Purification and characterization of d-allulose 3-epimerase derived from Arthrobacter globiformis M30, a GRAS microorganism
An enzyme that catalyzes C-3 epimerization between d-fructose and d-allulose was found in Arthrobacter globiformis strain M30. Arthrobacter species have long been used in the food industry and are well-known for their high degree of safety. The enzyme was purified by ion exchange and hydrophobic int...
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| Veröffentlicht in: | Journal of bioscience and bioengineering 2017-02, Vol.123 (2), p.170-176 |
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| creator | Yoshihara, Akihide Kozakai, Taro Shintani, Tomoya Matsutani, Ryo Ohtani, Kouhei Iida, Tetsuo Akimitsu, Kazuya Izumori, Ken Gullapalli, Pushpa Kiran |
| description | An enzyme that catalyzes C-3 epimerization between d-fructose and d-allulose was found in Arthrobacter globiformis strain M30. Arthrobacter species have long been used in the food industry and are well-known for their high degree of safety. The enzyme was purified by ion exchange and hydrophobic interaction chromatographies and characterized as a d-allulose 3-epimerase (d-AE). The molecular weight of the purified enzyme was estimated to be 128 kDa with four identical subunits. The enzyme showed maximal activity and thermostability in the presence of Mg2+. The optimal pH and temperature for enzymatic activity were 7.0–8.0 and 70°C, respectively. The enzyme was immobilized to ion exchange resin whereupon it was stable for longer periods than the free enzyme when stored at below 10°C. In the column reaction, the enzyme activity also maintained stability for more than 4 months. Under these conditions, 215 kg of d-allulose produced per liter immobilized enzyme, and this was the highest production yield of d-allulose reported so far. These highly stable properties suggest that this enzyme represents an ideal candidate for the industrial production of d-allulose. |
| doi_str_mv | 10.1016/j.jbiosc.2016.09.004 |
| format | Article |
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Arthrobacter species have long been used in the food industry and are well-known for their high degree of safety. The enzyme was purified by ion exchange and hydrophobic interaction chromatographies and characterized as a d-allulose 3-epimerase (d-AE). The molecular weight of the purified enzyme was estimated to be 128 kDa with four identical subunits. The enzyme showed maximal activity and thermostability in the presence of Mg2+. The optimal pH and temperature for enzymatic activity were 7.0–8.0 and 70°C, respectively. The enzyme was immobilized to ion exchange resin whereupon it was stable for longer periods than the free enzyme when stored at below 10°C. In the column reaction, the enzyme activity also maintained stability for more than 4 months. Under these conditions, 215 kg of d-allulose produced per liter immobilized enzyme, and this was the highest production yield of d-allulose reported so far. These highly stable properties suggest that this enzyme represents an ideal candidate for the industrial production of d-allulose.</description><identifier>ISSN: 1389-1723</identifier><identifier>EISSN: 1347-4421</identifier><identifier>DOI: 10.1016/j.jbiosc.2016.09.004</identifier><identifier>PMID: 27713017</identifier><language>eng</language><publisher>Japan: Elsevier B.V</publisher><subject>Arthrobacter - chemistry ; Arthrobacter - enzymology ; Arthrobacter globiformis M30 ; d-Allulose ; d-Allulose 3-epimerase ; Enzyme Stability ; Fructose - biosynthesis ; Fructose - metabolism ; Hydrogen-Ion Concentration ; Immobilized d-AE ; Kinetics ; Magnesium ; Metabolic Engineering ; Molecular Weight ; Racemases and Epimerases - analysis ; Racemases and Epimerases - isolation & purification ; Racemases and Epimerases - metabolism ; Temperature</subject><ispartof>Journal of bioscience and bioengineering, 2017-02, Vol.123 (2), p.170-176</ispartof><rights>2016 The Society for Biotechnology, Japan</rights><rights>Copyright © 2016 The Society for Biotechnology, Japan. Published by Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c407t-26aae3c7954306c736f703ea53d0488ddf129038cf078f74d2acb1c59c8aaa873</citedby><cites>FETCH-LOGICAL-c407t-26aae3c7954306c736f703ea53d0488ddf129038cf078f74d2acb1c59c8aaa873</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.jbiosc.2016.09.004$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3541,27915,27916,45986</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27713017$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yoshihara, Akihide</creatorcontrib><creatorcontrib>Kozakai, Taro</creatorcontrib><creatorcontrib>Shintani, Tomoya</creatorcontrib><creatorcontrib>Matsutani, Ryo</creatorcontrib><creatorcontrib>Ohtani, Kouhei</creatorcontrib><creatorcontrib>Iida, Tetsuo</creatorcontrib><creatorcontrib>Akimitsu, Kazuya</creatorcontrib><creatorcontrib>Izumori, Ken</creatorcontrib><creatorcontrib>Gullapalli, Pushpa Kiran</creatorcontrib><title>Purification and characterization of d-allulose 3-epimerase derived from Arthrobacter globiformis M30, a GRAS microorganism</title><title>Journal of bioscience and bioengineering</title><addtitle>J Biosci Bioeng</addtitle><description>An enzyme that catalyzes C-3 epimerization between d-fructose and d-allulose was found in Arthrobacter globiformis strain M30. Arthrobacter species have long been used in the food industry and are well-known for their high degree of safety. The enzyme was purified by ion exchange and hydrophobic interaction chromatographies and characterized as a d-allulose 3-epimerase (d-AE). The molecular weight of the purified enzyme was estimated to be 128 kDa with four identical subunits. The enzyme showed maximal activity and thermostability in the presence of Mg2+. The optimal pH and temperature for enzymatic activity were 7.0–8.0 and 70°C, respectively. The enzyme was immobilized to ion exchange resin whereupon it was stable for longer periods than the free enzyme when stored at below 10°C. In the column reaction, the enzyme activity also maintained stability for more than 4 months. Under these conditions, 215 kg of d-allulose produced per liter immobilized enzyme, and this was the highest production yield of d-allulose reported so far. These highly stable properties suggest that this enzyme represents an ideal candidate for the industrial production of d-allulose.</description><subject>Arthrobacter - chemistry</subject><subject>Arthrobacter - enzymology</subject><subject>Arthrobacter globiformis M30</subject><subject>d-Allulose</subject><subject>d-Allulose 3-epimerase</subject><subject>Enzyme Stability</subject><subject>Fructose - biosynthesis</subject><subject>Fructose - metabolism</subject><subject>Hydrogen-Ion Concentration</subject><subject>Immobilized d-AE</subject><subject>Kinetics</subject><subject>Magnesium</subject><subject>Metabolic Engineering</subject><subject>Molecular Weight</subject><subject>Racemases and Epimerases - analysis</subject><subject>Racemases and Epimerases - isolation & purification</subject><subject>Racemases and Epimerases - metabolism</subject><subject>Temperature</subject><issn>1389-1723</issn><issn>1347-4421</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1v1DAQhi1ERT_gHyDkIwcS7NgbOxekVVVapKJWBc7WxB63XiXxYieVgD-PlxSOnDxjPa9n_BDymrOaM96-39W7PsRs66Z0NetqxuQzcsKFVJWUDX9-qHVXcdWIY3Ka844xrpjiL8hxoxQXpTshv26XFHywMIc4UZgctQ-QwM6Yws_1MnrqKhiGZYgZqahwH0ZMUGpXoEd01Kc40m2aH1Ls_0Tp_RD74GMaQ6afBXtHgV7ebb_QMdgUY7qHKeTxJTnyMGR89XSekW8fL76eX1XXN5efzrfXlZVMzVXTAqCwqttIwVqrROsVEwgb4ZjU2jnPm44JbT1T2ivpGrA9t5vOagDQSpyRt-u7-xS_L5hnU9ayOAwwYVyy4VpshFayaQsqV7SsmXNCb_YpjJB-GM7MQbvZmVW7OWg3rDNFe4m9eZqw9CO6f6G_ngvwYQWw_PMxYDLZBpwsupDQzsbF8P8JvwFOF5aY</recordid><startdate>20170201</startdate><enddate>20170201</enddate><creator>Yoshihara, Akihide</creator><creator>Kozakai, Taro</creator><creator>Shintani, Tomoya</creator><creator>Matsutani, Ryo</creator><creator>Ohtani, Kouhei</creator><creator>Iida, Tetsuo</creator><creator>Akimitsu, Kazuya</creator><creator>Izumori, Ken</creator><creator>Gullapalli, Pushpa Kiran</creator><general>Elsevier B.V</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></search><sort><creationdate>20170201</creationdate><title>Purification and characterization of d-allulose 3-epimerase derived from Arthrobacter globiformis M30, a GRAS microorganism</title><author>Yoshihara, Akihide ; Kozakai, Taro ; Shintani, Tomoya ; Matsutani, Ryo ; Ohtani, Kouhei ; Iida, Tetsuo ; Akimitsu, Kazuya ; Izumori, Ken ; Gullapalli, Pushpa Kiran</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c407t-26aae3c7954306c736f703ea53d0488ddf129038cf078f74d2acb1c59c8aaa873</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Arthrobacter - chemistry</topic><topic>Arthrobacter - enzymology</topic><topic>Arthrobacter globiformis M30</topic><topic>d-Allulose</topic><topic>d-Allulose 3-epimerase</topic><topic>Enzyme Stability</topic><topic>Fructose - biosynthesis</topic><topic>Fructose - metabolism</topic><topic>Hydrogen-Ion Concentration</topic><topic>Immobilized d-AE</topic><topic>Kinetics</topic><topic>Magnesium</topic><topic>Metabolic Engineering</topic><topic>Molecular Weight</topic><topic>Racemases and Epimerases - analysis</topic><topic>Racemases and Epimerases - isolation & purification</topic><topic>Racemases and Epimerases - metabolism</topic><topic>Temperature</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yoshihara, Akihide</creatorcontrib><creatorcontrib>Kozakai, Taro</creatorcontrib><creatorcontrib>Shintani, Tomoya</creatorcontrib><creatorcontrib>Matsutani, Ryo</creatorcontrib><creatorcontrib>Ohtani, Kouhei</creatorcontrib><creatorcontrib>Iida, Tetsuo</creatorcontrib><creatorcontrib>Akimitsu, Kazuya</creatorcontrib><creatorcontrib>Izumori, Ken</creatorcontrib><creatorcontrib>Gullapalli, Pushpa Kiran</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><jtitle>Journal of bioscience and bioengineering</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yoshihara, Akihide</au><au>Kozakai, Taro</au><au>Shintani, Tomoya</au><au>Matsutani, Ryo</au><au>Ohtani, Kouhei</au><au>Iida, Tetsuo</au><au>Akimitsu, Kazuya</au><au>Izumori, Ken</au><au>Gullapalli, Pushpa Kiran</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and characterization of d-allulose 3-epimerase derived from Arthrobacter globiformis M30, a GRAS microorganism</atitle><jtitle>Journal of bioscience and bioengineering</jtitle><addtitle>J Biosci Bioeng</addtitle><date>2017-02-01</date><risdate>2017</risdate><volume>123</volume><issue>2</issue><spage>170</spage><epage>176</epage><pages>170-176</pages><issn>1389-1723</issn><eissn>1347-4421</eissn><abstract>An enzyme that catalyzes C-3 epimerization between d-fructose and d-allulose was found in Arthrobacter globiformis strain M30. Arthrobacter species have long been used in the food industry and are well-known for their high degree of safety. The enzyme was purified by ion exchange and hydrophobic interaction chromatographies and characterized as a d-allulose 3-epimerase (d-AE). The molecular weight of the purified enzyme was estimated to be 128 kDa with four identical subunits. The enzyme showed maximal activity and thermostability in the presence of Mg2+. The optimal pH and temperature for enzymatic activity were 7.0–8.0 and 70°C, respectively. The enzyme was immobilized to ion exchange resin whereupon it was stable for longer periods than the free enzyme when stored at below 10°C. In the column reaction, the enzyme activity also maintained stability for more than 4 months. Under these conditions, 215 kg of d-allulose produced per liter immobilized enzyme, and this was the highest production yield of d-allulose reported so far. These highly stable properties suggest that this enzyme represents an ideal candidate for the industrial production of d-allulose.</abstract><cop>Japan</cop><pub>Elsevier B.V</pub><pmid>27713017</pmid><doi>10.1016/j.jbiosc.2016.09.004</doi><tpages>7</tpages></addata></record> |
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| subjects | Arthrobacter - chemistry Arthrobacter - enzymology Arthrobacter globiformis M30 d-Allulose d-Allulose 3-epimerase Enzyme Stability Fructose - biosynthesis Fructose - metabolism Hydrogen-Ion Concentration Immobilized d-AE Kinetics Magnesium Metabolic Engineering Molecular Weight Racemases and Epimerases - analysis Racemases and Epimerases - isolation & purification Racemases and Epimerases - metabolism Temperature |
| title | Purification and characterization of d-allulose 3-epimerase derived from Arthrobacter globiformis M30, a GRAS microorganism |
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