Creating an Efficient Methanol‐Stable Biocatalyst by Protein and Immobilization Engineering Steps towards Efficient Biosynthesis of Biodiesel
Abstract Two ternary sol–gel matrices, an octyltriethoxysilane‐based aliphatic matrix and a phenyltriethoxysilane (PTEOS)‐based aromatic matrix, were used to immobilize a methanol‐stable variant of lipase from Geobacillus stearothermophilus T6 for the synthesis of biodiesel from waste oil. Superior...
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crwiley:10.1002/cssc.201601158 2024-09-15T17:42:30+00:00 Creating an Efficient Methanol‐Stable Biocatalyst by Protein and Immobilization Engineering Steps towards Efficient Biosynthesis of Biodiesel Gihaz, Shalev Weiser, Diána Dror, Adi Sátorhelyi, Péter Jerabek‐Willemsen, Moran Poppe, László Fishman, Ayelet 2016 http://dx.doi.org/10.1002/cssc.201601158 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fcssc.201601158 http://onlinelibrary.wiley.com/wol1/doi/10.1002/cssc.201601158/fullpdf en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor ChemSusChem volume 9, issue 22, page 3161-3170 ISSN 1864-5631 1864-564X journal-article 2016 crwiley https://doi.org/10.1002/cssc.201601158 2024-08-30T04:09:32Z Abstract Two ternary sol–gel matrices, an octyltriethoxysilane‐based aliphatic matrix and a phenyltriethoxysilane (PTEOS)‐based aromatic matrix, were used to immobilize a methanol‐stable variant of lipase from Geobacillus stearothermophilus T6 for the synthesis of biodiesel from waste oil. Superior thermal stability of the mutant versus the wildtype in methanol was confirmed by intrinsic protein fluorescence measurements. The influence of skim milk and soluble E. coli lysate proteins as bulking and stabilizing agents in conjunction with sol–gel entrapment were investigated. E. coli lysate proteins were better stabilizing agents of the purified lipase mutant than skim milk, as evidenced by reverse engineering of the aromatic‐based system. This was also shown for commercial Candida antarctica lipase B (CaLB) and Thermomyces lanuginosus lipase (TLL). Uniform, dense, and nonaggregated particles imaged by scanning electron microscopy and a small particle size of 13 μm pertaining to the system comprising PTEOS and E. coli lysate proteins correlated well with high esterification activity. Combining protein and immobilization engineering resulted in a durable biocatalyst with efficient recycling ability and high biodiesel conversion rates. Article in Journal/Newspaper Antarc* Antarctica Wiley Online Library ChemSusChem 9 22 3161 3170 |
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Wiley Online Library |
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English |
description |
Abstract Two ternary sol–gel matrices, an octyltriethoxysilane‐based aliphatic matrix and a phenyltriethoxysilane (PTEOS)‐based aromatic matrix, were used to immobilize a methanol‐stable variant of lipase from Geobacillus stearothermophilus T6 for the synthesis of biodiesel from waste oil. Superior thermal stability of the mutant versus the wildtype in methanol was confirmed by intrinsic protein fluorescence measurements. The influence of skim milk and soluble E. coli lysate proteins as bulking and stabilizing agents in conjunction with sol–gel entrapment were investigated. E. coli lysate proteins were better stabilizing agents of the purified lipase mutant than skim milk, as evidenced by reverse engineering of the aromatic‐based system. This was also shown for commercial Candida antarctica lipase B (CaLB) and Thermomyces lanuginosus lipase (TLL). Uniform, dense, and nonaggregated particles imaged by scanning electron microscopy and a small particle size of 13 μm pertaining to the system comprising PTEOS and E. coli lysate proteins correlated well with high esterification activity. Combining protein and immobilization engineering resulted in a durable biocatalyst with efficient recycling ability and high biodiesel conversion rates. |
format |
Article in Journal/Newspaper |
author |
Gihaz, Shalev Weiser, Diána Dror, Adi Sátorhelyi, Péter Jerabek‐Willemsen, Moran Poppe, László Fishman, Ayelet |
spellingShingle |
Gihaz, Shalev Weiser, Diána Dror, Adi Sátorhelyi, Péter Jerabek‐Willemsen, Moran Poppe, László Fishman, Ayelet Creating an Efficient Methanol‐Stable Biocatalyst by Protein and Immobilization Engineering Steps towards Efficient Biosynthesis of Biodiesel |
author_facet |
Gihaz, Shalev Weiser, Diána Dror, Adi Sátorhelyi, Péter Jerabek‐Willemsen, Moran Poppe, László Fishman, Ayelet |
author_sort |
Gihaz, Shalev |
title |
Creating an Efficient Methanol‐Stable Biocatalyst by Protein and Immobilization Engineering Steps towards Efficient Biosynthesis of Biodiesel |
title_short |
Creating an Efficient Methanol‐Stable Biocatalyst by Protein and Immobilization Engineering Steps towards Efficient Biosynthesis of Biodiesel |
title_full |
Creating an Efficient Methanol‐Stable Biocatalyst by Protein and Immobilization Engineering Steps towards Efficient Biosynthesis of Biodiesel |
title_fullStr |
Creating an Efficient Methanol‐Stable Biocatalyst by Protein and Immobilization Engineering Steps towards Efficient Biosynthesis of Biodiesel |
title_full_unstemmed |
Creating an Efficient Methanol‐Stable Biocatalyst by Protein and Immobilization Engineering Steps towards Efficient Biosynthesis of Biodiesel |
title_sort |
creating an efficient methanol‐stable biocatalyst by protein and immobilization engineering steps towards efficient biosynthesis of biodiesel |
publisher |
Wiley |
publishDate |
2016 |
url |
http://dx.doi.org/10.1002/cssc.201601158 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fcssc.201601158 http://onlinelibrary.wiley.com/wol1/doi/10.1002/cssc.201601158/fullpdf |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
ChemSusChem volume 9, issue 22, page 3161-3170 ISSN 1864-5631 1864-564X |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1002/cssc.201601158 |
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ChemSusChem |
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9 |
container_issue |
22 |
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3161 |
op_container_end_page |
3170 |
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1810489092566155264 |