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Open AccessCommunication

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

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Key Laboratory of Molecular Enzymology and Engineering of Ministry of Education, School of Life Sciences, Jilin University, 2699 Qianjin Street, Changchun 130000, China
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State Key Laborarory of Supramolecular Structure and Materials, Jilin University, 2699 Qianjin Street, Changchun 130000, China
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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
Catalysts 2017, 7(4), 115; https://doi.org/10.3390/catal7040115
Received: 9 March 2017 / Revised: 10 April 2017 / Accepted: 12 April 2017 / Published: 14 April 2017
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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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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