamyl alcohol. At 75 A degrees C, 1 M of isoamyl alcohol, and 6 mg ml(-1) of enzyme 100 % yield was achieved in 6 h, while at prolonged reaction times, complete conversion was enabled even at lower temperatures, lower lipase loadings, and higher substrate concentrations. After 15 consecutive reuses (60 h), activity of catalyst dropped to 50 % of its initial value and total amount of 1.31 mol (170.55 g) of ester with 1 g of biocatalyst was produced. Even higher operational stability of lipase (25 % loss of activity in 200 h) was observed in the synthesis of l-ascorbyl oleate performed in organic solvent (t-butanol). Multiple use of one batch of immobilized biocatalyst in both cases led to a significant process cost reduction and substantial increment of corresponding productivities. Article in Journal/Newspaper Antarc* Antarctica TechnoRep - Faculty of Technology and Metallurgy Repository Bioprocess and Biosystems Engineering 40 1 23 34
institution Open Polar
collection TechnoRep - Faculty of Technology and Metallurgy Repository
op_collection_id ftunivbelgradftm
language unknown
topic Candida antarctica lipase B
Immobilization
Esterification
Isoamyl acetate
L-Ascorbyl oleate
spellingShingle Candida antarctica lipase B
Immobilization
Esterification
Isoamyl acetate
L-Ascorbyl oleate
Ćorović, Marija
Mihailović, Mladen
Banjanac, Katarina
Carević, Milica
Milivojević, Ana
Milosavić, Nenad
Bezbradica, Dejan
Immobilization of Candida antarctica lipase B onto Purolite(A (R)) MN102 and its application in solvent-free and organic media esterification
topic_facet Candida antarctica lipase B
Immobilization
Esterification
Isoamyl acetate
L-Ascorbyl oleate
description The aim of this study was to develop simple and efficient method for immobilization of Candida antarctica lipase B onto hydrophobic anion exchange resin Purolite(A (R)) MN102 and to apply immobilized catalyst for the enzymatic synthesis of two valuable esters-isoamyl acetate and l-ascorbyl oleate. At optimized conditions (1 M phosphate buffer pH = 7, 7 h at 25 A degrees C, and 18.75 mg of offered proteins g(-1) of support), immobilized lipase with hydrolytic activity of 888.4 p-nitrophenyl butyrate units g(-1) was obtained. Afterwards, preparation was applied for the solvent-free synthesis of isoamyl acetate from triacetin and isoamyl alcohol. At 75 A degrees C, 1 M of isoamyl alcohol, and 6 mg ml(-1) of enzyme 100 % yield was achieved in 6 h, while at prolonged reaction times, complete conversion was enabled even at lower temperatures, lower lipase loadings, and higher substrate concentrations. After 15 consecutive reuses (60 h), activity of catalyst dropped to 50 % of its initial value and total amount of 1.31 mol (170.55 g) of ester with 1 g of biocatalyst was produced. Even higher operational stability of lipase (25 % loss of activity in 200 h) was observed in the synthesis of l-ascorbyl oleate performed in organic solvent (t-butanol). Multiple use of one batch of immobilized biocatalyst in both cases led to a significant process cost reduction and substantial increment of corresponding productivities.
format Article in Journal/Newspaper
author Ćorović, Marija
Mihailović, Mladen
Banjanac, Katarina
Carević, Milica
Milivojević, Ana
Milosavić, Nenad
Bezbradica, Dejan
author_facet Ćorović, Marija
Mihailović, Mladen
Banjanac, Katarina
Carević, Milica
Milivojević, Ana
Milosavić, Nenad
Bezbradica, Dejan
author_sort Ćorović, Marija
title Immobilization of Candida antarctica lipase B onto Purolite(A (R)) MN102 and its application in solvent-free and organic media esterification
title_short Immobilization of Candida antarctica lipase B onto Purolite(A (R)) MN102 and its application in solvent-free and organic media esterification
title_full Immobilization of Candida antarctica lipase B onto Purolite(A (R)) MN102 and its application in solvent-free and organic media esterification
title_fullStr Immobilization of Candida antarctica lipase B onto Purolite(A (R)) MN102 and its application in solvent-free and organic media esterification
title_full_unstemmed Immobilization of Candida antarctica lipase B onto Purolite(A (R)) MN102 and its application in solvent-free and organic media esterification
title_sort immobilization of candida antarctica lipase b onto purolite(a (r)) mn102 and its application in solvent-free and organic media esterification
publisher Springer, New York
publishDate 2017
url http://TechnoRep.tmf.bg.ac.rs/handle/123456789/3655
https://doi.org/10.1007/s00449-016-1671-0
genre Antarc*
Antarctica
genre_facet Antarc*
Antarctica
op_source Bioprocess and Biosystems Engineering
op_relation info:eu-repo/grantAgreement/MESTD/Integrated and Interdisciplinary Research (IIR or III)/46010/RS//
1615-7591
http://TechnoRep.tmf.bg.ac.rs/handle/123456789/3655
doi:10.1007/s00449-016-1671-0
27534413
2-s2.0-84982279844
000391382800003
op_rights restrictedAccess
ARR
op_doi https://doi.org/10.1007/s00449-016-1671-0
container_title Bioprocess and Biosystems Engineering
container_volume 40
container_issue 1
container_start_page 23
op_container_end_page 34
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