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Catalysts 2017, 7(4), 115; doi:10.3390/catal7040115

Lipase-Mediated Amidation of Anilines with 1,3-Diketones via C–C Bond Cleavage

1
Key Laboratory of Molecular Enzymology and Engineering of Ministry of Education, School of Life Sciences, Jilin University, 2699 Qianjin Street, Changchun 130000, China
2
State Key Laborarory of Supramolecular Structure and Materials, Jilin University, 2699 Qianjin Street, Changchun 130000, China
3
China-Japan Union Hospital of Jilin University, 126 Xiantai Street, Changchun 130000, China
*
Authors to whom correspondence should be addressed.
Academic Editor: David D. Boehr
Received: 9 March 2017 / Revised: 10 April 2017 / Accepted: 12 April 2017 / Published: 14 April 2017
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Abstract

In this work, an efficient and green lipase-mediated technique has been mined for the amidation of anilines with 1,3-diketones via C–C bond cleavage. Under the optimal conditions, high yields (64.3%–96.2%) could be obtained when Novozym 435 was used as the catalyst. Furthermore, Novozym 435 exhibited a satisfying reusability and more than 80% of yield can be obtained after seven cycles. This work provides a more rapid and mild strategy for amide synthesis with high yield and expands the application of enzyme in organic synthesis. View Full-Text
Keywords: lipase; promiscuity; amidation; 1,3-diketones; C–C bond cleavage lipase; promiscuity; amidation; 1,3-diketones; C–C bond cleavage
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Zhang, L.; Li, F.; Wang, C.; Zheng, L.; Wang, Z.; Zhao, R.; Wang, L. Lipase-Mediated Amidation of Anilines with 1,3-Diketones via C–C Bond Cleavage. Catalysts 2017, 7, 115.

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