Enzymatic synthesis of glycosylated puerarin using maltogenic amylase from Bacillus stearothermophilus expressed in Bacillus subtilis
BACKGROUND: The maltogenic amylase from Bacillus stearothermophilus (BSMA) is a valuable biocatalyst that has been used to transglycosylate natural glycosides to improve solubility. To ensure safety, BSMA was produced in Bacillus subtilis, using new shuttle vector-based expression vectors. The trans...
Gespeichert in:
| Veröffentlicht in: | Journal of the science of food and agriculture 2010-05, Vol.90 (7), p.1179-1184 |
|---|---|
| Hauptverfasser: | , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1184 |
|---|---|
| container_issue | 7 |
| container_start_page | 1179 |
| container_title | Journal of the science of food and agriculture |
| container_volume | 90 |
| creator | Choi, Chung-Hyo Kim, Seung-Hee Jang, Jun-Hyuck Park, Jong-Tae Shim, Jae-Hoon Kim, Young-Wan Park, Kwan-Hwa |
| description | BACKGROUND: The maltogenic amylase from Bacillus stearothermophilus (BSMA) is a valuable biocatalyst that has been used to transglycosylate natural glycosides to improve solubility. To ensure safety, BSMA was produced in Bacillus subtilis, using new shuttle vector-based expression vectors. The transglycosylation of puerarin was also conducted with crude BSMA and analyzed.RESULTS: Two expression systems, each containing one of the promoters from the genes encoding Bacillus licheniformis maltogenic amylase (BLMA) and an α-amylase from B. subtilis NA64 (amyR2), were constructed. The amyR2 promoter system was chosen as the best system; it yielded 107 mg of pure BSMA from a 2 L culture. In the transglycosylation reactions of puerarin using crude BSMA, relative amounts for maltosyl-α-(1 [rightward arrow] 6)-puerarin, glucosyl-α-(1 [rightward arrow] 6)-puerarin, glucosyl-α-(1 [rightward arrow] 3)-puerarin, and puerarin were determined as 26:18:7:49. A two-step purification process, including gel permeation chromatography, yielded 1.7 g of the transfer products from 3 g of puerarin.CONCLUSION: The crude BSMA produced from a host generally recognized as safe (B. subtilis) can be used to transglycosylate various functional compounds. The expression system developed in this study will be helpful for the production of other food-grade enzymes by B. subtilis. |
| doi_str_mv | 10.1002/jsfa.3945 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_787077155</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>787077155</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4755-1d70f1de43eabf9652df96653681129d36131d033f1a228bd78893e6f7216a313</originalsourceid><addsrcrecordid>eNqF0V1r1EAUBuAgil2rF_4BDQWRXqSdj2Q-Lrul3SrFD9oieDPMJjPbWSeZOCfBxnv_t7Ps2oIg3iSQec57JrxZ9hKjI4wQOV6D1UdUltWjbIaR5AVCGD3OZumMFBUuyV72DGCNEJKSsafZHkFUUinlLPt11v2cWj24OoepG24NOMiDzVd-qgNMXg-myfvRRB1dl4_gulXeaj-ElenSjG4TAZPbGNp8rmvn_Qg5DEbHkMJiG_pbt_lk7vpoAFJYinmA43Jw3sHz7InVHsyL3Xs_uzk_uz69KC4_Lt6dnlwWdcmrqsANRxY3pqRGL61kFWnSk1WUCYyJbCjDFDeIUos1IWLZcCEkNcxygpmmmO5nb7e5fQzfRwODah3UxnvdmTCC4oIjznFV_V9SKoQoBUvy4C-5DmPs0m8oQgjjvBIoocMtqmMAiMaqPrpWx0lhpDYdqk2HatNhsq92geOyNc29_FNaAm92QEOtvY26qx08OMJKgtjGHW_dD-fN9O-N6v3V-cludbGdcKnCu_sJHb8pximv1JcPC0Xm1_NPn-lCfU3-9dZbHZRexXSLmyuCMEVYEMlLTn8DESXNfQ</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>222677580</pqid></control><display><type>article</type><title>Enzymatic synthesis of glycosylated puerarin using maltogenic amylase from Bacillus stearothermophilus expressed in Bacillus subtilis</title><source>MEDLINE</source><source>Wiley Online Library Journals Frontfile Complete</source><creator>Choi, Chung-Hyo ; Kim, Seung-Hee ; Jang, Jun-Hyuck ; Park, Jong-Tae ; Shim, Jae-Hoon ; Kim, Young-Wan ; Park, Kwan-Hwa</creator><creatorcontrib>Choi, Chung-Hyo ; Kim, Seung-Hee ; Jang, Jun-Hyuck ; Park, Jong-Tae ; Shim, Jae-Hoon ; Kim, Young-Wan ; Park, Kwan-Hwa</creatorcontrib><description>BACKGROUND: The maltogenic amylase from Bacillus stearothermophilus (BSMA) is a valuable biocatalyst that has been used to transglycosylate natural glycosides to improve solubility. To ensure safety, BSMA was produced in Bacillus subtilis, using new shuttle vector-based expression vectors. The transglycosylation of puerarin was also conducted with crude BSMA and analyzed.RESULTS: Two expression systems, each containing one of the promoters from the genes encoding Bacillus licheniformis maltogenic amylase (BLMA) and an α-amylase from B. subtilis NA64 (amyR2), were constructed. The amyR2 promoter system was chosen as the best system; it yielded 107 mg of pure BSMA from a 2 L culture. In the transglycosylation reactions of puerarin using crude BSMA, relative amounts for maltosyl-α-(1 [rightward arrow] 6)-puerarin, glucosyl-α-(1 [rightward arrow] 6)-puerarin, glucosyl-α-(1 [rightward arrow] 3)-puerarin, and puerarin were determined as 26:18:7:49. A two-step purification process, including gel permeation chromatography, yielded 1.7 g of the transfer products from 3 g of puerarin.CONCLUSION: The crude BSMA produced from a host generally recognized as safe (B. subtilis) can be used to transglycosylate various functional compounds. The expression system developed in this study will be helpful for the production of other food-grade enzymes by B. subtilis.</description><identifier>ISSN: 0022-5142</identifier><identifier>EISSN: 1097-0010</identifier><identifier>DOI: 10.1002/jsfa.3945</identifier><identifier>PMID: 20393999</identifier><identifier>CODEN: JSFAAE</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Amylase ; amylases ; Amylases - genetics ; Amylases - metabolism ; Bacillus stearothermophilus ; Bacillus stearothermophilus maltogenic amylase ; Bacillus subtilis ; Bacillus subtilis - enzymology ; Bacillus subtilis - genetics ; Bacteria ; Bioconversions. Hemisynthesis ; Biological and medical sciences ; Biotechnology ; Chromatography ; Culture ; DNA, Recombinant ; Encoding ; enzymatic treatment ; Enzymes ; Food industries ; Food microbiology ; Food science ; food technology ; food-grade enzymes ; Fundamental and applied biological sciences. Psychology ; Gel permeation chromatography ; Gene Expression ; Genes, Bacterial ; Genetic Engineering - methods ; Geobacillus stearothermophilus - enzymology ; Geobacillus stearothermophilus - genetics ; glycosylated puerarin ; Glycosylation ; isoflavones ; Isoflavones - biosynthesis ; maltogenic amylase ; Mathematical analysis ; Methods. Procedures. Technologies ; novel foods ; plasmid stability ; Plasmids ; Promoter Regions, Genetic ; Pueraria - chemistry ; puerarin ; shuttle vector ; Solubility ; Studies ; transglycosylation</subject><ispartof>Journal of the science of food and agriculture, 2010-05, Vol.90 (7), p.1179-1184</ispartof><rights>Copyright © 2010 Society of Chemical Industry</rights><rights>2015 INIST-CNRS</rights><rights>Copyright John Wiley and Sons, Limited May 2010</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4755-1d70f1de43eabf9652df96653681129d36131d033f1a228bd78893e6f7216a313</citedby><cites>FETCH-LOGICAL-c4755-1d70f1de43eabf9652df96653681129d36131d033f1a228bd78893e6f7216a313</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fjsfa.3945$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fjsfa.3945$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=22642069$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20393999$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Choi, Chung-Hyo</creatorcontrib><creatorcontrib>Kim, Seung-Hee</creatorcontrib><creatorcontrib>Jang, Jun-Hyuck</creatorcontrib><creatorcontrib>Park, Jong-Tae</creatorcontrib><creatorcontrib>Shim, Jae-Hoon</creatorcontrib><creatorcontrib>Kim, Young-Wan</creatorcontrib><creatorcontrib>Park, Kwan-Hwa</creatorcontrib><title>Enzymatic synthesis of glycosylated puerarin using maltogenic amylase from Bacillus stearothermophilus expressed in Bacillus subtilis</title><title>Journal of the science of food and agriculture</title><addtitle>J. Sci. Food Agric</addtitle><description>BACKGROUND: The maltogenic amylase from Bacillus stearothermophilus (BSMA) is a valuable biocatalyst that has been used to transglycosylate natural glycosides to improve solubility. To ensure safety, BSMA was produced in Bacillus subtilis, using new shuttle vector-based expression vectors. The transglycosylation of puerarin was also conducted with crude BSMA and analyzed.RESULTS: Two expression systems, each containing one of the promoters from the genes encoding Bacillus licheniformis maltogenic amylase (BLMA) and an α-amylase from B. subtilis NA64 (amyR2), were constructed. The amyR2 promoter system was chosen as the best system; it yielded 107 mg of pure BSMA from a 2 L culture. In the transglycosylation reactions of puerarin using crude BSMA, relative amounts for maltosyl-α-(1 [rightward arrow] 6)-puerarin, glucosyl-α-(1 [rightward arrow] 6)-puerarin, glucosyl-α-(1 [rightward arrow] 3)-puerarin, and puerarin were determined as 26:18:7:49. A two-step purification process, including gel permeation chromatography, yielded 1.7 g of the transfer products from 3 g of puerarin.CONCLUSION: The crude BSMA produced from a host generally recognized as safe (B. subtilis) can be used to transglycosylate various functional compounds. The expression system developed in this study will be helpful for the production of other food-grade enzymes by B. subtilis.</description><subject>Amylase</subject><subject>amylases</subject><subject>Amylases - genetics</subject><subject>Amylases - metabolism</subject><subject>Bacillus stearothermophilus</subject><subject>Bacillus stearothermophilus maltogenic amylase</subject><subject>Bacillus subtilis</subject><subject>Bacillus subtilis - enzymology</subject><subject>Bacillus subtilis - genetics</subject><subject>Bacteria</subject><subject>Bioconversions. Hemisynthesis</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Chromatography</subject><subject>Culture</subject><subject>DNA, Recombinant</subject><subject>Encoding</subject><subject>enzymatic treatment</subject><subject>Enzymes</subject><subject>Food industries</subject><subject>Food microbiology</subject><subject>Food science</subject><subject>food technology</subject><subject>food-grade enzymes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gel permeation chromatography</subject><subject>Gene Expression</subject><subject>Genes, Bacterial</subject><subject>Genetic Engineering - methods</subject><subject>Geobacillus stearothermophilus - enzymology</subject><subject>Geobacillus stearothermophilus - genetics</subject><subject>glycosylated puerarin</subject><subject>Glycosylation</subject><subject>isoflavones</subject><subject>Isoflavones - biosynthesis</subject><subject>maltogenic amylase</subject><subject>Mathematical analysis</subject><subject>Methods. Procedures. Technologies</subject><subject>novel foods</subject><subject>plasmid stability</subject><subject>Plasmids</subject><subject>Promoter Regions, Genetic</subject><subject>Pueraria - chemistry</subject><subject>puerarin</subject><subject>shuttle vector</subject><subject>Solubility</subject><subject>Studies</subject><subject>transglycosylation</subject><issn>0022-5142</issn><issn>1097-0010</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0V1r1EAUBuAgil2rF_4BDQWRXqSdj2Q-Lrul3SrFD9oieDPMJjPbWSeZOCfBxnv_t7Ps2oIg3iSQec57JrxZ9hKjI4wQOV6D1UdUltWjbIaR5AVCGD3OZumMFBUuyV72DGCNEJKSsafZHkFUUinlLPt11v2cWj24OoepG24NOMiDzVd-qgNMXg-myfvRRB1dl4_gulXeaj-ElenSjG4TAZPbGNp8rmvn_Qg5DEbHkMJiG_pbt_lk7vpoAFJYinmA43Jw3sHz7InVHsyL3Xs_uzk_uz69KC4_Lt6dnlwWdcmrqsANRxY3pqRGL61kFWnSk1WUCYyJbCjDFDeIUos1IWLZcCEkNcxygpmmmO5nb7e5fQzfRwODah3UxnvdmTCC4oIjznFV_V9SKoQoBUvy4C-5DmPs0m8oQgjjvBIoocMtqmMAiMaqPrpWx0lhpDYdqk2HatNhsq92geOyNc29_FNaAm92QEOtvY26qx08OMJKgtjGHW_dD-fN9O-N6v3V-cludbGdcKnCu_sJHb8pximv1JcPC0Xm1_NPn-lCfU3-9dZbHZRexXSLmyuCMEVYEMlLTn8DESXNfQ</recordid><startdate>201005</startdate><enddate>201005</enddate><creator>Choi, Chung-Hyo</creator><creator>Kim, Seung-Hee</creator><creator>Jang, Jun-Hyuck</creator><creator>Park, Jong-Tae</creator><creator>Shim, Jae-Hoon</creator><creator>Kim, Young-Wan</creator><creator>Park, Kwan-Hwa</creator><general>John Wiley & Sons, Ltd</general><general>Wiley</general><general>John Wiley and Sons, Limited</general><scope>FBQ</scope><scope>BSCLL</scope><scope>IQODW</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>7QF</scope><scope>7QL</scope><scope>7QQ</scope><scope>7QR</scope><scope>7SC</scope><scope>7SE</scope><scope>7SN</scope><scope>7SP</scope><scope>7SR</scope><scope>7ST</scope><scope>7T5</scope><scope>7T7</scope><scope>7TA</scope><scope>7TB</scope><scope>7TM</scope><scope>7U5</scope><scope>7U9</scope><scope>8BQ</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>H94</scope><scope>JG9</scope><scope>JQ2</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>M7N</scope><scope>P64</scope><scope>SOI</scope><scope>7X8</scope></search><sort><creationdate>201005</creationdate><title>Enzymatic synthesis of glycosylated puerarin using maltogenic amylase from Bacillus stearothermophilus expressed in Bacillus subtilis</title><author>Choi, Chung-Hyo ; Kim, Seung-Hee ; Jang, Jun-Hyuck ; Park, Jong-Tae ; Shim, Jae-Hoon ; Kim, Young-Wan ; Park, Kwan-Hwa</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4755-1d70f1de43eabf9652df96653681129d36131d033f1a228bd78893e6f7216a313</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Amylase</topic><topic>amylases</topic><topic>Amylases - genetics</topic><topic>Amylases - metabolism</topic><topic>Bacillus stearothermophilus</topic><topic>Bacillus stearothermophilus maltogenic amylase</topic><topic>Bacillus subtilis</topic><topic>Bacillus subtilis - enzymology</topic><topic>Bacillus subtilis - genetics</topic><topic>Bacteria</topic><topic>Bioconversions. Hemisynthesis</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Chromatography</topic><topic>Culture</topic><topic>DNA, Recombinant</topic><topic>Encoding</topic><topic>enzymatic treatment</topic><topic>Enzymes</topic><topic>Food industries</topic><topic>Food microbiology</topic><topic>Food science</topic><topic>food technology</topic><topic>food-grade enzymes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gel permeation chromatography</topic><topic>Gene Expression</topic><topic>Genes, Bacterial</topic><topic>Genetic Engineering - methods</topic><topic>Geobacillus stearothermophilus - enzymology</topic><topic>Geobacillus stearothermophilus - genetics</topic><topic>glycosylated puerarin</topic><topic>Glycosylation</topic><topic>isoflavones</topic><topic>Isoflavones - biosynthesis</topic><topic>maltogenic amylase</topic><topic>Mathematical analysis</topic><topic>Methods. Procedures. Technologies</topic><topic>novel foods</topic><topic>plasmid stability</topic><topic>Plasmids</topic><topic>Promoter Regions, Genetic</topic><topic>Pueraria - chemistry</topic><topic>puerarin</topic><topic>shuttle vector</topic><topic>Solubility</topic><topic>Studies</topic><topic>transglycosylation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Choi, Chung-Hyo</creatorcontrib><creatorcontrib>Kim, Seung-Hee</creatorcontrib><creatorcontrib>Jang, Jun-Hyuck</creatorcontrib><creatorcontrib>Park, Jong-Tae</creatorcontrib><creatorcontrib>Shim, Jae-Hoon</creatorcontrib><creatorcontrib>Kim, Young-Wan</creatorcontrib><creatorcontrib>Park, Kwan-Hwa</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Aluminium Industry Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Ceramic Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Computer and Information Systems Abstracts</collection><collection>Corrosion Abstracts</collection><collection>Ecology Abstracts</collection><collection>Electronics & Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Environment Abstracts</collection><collection>Immunology Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Materials Business File</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Engineering Research Database</collection><collection>Aerospace Database</collection><collection>Copper Technical Reference Library</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Materials Research Database</collection><collection>ProQuest Computer Science Collection</collection><collection>Civil Engineering Abstracts</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Computer and Information Systems Abstracts Academic</collection><collection>Computer and Information Systems Abstracts Professional</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environment Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of the science of food and agriculture</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Choi, Chung-Hyo</au><au>Kim, Seung-Hee</au><au>Jang, Jun-Hyuck</au><au>Park, Jong-Tae</au><au>Shim, Jae-Hoon</au><au>Kim, Young-Wan</au><au>Park, Kwan-Hwa</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Enzymatic synthesis of glycosylated puerarin using maltogenic amylase from Bacillus stearothermophilus expressed in Bacillus subtilis</atitle><jtitle>Journal of the science of food and agriculture</jtitle><addtitle>J. Sci. Food Agric</addtitle><date>2010-05</date><risdate>2010</risdate><volume>90</volume><issue>7</issue><spage>1179</spage><epage>1184</epage><pages>1179-1184</pages><issn>0022-5142</issn><eissn>1097-0010</eissn><coden>JSFAAE</coden><abstract>BACKGROUND: The maltogenic amylase from Bacillus stearothermophilus (BSMA) is a valuable biocatalyst that has been used to transglycosylate natural glycosides to improve solubility. To ensure safety, BSMA was produced in Bacillus subtilis, using new shuttle vector-based expression vectors. The transglycosylation of puerarin was also conducted with crude BSMA and analyzed.RESULTS: Two expression systems, each containing one of the promoters from the genes encoding Bacillus licheniformis maltogenic amylase (BLMA) and an α-amylase from B. subtilis NA64 (amyR2), were constructed. The amyR2 promoter system was chosen as the best system; it yielded 107 mg of pure BSMA from a 2 L culture. In the transglycosylation reactions of puerarin using crude BSMA, relative amounts for maltosyl-α-(1 [rightward arrow] 6)-puerarin, glucosyl-α-(1 [rightward arrow] 6)-puerarin, glucosyl-α-(1 [rightward arrow] 3)-puerarin, and puerarin were determined as 26:18:7:49. A two-step purification process, including gel permeation chromatography, yielded 1.7 g of the transfer products from 3 g of puerarin.CONCLUSION: The crude BSMA produced from a host generally recognized as safe (B. subtilis) can be used to transglycosylate various functional compounds. The expression system developed in this study will be helpful for the production of other food-grade enzymes by B. subtilis.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>20393999</pmid><doi>10.1002/jsfa.3945</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0022-5142 |
| ispartof | Journal of the science of food and agriculture, 2010-05, Vol.90 (7), p.1179-1184 |
| issn | 0022-5142 1097-0010 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_787077155 |
| source | MEDLINE; Wiley Online Library Journals Frontfile Complete |
| subjects | Amylase amylases Amylases - genetics Amylases - metabolism Bacillus stearothermophilus Bacillus stearothermophilus maltogenic amylase Bacillus subtilis Bacillus subtilis - enzymology Bacillus subtilis - genetics Bacteria Bioconversions. Hemisynthesis Biological and medical sciences Biotechnology Chromatography Culture DNA, Recombinant Encoding enzymatic treatment Enzymes Food industries Food microbiology Food science food technology food-grade enzymes Fundamental and applied biological sciences. Psychology Gel permeation chromatography Gene Expression Genes, Bacterial Genetic Engineering - methods Geobacillus stearothermophilus - enzymology Geobacillus stearothermophilus - genetics glycosylated puerarin Glycosylation isoflavones Isoflavones - biosynthesis maltogenic amylase Mathematical analysis Methods. Procedures. Technologies novel foods plasmid stability Plasmids Promoter Regions, Genetic Pueraria - chemistry puerarin shuttle vector Solubility Studies transglycosylation |
| title | Enzymatic synthesis of glycosylated puerarin using maltogenic amylase from Bacillus stearothermophilus expressed in Bacillus subtilis |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-08T05%3A14%3A31IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Enzymatic%20synthesis%20of%20glycosylated%20puerarin%20using%20maltogenic%20amylase%20from%20Bacillus%20stearothermophilus%20expressed%20in%20Bacillus%20subtilis&rft.jtitle=Journal%20of%20the%20science%20of%20food%20and%20agriculture&rft.au=Choi,%20Chung-Hyo&rft.date=2010-05&rft.volume=90&rft.issue=7&rft.spage=1179&rft.epage=1184&rft.pages=1179-1184&rft.issn=0022-5142&rft.eissn=1097-0010&rft.coden=JSFAAE&rft_id=info:doi/10.1002/jsfa.3945&rft_dat=%3Cproquest_cross%3E787077155%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=222677580&rft_id=info:pmid/20393999&rfr_iscdi=true |