Displaying Candida antarctica lipase B on the cell surface of Aspergillus niger as a potential food-grade whole-cell catalyst
Abstract Aspergillus niger is a recognized workhorse used to produce food processing enzymes because of its extraordinarily high protein-producing capacity. We have developed a new cell surface display system de novo in A. niger using expression elements from generally recognized as safe certified m...
Published in: | Journal of Industrial Microbiology and Biotechnology |
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Oxford University Press (OUP)
2014
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Online Access: | http://dx.doi.org/10.1007/s10295-014-1410-y http://link.springer.com/content/pdf/10.1007/s10295-014-1410-y.pdf http://link.springer.com/article/10.1007/s10295-014-1410-y/fulltext.html http://academic.oup.com/jimb/article-pdf/41/4/711/36811146/jimb0711.pdf |
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croxfordunivpr:10.1007/s10295-014-1410-y 2024-09-15T17:47:39+00:00 Displaying Candida antarctica lipase B on the cell surface of Aspergillus niger as a potential food-grade whole-cell catalyst Pan, Zhi-You Yang, Zhi-Ming Pan, Li Zheng, Sui-Ping Han, Shuang-Yan Lin, Ying 2014 http://dx.doi.org/10.1007/s10295-014-1410-y http://link.springer.com/content/pdf/10.1007/s10295-014-1410-y.pdf http://link.springer.com/article/10.1007/s10295-014-1410-y/fulltext.html http://academic.oup.com/jimb/article-pdf/41/4/711/36811146/jimb0711.pdf en eng Oxford University Press (OUP) https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model Journal of Industrial Microbiology and Biotechnology volume 41, issue 4, page 711-720 ISSN 1476-5535 1367-5435 journal-article 2014 croxfordunivpr https://doi.org/10.1007/s10295-014-1410-y 2024-07-29T04:22:41Z Abstract Aspergillus niger is a recognized workhorse used to produce food processing enzymes because of its extraordinarily high protein-producing capacity. We have developed a new cell surface display system de novo in A. niger using expression elements from generally recognized as safe certified microorganisms. Candida antarctica lipase B (CALB), a widely used hydrolase, was fused to an endogenous cell wall mannoprotein, CwpA, and functionally displayed on the cell surface. Localization of CALB was confirmed by enzymatic assay and immunofluorescence analysis using laser scanning confocal microscopy. After induction by maltose for 45 h, the hydrolytic activity and synthesis activity of A. niger mycelium-surface displayed CALB (AN-CALB) reached 400 and 240 U/g dry cell, respectively. AN-CALB was successfully used as a whole-cell catalyst for the enzymatic production of ethyl esters from a series of fatty acids of different chain lengths and ethanol. In a solvent-free system, AN-CALB showed great synthetic activity and afforded high substrate mole conversions, which amounted to 87 % for ethyl hexanoate after 2 h, 89 % for ethyl laurate after 2 h, and 84 % for ethyl stearate after 3 h. These results suggested that CwpA can act as an efficient anchoring motif for displaying enzyme on A. niger, and AN-CALB is a robust, green, and cost-effective alternative food-grade whole-cell catalyst to commercial lipase. Article in Journal/Newspaper Antarc* Antarctica Oxford University Press Journal of Industrial Microbiology and Biotechnology 41 4 711 720 |
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Oxford University Press |
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croxfordunivpr |
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English |
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Abstract Aspergillus niger is a recognized workhorse used to produce food processing enzymes because of its extraordinarily high protein-producing capacity. We have developed a new cell surface display system de novo in A. niger using expression elements from generally recognized as safe certified microorganisms. Candida antarctica lipase B (CALB), a widely used hydrolase, was fused to an endogenous cell wall mannoprotein, CwpA, and functionally displayed on the cell surface. Localization of CALB was confirmed by enzymatic assay and immunofluorescence analysis using laser scanning confocal microscopy. After induction by maltose for 45 h, the hydrolytic activity and synthesis activity of A. niger mycelium-surface displayed CALB (AN-CALB) reached 400 and 240 U/g dry cell, respectively. AN-CALB was successfully used as a whole-cell catalyst for the enzymatic production of ethyl esters from a series of fatty acids of different chain lengths and ethanol. In a solvent-free system, AN-CALB showed great synthetic activity and afforded high substrate mole conversions, which amounted to 87 % for ethyl hexanoate after 2 h, 89 % for ethyl laurate after 2 h, and 84 % for ethyl stearate after 3 h. These results suggested that CwpA can act as an efficient anchoring motif for displaying enzyme on A. niger, and AN-CALB is a robust, green, and cost-effective alternative food-grade whole-cell catalyst to commercial lipase. |
format |
Article in Journal/Newspaper |
author |
Pan, Zhi-You Yang, Zhi-Ming Pan, Li Zheng, Sui-Ping Han, Shuang-Yan Lin, Ying |
spellingShingle |
Pan, Zhi-You Yang, Zhi-Ming Pan, Li Zheng, Sui-Ping Han, Shuang-Yan Lin, Ying Displaying Candida antarctica lipase B on the cell surface of Aspergillus niger as a potential food-grade whole-cell catalyst |
author_facet |
Pan, Zhi-You Yang, Zhi-Ming Pan, Li Zheng, Sui-Ping Han, Shuang-Yan Lin, Ying |
author_sort |
Pan, Zhi-You |
title |
Displaying Candida antarctica lipase B on the cell surface of Aspergillus niger as a potential food-grade whole-cell catalyst |
title_short |
Displaying Candida antarctica lipase B on the cell surface of Aspergillus niger as a potential food-grade whole-cell catalyst |
title_full |
Displaying Candida antarctica lipase B on the cell surface of Aspergillus niger as a potential food-grade whole-cell catalyst |
title_fullStr |
Displaying Candida antarctica lipase B on the cell surface of Aspergillus niger as a potential food-grade whole-cell catalyst |
title_full_unstemmed |
Displaying Candida antarctica lipase B on the cell surface of Aspergillus niger as a potential food-grade whole-cell catalyst |
title_sort |
displaying candida antarctica lipase b on the cell surface of aspergillus niger as a potential food-grade whole-cell catalyst |
publisher |
Oxford University Press (OUP) |
publishDate |
2014 |
url |
http://dx.doi.org/10.1007/s10295-014-1410-y http://link.springer.com/content/pdf/10.1007/s10295-014-1410-y.pdf http://link.springer.com/article/10.1007/s10295-014-1410-y/fulltext.html http://academic.oup.com/jimb/article-pdf/41/4/711/36811146/jimb0711.pdf |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Journal of Industrial Microbiology and Biotechnology volume 41, issue 4, page 711-720 ISSN 1476-5535 1367-5435 |
op_rights |
https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model |
op_doi |
https://doi.org/10.1007/s10295-014-1410-y |
container_title |
Journal of Industrial Microbiology and Biotechnology |
container_volume |
41 |
container_issue |
4 |
container_start_page |
711 |
op_container_end_page |
720 |
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1810497115081670656 |