A novel enzymatic approach in the production of food with low purine content using Arxula adeninivorans endogenous and recombinant purine degradative enzymes
The purine degradation pathway in humans ends with uric acid, which has low water solubility. When the production of uric acid is increased either by elevated purine intake or by impaired kidney function, uric acid will accumulate in the blood (hyperuricemia). This increases the risk of gout, a dise...
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| Veröffentlicht in: | Bioengineered 2015-01, Vol.6 (1), p.20-25 |
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| creator | Jankowska, Dagmara A Trautwein-Schult, Anke Cordes, Arno Bode, Rüdiger Baronian, Keith Kunze, Gotthard |
| description | The purine degradation pathway in humans ends with uric acid, which has low water solubility. When the production of uric acid is increased either by elevated purine intake or by impaired kidney function, uric acid will accumulate in the blood (hyperuricemia). This increases the risk of gout, a disease described in humans for at least 1000 years. Many lower organisms, such as the yeast Arxula adeninivorans, possess the enzyme, urate oxidase that converts uric acid to 5-hydroxyisourate, thus preventing uric acid accumulation. We have examined the complete purine degradation pathway in A. adeninivorans and analyzed enzymes involved. Recombinant adenine deaminase, guanine deaminase, urate oxidase and endogenous xanthine oxidoreductase have been investigated as potential additives to degrade purines in the food. Here, we review the current model of the purine degradation pathway of A. adeninivorans and present an overview of proposed enzyme system with perspectives for its further development. |
| doi_str_mv | 10.4161/21655979.2014.991667 |
| format | Article |
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When the production of uric acid is increased either by elevated purine intake or by impaired kidney function, uric acid will accumulate in the blood (hyperuricemia). This increases the risk of gout, a disease described in humans for at least 1000 years. Many lower organisms, such as the yeast Arxula adeninivorans, possess the enzyme, urate oxidase that converts uric acid to 5-hydroxyisourate, thus preventing uric acid accumulation. We have examined the complete purine degradation pathway in A. adeninivorans and analyzed enzymes involved. Recombinant adenine deaminase, guanine deaminase, urate oxidase and endogenous xanthine oxidoreductase have been investigated as potential additives to degrade purines in the food. Here, we review the current model of the purine degradation pathway of A. adeninivorans and present an overview of proposed enzyme system with perspectives for its further development.</description><identifier>ISSN: 2165-5979</identifier><identifier>EISSN: 2165-5987</identifier><identifier>DOI: 10.4161/21655979.2014.991667</identifier><identifier>PMID: 25513995</identifier><language>eng</language><publisher>United States: Taylor & Francis</publisher><subject>Arxula adeninivorans ; enzymes ; Food Additives - metabolism ; food treatment ; Fungal Proteins - genetics ; Fungal Proteins - metabolism ; gout ; hyperuricemia ; purine degradation pathway ; purines ; Purines - metabolism ; Reviews ; Saccharomycetales - enzymology ; Saccharomycetales - genetics ; Saccharomycetales - metabolism ; Urate Oxidase - genetics ; Urate Oxidase - metabolism ; yeast</subject><ispartof>Bioengineered, 2015-01, Vol.6 (1), p.20-25</ispartof><rights>2015 Taylor & Francis Group, LLC 2015</rights><rights>2015 Taylor & Francis Group, LLC 2015 Taylor & Francis Group, LLC</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c418t-5b55bc7f14e4156dad91491c90ae3d398cb3f4f0921c22c7e9d40ef49c1b81cc3</citedby><cites>FETCH-LOGICAL-c418t-5b55bc7f14e4156dad91491c90ae3d398cb3f4f0921c22c7e9d40ef49c1b81cc3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4601196/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4601196/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25513995$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jankowska, Dagmara A</creatorcontrib><creatorcontrib>Trautwein-Schult, Anke</creatorcontrib><creatorcontrib>Cordes, Arno</creatorcontrib><creatorcontrib>Bode, Rüdiger</creatorcontrib><creatorcontrib>Baronian, Keith</creatorcontrib><creatorcontrib>Kunze, Gotthard</creatorcontrib><title>A novel enzymatic approach in the production of food with low purine content using Arxula adeninivorans endogenous and recombinant purine degradative enzymes</title><title>Bioengineered</title><addtitle>Bioengineered</addtitle><description>The purine degradation pathway in humans ends with uric acid, which has low water solubility. 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Here, we review the current model of the purine degradation pathway of A. adeninivorans and present an overview of proposed enzyme system with perspectives for its further development.</description><subject>Arxula adeninivorans</subject><subject>enzymes</subject><subject>Food Additives - metabolism</subject><subject>food treatment</subject><subject>Fungal Proteins - genetics</subject><subject>Fungal Proteins - metabolism</subject><subject>gout</subject><subject>hyperuricemia</subject><subject>purine degradation pathway</subject><subject>purines</subject><subject>Purines - metabolism</subject><subject>Reviews</subject><subject>Saccharomycetales - enzymology</subject><subject>Saccharomycetales - genetics</subject><subject>Saccharomycetales - metabolism</subject><subject>Urate Oxidase - genetics</subject><subject>Urate Oxidase - metabolism</subject><subject>yeast</subject><issn>2165-5979</issn><issn>2165-5987</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kcGO0zAQhiMEYlfLvgFCPnJpsRM7iS-gagW7SCtxgbPl2OPWKPEEO2kp78K74irdCi6cbI__-ecffUXxmtE1ZzV7V7JaCNnIdUkZX0vJ6rp5Vlyfyish2-b55d7Iq-I2pe-UUkYrLpr2ZXFVCsEqKcV18XtDAu6hJxB-HQc9eUP0OEbUZkd8INMOSH7Z2UweA0FHHKIlBz_tSI8HMs7RByAGwwRhInPyYUs28efca6ItBB_8HqMOKftb3ELAOREdLIlgcOh80LnrbGJhG7XNEfawpIH0qnjhdJ_g9nzeFN8-ffx697B6_HL_-W7zuDKctdNKdEJ0pnGMA2eittpKxiUzkmqobCVb01WOOypLZsrSNCAtp-C4NKxrmTHVTfF-8R3nbgBr8i5R92qMftDxqFB79e9P8Du1xb3iNWVM1tng7dkg4o8Z0qQGnwz0vQ6QV1aZD-e8riXPUr5ITcSUIrjLGEbVCa56gqtOcNUCN7e9-TvipekJZRZ8WAQ-OIyDPmDsrZr0scfoMgLjk6r-O-IP2QC5hw</recordid><startdate>20150101</startdate><enddate>20150101</enddate><creator>Jankowska, Dagmara A</creator><creator>Trautwein-Schult, Anke</creator><creator>Cordes, Arno</creator><creator>Bode, Rüdiger</creator><creator>Baronian, Keith</creator><creator>Kunze, Gotthard</creator><general>Taylor & Francis</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20150101</creationdate><title>A novel enzymatic approach in the production of food with low purine content using Arxula adeninivorans endogenous and recombinant purine degradative enzymes</title><author>Jankowska, Dagmara A ; Trautwein-Schult, Anke ; Cordes, Arno ; Bode, Rüdiger ; Baronian, Keith ; Kunze, Gotthard</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c418t-5b55bc7f14e4156dad91491c90ae3d398cb3f4f0921c22c7e9d40ef49c1b81cc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Arxula adeninivorans</topic><topic>enzymes</topic><topic>Food Additives - metabolism</topic><topic>food treatment</topic><topic>Fungal Proteins - genetics</topic><topic>Fungal Proteins - metabolism</topic><topic>gout</topic><topic>hyperuricemia</topic><topic>purine degradation pathway</topic><topic>purines</topic><topic>Purines - metabolism</topic><topic>Reviews</topic><topic>Saccharomycetales - enzymology</topic><topic>Saccharomycetales - genetics</topic><topic>Saccharomycetales - metabolism</topic><topic>Urate Oxidase - genetics</topic><topic>Urate Oxidase - metabolism</topic><topic>yeast</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jankowska, Dagmara A</creatorcontrib><creatorcontrib>Trautwein-Schult, Anke</creatorcontrib><creatorcontrib>Cordes, Arno</creatorcontrib><creatorcontrib>Bode, Rüdiger</creatorcontrib><creatorcontrib>Baronian, Keith</creatorcontrib><creatorcontrib>Kunze, Gotthard</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Bioengineered</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jankowska, Dagmara A</au><au>Trautwein-Schult, Anke</au><au>Cordes, Arno</au><au>Bode, Rüdiger</au><au>Baronian, Keith</au><au>Kunze, Gotthard</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A novel enzymatic approach in the production of food with low purine content using Arxula adeninivorans endogenous and recombinant purine degradative enzymes</atitle><jtitle>Bioengineered</jtitle><addtitle>Bioengineered</addtitle><date>2015-01-01</date><risdate>2015</risdate><volume>6</volume><issue>1</issue><spage>20</spage><epage>25</epage><pages>20-25</pages><issn>2165-5979</issn><eissn>2165-5987</eissn><abstract>The purine degradation pathway in humans ends with uric acid, which has low water solubility. When the production of uric acid is increased either by elevated purine intake or by impaired kidney function, uric acid will accumulate in the blood (hyperuricemia). This increases the risk of gout, a disease described in humans for at least 1000 years. Many lower organisms, such as the yeast Arxula adeninivorans, possess the enzyme, urate oxidase that converts uric acid to 5-hydroxyisourate, thus preventing uric acid accumulation. We have examined the complete purine degradation pathway in A. adeninivorans and analyzed enzymes involved. Recombinant adenine deaminase, guanine deaminase, urate oxidase and endogenous xanthine oxidoreductase have been investigated as potential additives to degrade purines in the food. 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| subjects | Arxula adeninivorans enzymes Food Additives - metabolism food treatment Fungal Proteins - genetics Fungal Proteins - metabolism gout hyperuricemia purine degradation pathway purines Purines - metabolism Reviews Saccharomycetales - enzymology Saccharomycetales - genetics Saccharomycetales - metabolism Urate Oxidase - genetics Urate Oxidase - metabolism yeast |
| title | A novel enzymatic approach in the production of food with low purine content using Arxula adeninivorans endogenous and recombinant purine degradative enzymes |
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