Immobilization of Candida antarctica A and Thermomyces lanuginosus lipases on cotton terry cloth fibrils using polyethyleneimine

In this study, cotton terry cloth fibrils were coated with 0.2% polyethyleneimine (PEI). Lipases from Candida antarctica A (CALA) and Thermomyces lanuginosus (TL) were immobilized on this support through adsorption followed by cross-linking with 0.2% glutaraldehyde. PEI-enzyme aggregates formation a...

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Published in:Colloids and Surfaces B: Biointerfaces
Main Authors: ALBAYRAK, NEDİM, Ondul, Eda, Dizge, Nadir
Format: Article in Journal/Newspaper
Language:English
Published: 2012
Subjects:
Online Access:https://doi.org/10.1016/j.colsurfb.2012.02.020
https://avesis.yyu.edu.tr/publication/details/cc82c339-8afe-49ba-bbc0-c5059865466a/oai
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spelling ftyyuniv:cc82c339-8afe-49ba-bbc0-c5059865466a 2023-05-15T13:58:49+02:00 Immobilization of Candida antarctica A and Thermomyces lanuginosus lipases on cotton terry cloth fibrils using polyethyleneimine ALBAYRAK, NEDİM Ondul, Eda Dizge, Nadir 2012-06-15T00:00:00Z https://doi.org/10.1016/j.colsurfb.2012.02.020 https://avesis.yyu.edu.tr/publication/details/cc82c339-8afe-49ba-bbc0-c5059865466a/oai eng eng cc82c339-8afe-49ba-bbc0-c5059865466a doi:10.1016/j.colsurfb.2012.02.020 https://avesis.yyu.edu.tr/publication/details/cc82c339-8afe-49ba-bbc0-c5059865466a/oai info:eu-repo/semantics/closedAccess info:eu-repo/semantics/article 2012 ftyyuniv https://doi.org/10.1016/j.colsurfb.2012.02.020 2022-02-21T17:26:53Z In this study, cotton terry cloth fibrils were coated with 0.2% polyethyleneimine (PEI). Lipases from Candida antarctica A (CALA) and Thermomyces lanuginosus (TL) were immobilized on this support through adsorption followed by cross-linking with 0.2% glutaraldehyde. PEI-enzyme aggregates formation and growth of aggregates on cotton cloth fibrils lead to multilayer immobilization of the lipases. PEI and lipase was mixed to form PEI-enzyme complex/aggregate. The highest amount of enzyme precipitate was obtained at the PEI to enzyme ratio of 1/20-1/40 for both lipases. The effect of pH was also investigated for aggregates formation. The results showed that when pH values were below 8, aggregation and precipitation were not occurred for C. antarctica A lipase. However, pH did not affect PEI-enzyme aggregate formation for T. lanuginosus lipase. Immobilized enzyme amount was approximately 180 mg/g support and 200 mg/g support for T. lanuginosus and C. antarctica A lipases, respectively. Effect of the reaction temperature on the relative activity of the free and immobilized lipases at various temperature (30-80 degrees C) was studied. It was found that immobilization had no effect on the optimum temperature and it was 60 degrees C for both free and immobilized enzymes. The effect of operational and storage stability on activity of free and immobilized lipases were also investigated. Immobilized lipases exhibited that they could be stored at room temperature with a little activity lost during 28 days. (C) 2012 Elsevier B.V. All rights reserved. Article in Journal/Newspaper Antarc* Antarctica Van Yüzüncü Yıl University Research Information System Colloids and Surfaces B: Biointerfaces 95 109 114
institution Open Polar
collection Van Yüzüncü Yıl University Research Information System
op_collection_id ftyyuniv
language English
description In this study, cotton terry cloth fibrils were coated with 0.2% polyethyleneimine (PEI). Lipases from Candida antarctica A (CALA) and Thermomyces lanuginosus (TL) were immobilized on this support through adsorption followed by cross-linking with 0.2% glutaraldehyde. PEI-enzyme aggregates formation and growth of aggregates on cotton cloth fibrils lead to multilayer immobilization of the lipases. PEI and lipase was mixed to form PEI-enzyme complex/aggregate. The highest amount of enzyme precipitate was obtained at the PEI to enzyme ratio of 1/20-1/40 for both lipases. The effect of pH was also investigated for aggregates formation. The results showed that when pH values were below 8, aggregation and precipitation were not occurred for C. antarctica A lipase. However, pH did not affect PEI-enzyme aggregate formation for T. lanuginosus lipase. Immobilized enzyme amount was approximately 180 mg/g support and 200 mg/g support for T. lanuginosus and C. antarctica A lipases, respectively. Effect of the reaction temperature on the relative activity of the free and immobilized lipases at various temperature (30-80 degrees C) was studied. It was found that immobilization had no effect on the optimum temperature and it was 60 degrees C for both free and immobilized enzymes. The effect of operational and storage stability on activity of free and immobilized lipases were also investigated. Immobilized lipases exhibited that they could be stored at room temperature with a little activity lost during 28 days. (C) 2012 Elsevier B.V. All rights reserved.
format Article in Journal/Newspaper
author ALBAYRAK, NEDİM
Ondul, Eda
Dizge, Nadir
spellingShingle ALBAYRAK, NEDİM
Ondul, Eda
Dizge, Nadir
Immobilization of Candida antarctica A and Thermomyces lanuginosus lipases on cotton terry cloth fibrils using polyethyleneimine
author_facet ALBAYRAK, NEDİM
Ondul, Eda
Dizge, Nadir
author_sort ALBAYRAK, NEDİM
title Immobilization of Candida antarctica A and Thermomyces lanuginosus lipases on cotton terry cloth fibrils using polyethyleneimine
title_short Immobilization of Candida antarctica A and Thermomyces lanuginosus lipases on cotton terry cloth fibrils using polyethyleneimine
title_full Immobilization of Candida antarctica A and Thermomyces lanuginosus lipases on cotton terry cloth fibrils using polyethyleneimine
title_fullStr Immobilization of Candida antarctica A and Thermomyces lanuginosus lipases on cotton terry cloth fibrils using polyethyleneimine
title_full_unstemmed Immobilization of Candida antarctica A and Thermomyces lanuginosus lipases on cotton terry cloth fibrils using polyethyleneimine
title_sort immobilization of candida antarctica a and thermomyces lanuginosus lipases on cotton terry cloth fibrils using polyethyleneimine
publishDate 2012
url https://doi.org/10.1016/j.colsurfb.2012.02.020
https://avesis.yyu.edu.tr/publication/details/cc82c339-8afe-49ba-bbc0-c5059865466a/oai
genre Antarc*
Antarctica
genre_facet Antarc*
Antarctica
op_relation cc82c339-8afe-49ba-bbc0-c5059865466a
doi:10.1016/j.colsurfb.2012.02.020
https://avesis.yyu.edu.tr/publication/details/cc82c339-8afe-49ba-bbc0-c5059865466a/oai
op_rights info:eu-repo/semantics/closedAccess
op_doi https://doi.org/10.1016/j.colsurfb.2012.02.020
container_title Colloids and Surfaces B: Biointerfaces
container_volume 95
container_start_page 109
op_container_end_page 114
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