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...
Published in: | Bioprocess and Biosystems Engineering |
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2017
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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 |
_version_ |
1786206809932955648 |