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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Main Authors: Chenghua Wang, Ran Zhang, Yu Sun, You Wen, Xiaoling Liu, Xinhui Xing
Format: Article
Language:English
Published: Tsinghua University Press 2023-07-01
Series:Food Science and Human Wellness
Subjects:
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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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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