Combinatorial co-expression of xanthine dehydrogenase and chaperone XdhC from Acinetobacter baumannii and Rhodobacter capsulatus and their applications in decreasing purine content in food
This study investigated the combinatorial expression of xanthine dehydrogenase (XDH) and chaperone XdhC from Acinetobacter baumannii and Rhodobacter capsulatus and their applications in decreasing purine content in the beer, beef and yeast. Naturally occurring xdhABC gene clusters of A. baumannii CI...
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Language: | English |
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Tsinghua University Press
2023-07-01
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Series: | Food Science and Human Wellness |
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Online Access: | http://www.sciencedirect.com/science/article/pii/S2213453022002543 |
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author | Chenghua Wang Ran Zhang Yu Sun You Wen Xiaoling Liu Xinhui Xing |
author_facet | Chenghua Wang Ran Zhang Yu Sun You Wen Xiaoling Liu Xinhui Xing |
author_sort | Chenghua Wang |
collection | DOAJ |
description | This study investigated the combinatorial expression of xanthine dehydrogenase (XDH) and chaperone XdhC from Acinetobacter baumannii and Rhodobacter capsulatus and their applications in decreasing purine content in the beer, beef and yeast. Naturally occurring xdhABC gene clusters of A. baumannii CICC 10254 and R. capsulatus CGMCC 1.3366 as well as two refactored clusters constructed by exchanging their xdhC genes were overexpressed in Escherichia coli and purified to near homogeneity. RcXDH chaperoned by AbXdhC showed nearly the same catalytic performance as that by RcXdhC, except for the decreased substrate affinity. While the AbXDH co-expressed with RcXdhC displayed enhanced acidic adaptation but weakened catalytic activity. All the XDHs degraded purines in beer, beef and yeast extract effectively, indicating potential applications in low-purine foods to prevent hyperuricemia and gout. The study also presents a method for exploiting the better chaperone XdhC and novel XDHs by functional complement activity using existing XdhCs such as RcXdhC. |
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issn | 2213-4530 |
language | English |
last_indexed | 2024-03-12T05:35:33Z |
publishDate | 2023-07-01 |
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spelling | doaj.art-789ef48b1be54634a4b5436052d565262023-09-03T06:31:08ZengTsinghua University PressFood Science and Human Wellness2213-45302023-07-0112413431350Combinatorial co-expression of xanthine dehydrogenase and chaperone XdhC from Acinetobacter baumannii and Rhodobacter capsulatus and their applications in decreasing purine content in foodChenghua Wang0Ran Zhang1Yu Sun2You Wen3Xiaoling Liu4Xinhui Xing5College of Light Industry and Food Engineering, Guangxi University, Nanning 530004, China; Corresponding author at: College of Light Industry and Food Engineering, Guangxi University, Nanning 530004, China. Fax: +86-771-323-2874.College of Light Industry and Food Engineering, Guangxi University, Nanning 530004, ChinaCollege of Light Industry and Food Engineering, Guangxi University, Nanning 530004, ChinaCollege of Light Industry and Food Engineering, Guangxi University, Nanning 530004, ChinaCollege of Light Industry and Food Engineering, Guangxi University, Nanning 530004, ChinaKey Laboratory of Industrial Biocatalysis, Ministry of Education, Institute of Biochemical Engineering, Department of Chemical Engineering, Tsinghua University, Beijing 100084, ChinaThis study investigated the combinatorial expression of xanthine dehydrogenase (XDH) and chaperone XdhC from Acinetobacter baumannii and Rhodobacter capsulatus and their applications in decreasing purine content in the beer, beef and yeast. Naturally occurring xdhABC gene clusters of A. baumannii CICC 10254 and R. capsulatus CGMCC 1.3366 as well as two refactored clusters constructed by exchanging their xdhC genes were overexpressed in Escherichia coli and purified to near homogeneity. RcXDH chaperoned by AbXdhC showed nearly the same catalytic performance as that by RcXdhC, except for the decreased substrate affinity. While the AbXDH co-expressed with RcXdhC displayed enhanced acidic adaptation but weakened catalytic activity. All the XDHs degraded purines in beer, beef and yeast extract effectively, indicating potential applications in low-purine foods to prevent hyperuricemia and gout. The study also presents a method for exploiting the better chaperone XdhC and novel XDHs by functional complement activity using existing XdhCs such as RcXdhC.http://www.sciencedirect.com/science/article/pii/S2213453022002543Co-expressionLow purine foodUric acidXanthine dehydrogenaseXdhC |
spellingShingle | Chenghua Wang Ran Zhang Yu Sun You Wen Xiaoling Liu Xinhui Xing Combinatorial co-expression of xanthine dehydrogenase and chaperone XdhC from Acinetobacter baumannii and Rhodobacter capsulatus and their applications in decreasing purine content in food Food Science and Human Wellness Co-expression Low purine food Uric acid Xanthine dehydrogenase XdhC |
title | Combinatorial co-expression of xanthine dehydrogenase and chaperone XdhC from Acinetobacter baumannii and Rhodobacter capsulatus and their applications in decreasing purine content in food |
title_full | Combinatorial co-expression of xanthine dehydrogenase and chaperone XdhC from Acinetobacter baumannii and Rhodobacter capsulatus and their applications in decreasing purine content in food |
title_fullStr | Combinatorial co-expression of xanthine dehydrogenase and chaperone XdhC from Acinetobacter baumannii and Rhodobacter capsulatus and their applications in decreasing purine content in food |
title_full_unstemmed | Combinatorial co-expression of xanthine dehydrogenase and chaperone XdhC from Acinetobacter baumannii and Rhodobacter capsulatus and their applications in decreasing purine content in food |
title_short | Combinatorial co-expression of xanthine dehydrogenase and chaperone XdhC from Acinetobacter baumannii and Rhodobacter capsulatus and their applications in decreasing purine content in food |
title_sort | combinatorial co expression of xanthine dehydrogenase and chaperone xdhc from acinetobacter baumannii and rhodobacter capsulatus and their applications in decreasing purine content in food |
topic | Co-expression Low purine food Uric acid Xanthine dehydrogenase XdhC |
url | http://www.sciencedirect.com/science/article/pii/S2213453022002543 |
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