Identification of d-carbamoylase for biocatalytic cascade synthesis of d-tryptophan featuring high enantioselectivity

Identification of d-carbamoylase for biocatalytic cascade synthesis of d-tryptophan featuring... Bioresource Technology 249 (2018) 720–728 Contents lists available at ScienceDirect Bioresource Technology journal homepage: www.elsevier.com/locate/biortech Identification of D-carbamoylase for biocatalytic cascade synthesis of D- tryptophan featuring high enantioselectivity Yafei Liu, Guochao Xu, Ruizhi Han, Jinjun Dong, Ye Ni The Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi 214122, Jiangsu, China GR APHICAL A BSTRACT ARTICLE I NFO ABSTRACT Keywords: In this study, an enantioselective D-carbamoylase (AcHyuC) was identified from Arthrobacter crystallopoietes with D-Carbamoylase optimum pH of 8.5, much more compatible with hydantoinase process than other reported D-N-carbamoylases. D-Tryptophan AcHyuC has a substrate preference for aromatic carbamoyl-compounds. The dynamic kinetic resolution (DKR) DKR cascade cascade was developed by combining this AcHyuC with hydantoin racemase from Arthrobacter aurescens Hydantoinase process (AaHyuA) and D-hydantoinase from Agrobacterium tumefaciens (AtHyuH) for enantioselective resolution of L- Arthrobacter crystallopoietes indolylmethylhydantoin into D-Trp. The optimum pH of DKR cascade reaction was determined to be 8.0, and PEG 400 could facilitate the reaction. As much as 80 mM L-indolylmethylhydantoin could be fully converted to D- −1 −1 Trp within 12 h at 0.5 L scale, with 99.4% yield, > 99.9% e.e. and productivity of 36.6 g L d . This study provides http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Bioresource Technology Elsevier

Identification of d-carbamoylase for biocatalytic cascade synthesis of d-tryptophan featuring high enantioselectivity

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Publisher
Elsevier
Copyright
Copyright © 2017 Elsevier Ltd
ISSN
0960-8524
D.O.I.
10.1016/j.biortech.2017.09.162
Publisher site
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Abstract

Bioresource Technology 249 (2018) 720–728 Contents lists available at ScienceDirect Bioresource Technology journal homepage: www.elsevier.com/locate/biortech Identification of D-carbamoylase for biocatalytic cascade synthesis of D- tryptophan featuring high enantioselectivity Yafei Liu, Guochao Xu, Ruizhi Han, Jinjun Dong, Ye Ni The Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi 214122, Jiangsu, China GR APHICAL A BSTRACT ARTICLE I NFO ABSTRACT Keywords: In this study, an enantioselective D-carbamoylase (AcHyuC) was identified from Arthrobacter crystallopoietes with D-Carbamoylase optimum pH of 8.5, much more compatible with hydantoinase process than other reported D-N-carbamoylases. D-Tryptophan AcHyuC has a substrate preference for aromatic carbamoyl-compounds. The dynamic kinetic resolution (DKR) DKR cascade cascade was developed by combining this AcHyuC with hydantoin racemase from Arthrobacter aurescens Hydantoinase process (AaHyuA) and D-hydantoinase from Agrobacterium tumefaciens (AtHyuH) for enantioselective resolution of L- Arthrobacter crystallopoietes indolylmethylhydantoin into D-Trp. The optimum pH of DKR cascade reaction was determined to be 8.0, and PEG 400 could facilitate the reaction. As much as 80 mM L-indolylmethylhydantoin could be fully converted to D- −1 −1 Trp within 12 h at 0.5 L scale, with 99.4% yield, > 99.9% e.e. and productivity of 36.6 g L d . This study provides

Journal

Bioresource TechnologyElsevier

Published: Feb 1, 2018

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