Systemic Concocting of Cross‐Linked Enzyme Aggregates of Candida antarctica Lipase B (Novozyme 435) for the Biomanufacturing of Rhamnolipids
Abstract In the present study, Candida antarctica lipase B was immobilized on amine‐functionalized silica microspheres as cross‐linked enzyme aggregates (CLEA) and utilized for the biomanufacturing of rhamnolipids (RL). Lipase CLEA synthesized under optimized conditions of 2.0:1.0 by volume of silic...
Published in: | Journal of Surfactants and Detergents |
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Online Access: | http://dx.doi.org/10.1002/jsde.12266 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fjsde.12266 https://onlinelibrary.wiley.com/doi/pdf/10.1002/jsde.12266 https://onlinelibrary.wiley.com/doi/full-xml/10.1002/jsde.12266 |
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crwiley:10.1002/jsde.12266 2024-06-02T07:57:19+00:00 Systemic Concocting of Cross‐Linked Enzyme Aggregates of Candida antarctica Lipase B (Novozyme 435) for the Biomanufacturing of Rhamnolipids Rathankumar, Abiram Karanam SaiLavanyaa, Sundar Saikia, Kongkona Gururajan, Anusha Sivanesan, Subramanian Gosselin, Mathilde Vaidyanathan, Vinoth Kumar Cabana, Hubert Natural Sciences and Engineering Research Council of Canada 2019 http://dx.doi.org/10.1002/jsde.12266 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fjsde.12266 https://onlinelibrary.wiley.com/doi/pdf/10.1002/jsde.12266 https://onlinelibrary.wiley.com/doi/full-xml/10.1002/jsde.12266 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor Journal of Surfactants and Detergents volume 22, issue 3, page 477-490 ISSN 1097-3958 1558-9293 journal-article 2019 crwiley https://doi.org/10.1002/jsde.12266 2024-05-03T11:02:59Z Abstract In the present study, Candida antarctica lipase B was immobilized on amine‐functionalized silica microspheres as cross‐linked enzyme aggregates (CLEA) and utilized for the biomanufacturing of rhamnolipids (RL). Lipase CLEA synthesized under optimized conditions of 2.0:1.0 by volume of silica microsphere/enzyme concentration, a 1.0:2.5 (v/v) ratio of enzyme/2‐propanol, 7 mM glutaraldehyde concentration, when incubated at pH 9.0 and 40 °C, for a cross‐linking time of 30 min were observed to exhibit superior biocatalytic properties and a maximum enzyme load of 770 U g −1 . Lipase CLEA exhibited enhanced pH stability in acidic and alkaline media and increased temperature resistance as compared to free lipase. Both free and CLEA lipases were used to synthesize RL in different solvent systems. After 12 h, from initiation of the esterification, the degree of esterification (molar conversion yield) reached 46% and 71% in the batch mode. 1 H and 13 C nuclear magnetic resonance (NMR) and high‐performance liquid chromatographic (HPLC) analysis confirm RL production by CLEA lipase. The CLEA showed greater confrontation to enzyme‐mediated bioprocess approach as compared to its soluble counterpart and exhibited excellent RL production and catalytic activity even after its tenth successive reuse. Article in Journal/Newspaper Antarc* Antarctica Wiley Online Library Journal of Surfactants and Detergents 22 3 477 490 |
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Wiley Online Library |
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crwiley |
language |
English |
description |
Abstract In the present study, Candida antarctica lipase B was immobilized on amine‐functionalized silica microspheres as cross‐linked enzyme aggregates (CLEA) and utilized for the biomanufacturing of rhamnolipids (RL). Lipase CLEA synthesized under optimized conditions of 2.0:1.0 by volume of silica microsphere/enzyme concentration, a 1.0:2.5 (v/v) ratio of enzyme/2‐propanol, 7 mM glutaraldehyde concentration, when incubated at pH 9.0 and 40 °C, for a cross‐linking time of 30 min were observed to exhibit superior biocatalytic properties and a maximum enzyme load of 770 U g −1 . Lipase CLEA exhibited enhanced pH stability in acidic and alkaline media and increased temperature resistance as compared to free lipase. Both free and CLEA lipases were used to synthesize RL in different solvent systems. After 12 h, from initiation of the esterification, the degree of esterification (molar conversion yield) reached 46% and 71% in the batch mode. 1 H and 13 C nuclear magnetic resonance (NMR) and high‐performance liquid chromatographic (HPLC) analysis confirm RL production by CLEA lipase. The CLEA showed greater confrontation to enzyme‐mediated bioprocess approach as compared to its soluble counterpart and exhibited excellent RL production and catalytic activity even after its tenth successive reuse. |
author2 |
Natural Sciences and Engineering Research Council of Canada |
format |
Article in Journal/Newspaper |
author |
Rathankumar, Abiram Karanam SaiLavanyaa, Sundar Saikia, Kongkona Gururajan, Anusha Sivanesan, Subramanian Gosselin, Mathilde Vaidyanathan, Vinoth Kumar Cabana, Hubert |
spellingShingle |
Rathankumar, Abiram Karanam SaiLavanyaa, Sundar Saikia, Kongkona Gururajan, Anusha Sivanesan, Subramanian Gosselin, Mathilde Vaidyanathan, Vinoth Kumar Cabana, Hubert Systemic Concocting of Cross‐Linked Enzyme Aggregates of Candida antarctica Lipase B (Novozyme 435) for the Biomanufacturing of Rhamnolipids |
author_facet |
Rathankumar, Abiram Karanam SaiLavanyaa, Sundar Saikia, Kongkona Gururajan, Anusha Sivanesan, Subramanian Gosselin, Mathilde Vaidyanathan, Vinoth Kumar Cabana, Hubert |
author_sort |
Rathankumar, Abiram Karanam |
title |
Systemic Concocting of Cross‐Linked Enzyme Aggregates of Candida antarctica Lipase B (Novozyme 435) for the Biomanufacturing of Rhamnolipids |
title_short |
Systemic Concocting of Cross‐Linked Enzyme Aggregates of Candida antarctica Lipase B (Novozyme 435) for the Biomanufacturing of Rhamnolipids |
title_full |
Systemic Concocting of Cross‐Linked Enzyme Aggregates of Candida antarctica Lipase B (Novozyme 435) for the Biomanufacturing of Rhamnolipids |
title_fullStr |
Systemic Concocting of Cross‐Linked Enzyme Aggregates of Candida antarctica Lipase B (Novozyme 435) for the Biomanufacturing of Rhamnolipids |
title_full_unstemmed |
Systemic Concocting of Cross‐Linked Enzyme Aggregates of Candida antarctica Lipase B (Novozyme 435) for the Biomanufacturing of Rhamnolipids |
title_sort |
systemic concocting of cross‐linked enzyme aggregates of candida antarctica lipase b (novozyme 435) for the biomanufacturing of rhamnolipids |
publisher |
Wiley |
publishDate |
2019 |
url |
http://dx.doi.org/10.1002/jsde.12266 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fjsde.12266 https://onlinelibrary.wiley.com/doi/pdf/10.1002/jsde.12266 https://onlinelibrary.wiley.com/doi/full-xml/10.1002/jsde.12266 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Journal of Surfactants and Detergents volume 22, issue 3, page 477-490 ISSN 1097-3958 1558-9293 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1002/jsde.12266 |
container_title |
Journal of Surfactants and Detergents |
container_volume |
22 |
container_issue |
3 |
container_start_page |
477 |
op_container_end_page |
490 |
_version_ |
1800740470910877696 |