Effects of different expression systems on characterization of adenylate deaminase from Aspergillus oryzae
Adenylate deaminase (AMPD) is an amino hydrolase that catalyzes the irreversible hydrolysis of adenosine monophosphate (AMP) to inosine monophosphate (IMP) and ammonia. In this study, the effect of different hosts on the enzymatic properties of AMPD from Aspergillus oryzae GX-08 was investigated and...
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| Veröffentlicht in: | Bioprocess and biosystems engineering 2020-05, Vol.43 (5), p.919-926 |
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| creator | Ke, Chengzhu Li, Shubo Cui, Yanyan Qiu, Hua Pang, Zongwen |
| description | Adenylate deaminase (AMPD) is an amino hydrolase that catalyzes the irreversible hydrolysis of adenosine monophosphate (AMP) to inosine monophosphate (IMP) and ammonia. In this study, the effect of different hosts on the enzymatic properties of AMPD from
Aspergillus oryzae
GX-08 was investigated and showed that
Bacillus subtilis
WB600 was more suitable for producing AMPD with a higher activity of 2540 U/mL. After purification, the optimal temperature and pH of recombinant AMPD were 55 °C and pH 6.0, respectively, and its activity was significantly enhanced by 10 mM Fe
3+
with an increase of 236%. More importantly, the recombinant AMPD specifically and effectively catalyzed the conversion between AMP and IMP, in which 10 mL of crude AMPD achieved a conversion ratio of 76.4% after 40 min. Therefore,
B. subtilis
WB600 provides a potential platform for producing AMPD with excellent catalytic ability and catalytic specificity. |
| doi_str_mv | 10.1007/s00449-020-02288-7 |
| format | Article |
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Aspergillus oryzae
GX-08 was investigated and showed that
Bacillus subtilis
WB600 was more suitable for producing AMPD with a higher activity of 2540 U/mL. After purification, the optimal temperature and pH of recombinant AMPD were 55 °C and pH 6.0, respectively, and its activity was significantly enhanced by 10 mM Fe
3+
with an increase of 236%. More importantly, the recombinant AMPD specifically and effectively catalyzed the conversion between AMP and IMP, in which 10 mL of crude AMPD achieved a conversion ratio of 76.4% after 40 min. Therefore,
B. subtilis
WB600 provides a potential platform for producing AMPD with excellent catalytic ability and catalytic specificity.</description><identifier>ISSN: 1615-7591</identifier><identifier>EISSN: 1615-7605</identifier><identifier>DOI: 10.1007/s00449-020-02288-7</identifier><identifier>PMID: 32020448</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Adenosine monophosphate ; Ammonia ; AMP ; AMP Deaminase - biosynthesis ; AMP Deaminase - genetics ; Aspergillus oryzae ; Aspergillus oryzae - enzymology ; Aspergillus oryzae - genetics ; Bacillus subtilis - enzymology ; Bacillus subtilis - genetics ; Biotechnology ; Biotechnology & Applied Microbiology ; Chemistry ; Chemistry and Materials Science ; Conversion ; Conversion ratio ; Engineering ; Engineering, Chemical ; Environmental Engineering/Biotechnology ; Food Science ; Fungal Proteins - biosynthesis ; Fungal Proteins - genetics ; Hydrolase ; Industrial and Production Engineering ; Industrial Chemistry/Chemical Engineering ; Inosine monophosphate ; Iron ; Life Sciences & Biomedicine ; pH effects ; Purification ; Recombinant Proteins - biosynthesis ; Recombinant Proteins - genetics ; Research Paper ; Science & Technology ; Technology</subject><ispartof>Bioprocess and biosystems engineering, 2020-05, Vol.43 (5), p.919-926</ispartof><rights>Springer-Verlag GmbH Germany, part of Springer Nature 2020</rights><rights>Springer-Verlag GmbH Germany, part of Springer Nature 2020.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>true</woscitedreferencessubscribed><woscitedreferencescount>3</woscitedreferencescount><woscitedreferencesoriginalsourcerecordid>wos000511050300004</woscitedreferencesoriginalsourcerecordid><citedby>FETCH-LOGICAL-c412t-da69574f310d8fcd361b51178a136861f4048f10753b9d55e61449888c7b88373</citedby><cites>FETCH-LOGICAL-c412t-da69574f310d8fcd361b51178a136861f4048f10753b9d55e61449888c7b88373</cites><orcidid>0000-0002-7313-817X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00449-020-02288-7$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00449-020-02288-7$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>315,781,785,27929,27930,28253,41493,42562,51324</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32020448$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ke, Chengzhu</creatorcontrib><creatorcontrib>Li, Shubo</creatorcontrib><creatorcontrib>Cui, Yanyan</creatorcontrib><creatorcontrib>Qiu, Hua</creatorcontrib><creatorcontrib>Pang, Zongwen</creatorcontrib><title>Effects of different expression systems on characterization of adenylate deaminase from Aspergillus oryzae</title><title>Bioprocess and biosystems engineering</title><addtitle>Bioprocess Biosyst Eng</addtitle><addtitle>BIOPROC BIOSYST ENG</addtitle><addtitle>Bioprocess Biosyst Eng</addtitle><description>Adenylate deaminase (AMPD) is an amino hydrolase that catalyzes the irreversible hydrolysis of adenosine monophosphate (AMP) to inosine monophosphate (IMP) and ammonia. In this study, the effect of different hosts on the enzymatic properties of AMPD from
Aspergillus oryzae
GX-08 was investigated and showed that
Bacillus subtilis
WB600 was more suitable for producing AMPD with a higher activity of 2540 U/mL. After purification, the optimal temperature and pH of recombinant AMPD were 55 °C and pH 6.0, respectively, and its activity was significantly enhanced by 10 mM Fe
3+
with an increase of 236%. More importantly, the recombinant AMPD specifically and effectively catalyzed the conversion between AMP and IMP, in which 10 mL of crude AMPD achieved a conversion ratio of 76.4% after 40 min. Therefore,
B. subtilis
WB600 provides a potential platform for producing AMPD with excellent catalytic ability and catalytic specificity.</description><subject>Adenosine monophosphate</subject><subject>Ammonia</subject><subject>AMP</subject><subject>AMP Deaminase - biosynthesis</subject><subject>AMP Deaminase - genetics</subject><subject>Aspergillus oryzae</subject><subject>Aspergillus oryzae - enzymology</subject><subject>Aspergillus oryzae - genetics</subject><subject>Bacillus subtilis - enzymology</subject><subject>Bacillus subtilis - genetics</subject><subject>Biotechnology</subject><subject>Biotechnology & Applied Microbiology</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Conversion</subject><subject>Conversion ratio</subject><subject>Engineering</subject><subject>Engineering, Chemical</subject><subject>Environmental Engineering/Biotechnology</subject><subject>Food Science</subject><subject>Fungal Proteins - biosynthesis</subject><subject>Fungal Proteins - genetics</subject><subject>Hydrolase</subject><subject>Industrial and Production Engineering</subject><subject>Industrial Chemistry/Chemical Engineering</subject><subject>Inosine monophosphate</subject><subject>Iron</subject><subject>Life Sciences & Biomedicine</subject><subject>pH effects</subject><subject>Purification</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - genetics</subject><subject>Research Paper</subject><subject>Science & Technology</subject><subject>Technology</subject><issn>1615-7591</issn><issn>1615-7605</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>AOWDO</sourceid><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqNkU2LFDEQhhtR3A_9Ax6kwYsgrZWvTua4DKsrLHjRc0inK2uG7mRM0ujsrzezvbuCB_EQUlDPW1S9b9O8IvCeAMgPGYDzTQcU6qNKdfJJc0p6IjrZg3j6UIsNOWnOct4BEKEoPG9OGK0iztVps7t0Dm3JbXTt6GudMJQWf-0T5uxjaPMhF5xrP7T2u0nGFkz-1pRjr2rMiOEwmYLtiGb2wWRsXYpze5H3mG78NC1Vmw63Bl80z5yZMr68_8-bbx8vv26vuusvnz5vL647ywkt3Wj6jZDcMQKjcnZkPRkEIVIZwnrVE8eBK0dACjZsRiGwJ9UFpZSVg1JMsvPm7Tp3n-KPBXPRs88Wp8kEjEvWlAnCFaGCVfTNX-guLinU7SqlhFKcyuNAulI2xZwTOr1PfjbpoAnoYxJ6TUJXU_VdEvooen0_ehlmHB8lD9ZXQK3ATxyiy9ZjsPiIAUA9GgSwWgHf-nJn-TYuoVTpu_-XVpqtdK5EuMH058h_7P8bXNW0EA</recordid><startdate>20200501</startdate><enddate>20200501</enddate><creator>Ke, Chengzhu</creator><creator>Li, Shubo</creator><creator>Cui, Yanyan</creator><creator>Qiu, Hua</creator><creator>Pang, Zongwen</creator><general>Springer Berlin Heidelberg</general><general>Springer Nature</general><general>Springer Nature B.V</general><scope>AOWDO</scope><scope>BLEPL</scope><scope>DTL</scope><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>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-7313-817X</orcidid></search><sort><creationdate>20200501</creationdate><title>Effects of different expression systems on characterization of adenylate deaminase from Aspergillus oryzae</title><author>Ke, Chengzhu ; Li, Shubo ; Cui, Yanyan ; Qiu, Hua ; Pang, Zongwen</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c412t-da69574f310d8fcd361b51178a136861f4048f10753b9d55e61449888c7b88373</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Adenosine monophosphate</topic><topic>Ammonia</topic><topic>AMP</topic><topic>AMP Deaminase - biosynthesis</topic><topic>AMP Deaminase - genetics</topic><topic>Aspergillus oryzae</topic><topic>Aspergillus oryzae - enzymology</topic><topic>Aspergillus oryzae - genetics</topic><topic>Bacillus subtilis - enzymology</topic><topic>Bacillus subtilis - genetics</topic><topic>Biotechnology</topic><topic>Biotechnology & Applied Microbiology</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Conversion</topic><topic>Conversion ratio</topic><topic>Engineering</topic><topic>Engineering, Chemical</topic><topic>Environmental Engineering/Biotechnology</topic><topic>Food Science</topic><topic>Fungal Proteins - biosynthesis</topic><topic>Fungal Proteins - genetics</topic><topic>Hydrolase</topic><topic>Industrial and Production Engineering</topic><topic>Industrial Chemistry/Chemical Engineering</topic><topic>Inosine monophosphate</topic><topic>Iron</topic><topic>Life Sciences & Biomedicine</topic><topic>pH effects</topic><topic>Purification</topic><topic>Recombinant Proteins - 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Academic</collection><jtitle>Bioprocess and biosystems engineering</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ke, Chengzhu</au><au>Li, Shubo</au><au>Cui, Yanyan</au><au>Qiu, Hua</au><au>Pang, Zongwen</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effects of different expression systems on characterization of adenylate deaminase from Aspergillus oryzae</atitle><jtitle>Bioprocess and biosystems engineering</jtitle><stitle>Bioprocess Biosyst Eng</stitle><stitle>BIOPROC BIOSYST ENG</stitle><addtitle>Bioprocess Biosyst Eng</addtitle><date>2020-05-01</date><risdate>2020</risdate><volume>43</volume><issue>5</issue><spage>919</spage><epage>926</epage><pages>919-926</pages><issn>1615-7591</issn><eissn>1615-7605</eissn><abstract>Adenylate deaminase (AMPD) is an amino hydrolase that catalyzes the irreversible hydrolysis of adenosine monophosphate (AMP) to inosine monophosphate (IMP) and ammonia. In this study, the effect of different hosts on the enzymatic properties of AMPD from
Aspergillus oryzae
GX-08 was investigated and showed that
Bacillus subtilis
WB600 was more suitable for producing AMPD with a higher activity of 2540 U/mL. After purification, the optimal temperature and pH of recombinant AMPD were 55 °C and pH 6.0, respectively, and its activity was significantly enhanced by 10 mM Fe
3+
with an increase of 236%. More importantly, the recombinant AMPD specifically and effectively catalyzed the conversion between AMP and IMP, in which 10 mL of crude AMPD achieved a conversion ratio of 76.4% after 40 min. Therefore,
B. subtilis
WB600 provides a potential platform for producing AMPD with excellent catalytic ability and catalytic specificity.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>32020448</pmid><doi>10.1007/s00449-020-02288-7</doi><tpages>8</tpages><orcidid>https://orcid.org/0000-0002-7313-817X</orcidid></addata></record> |
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| subjects | Adenosine monophosphate Ammonia AMP AMP Deaminase - biosynthesis AMP Deaminase - genetics Aspergillus oryzae Aspergillus oryzae - enzymology Aspergillus oryzae - genetics Bacillus subtilis - enzymology Bacillus subtilis - genetics Biotechnology Biotechnology & Applied Microbiology Chemistry Chemistry and Materials Science Conversion Conversion ratio Engineering Engineering, Chemical Environmental Engineering/Biotechnology Food Science Fungal Proteins - biosynthesis Fungal Proteins - genetics Hydrolase Industrial and Production Engineering Industrial Chemistry/Chemical Engineering Inosine monophosphate Iron Life Sciences & Biomedicine pH effects Purification Recombinant Proteins - biosynthesis Recombinant Proteins - genetics Research Paper Science & Technology Technology |
| title | Effects of different expression systems on characterization of adenylate deaminase from Aspergillus oryzae |
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