Effects of ascorbic acid on α-L-arabinofuranosidase and α-L-arabinopyranosidase activities from Bifidobacterium longum RD47 and its application to whole cell bioconversion of ginsenoside
Bifidobacterium longum RD47 was cultured in 24 kinds of modified MRS broths containing various ingredients to select the most promising source that induces microbial enzymes. Among the various ingredients, ascorbic acid significantly enhanced α-L-arabinofuranosidase and α-L-arabinopyranosidase activ...
Gespeichert in:
Veröffentlicht in: | Applied biological chemistry 2015-12, Vol.58 (6), p.857-865 |
---|---|
Hauptverfasser: | , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 865 |
---|---|
container_issue | 6 |
container_start_page | 857 |
container_title | Applied biological chemistry |
container_volume | 58 |
creator | Ku, Seockmo You, Hyun Ju Park, Myeong Soo Ji, Geun Eog |
description | Bifidobacterium longum RD47 was cultured in 24 kinds of modified MRS broths containing various ingredients to select the most promising source that induces microbial enzymes. Among the various ingredients, ascorbic acid significantly enhanced α-L-arabinofuranosidase and α-L-arabinopyranosidase activities in Bifidobacterium longum RD47. Addition of 2 % ascorbic acid (w/v) to MRS showed the maximum enzyme activities. Both whole cell and disrupted cell homogenates showed efficient ρ-nitrophenyl-β-D-glucopyranoside and ρ-nitrophenyl-β-D-glucofuranoside hydrolysis activities. The initially enhanced α-L-arabinopyranosidase and α-L-arabinofuranosidase activities by ascorbic acid were maintained over the cell disruption process. The optimal pH of α-L-arabinofuranosidase and α-L-arabinopyranosidase was 5.0 and 7.0, respectively. Both enzymes showed the maximum activities at 40.0 °C. Under the controlled condition using Bifidobacterium longum RD47, ginsenoside Rb2, and Rc were converted to ginsenoside Rd. |
doi_str_mv | 10.1007/s13765-015-0113-z |
format | Article |
fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_proquest_journals_2399171423</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2399171423</sourcerecordid><originalsourceid>FETCH-LOGICAL-c494t-eb6e9aa4006f27d232cbf23417206f03313dd60ef73bc12f568fff1d90f2ad033</originalsourceid><addsrcrecordid>eNp9Ustu1TAQtRCIXi58ABuwxIZNwK8b32yQoJSHdCUkoBI7y3HsdKrETu3kovav2PMNfBNOU0rLgoU90pyZc2bsg9BjSl5QQuTLRLksNwWh86G8uLiDVoxxUXAhvt1FKyr5tmCM8AP0IKVTQkohqLiPDlhZUlZVdIV-HjlnzZhwcFgnE2INBmsDDQ4e__pR7AoddQ0-uClqHxI0OlmsfXMLHM5vgmaEPYxgE3Yx9PgNOGhCndM2wtTjLvg2h89vhbwkgqyuh6EDo0fIqmPA309CZ7GxXYdrCCb4vY1pxvKULfhkL8XsQ3TP6S7ZR1dxjY7fHX09_FDsPr3_ePh6VxhRibGwdWkrrUXe3zHZMM5M7fIzUclyhnBOedOUxDrJa0OZ25Rb5xxtKuKYbjK-Rq8W3mGqe9sY68eoOzVE6HU8V0GDuo14OFFt2CtRim0lq0zw_IoghrPJplH1kOb1tLdhSopuSR5iI_O1Rs_-KT0NU_R5PcV4_jJJBZsnokuViSGlaN31MJSo2Rtq8YbK3lCzN9RF7nlyc4vrjj9myAVsKUgZ8q2Nf6X_x_p0aXI6KN1GSOr4CyO0JISyDSEV_w2QXtSs</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2399171423</pqid></control><display><type>article</type><title>Effects of ascorbic acid on α-L-arabinofuranosidase and α-L-arabinopyranosidase activities from Bifidobacterium longum RD47 and its application to whole cell bioconversion of ginsenoside</title><source>SpringerLink Journals</source><creator>Ku, Seockmo ; You, Hyun Ju ; Park, Myeong Soo ; Ji, Geun Eog</creator><creatorcontrib>Ku, Seockmo ; You, Hyun Ju ; Park, Myeong Soo ; Ji, Geun Eog</creatorcontrib><description>Bifidobacterium longum RD47 was cultured in 24 kinds of modified MRS broths containing various ingredients to select the most promising source that induces microbial enzymes. Among the various ingredients, ascorbic acid significantly enhanced α-L-arabinofuranosidase and α-L-arabinopyranosidase activities in Bifidobacterium longum RD47. Addition of 2 % ascorbic acid (w/v) to MRS showed the maximum enzyme activities. Both whole cell and disrupted cell homogenates showed efficient ρ-nitrophenyl-β-D-glucopyranoside and ρ-nitrophenyl-β-D-glucofuranoside hydrolysis activities. The initially enhanced α-L-arabinopyranosidase and α-L-arabinofuranosidase activities by ascorbic acid were maintained over the cell disruption process. The optimal pH of α-L-arabinofuranosidase and α-L-arabinopyranosidase was 5.0 and 7.0, respectively. Both enzymes showed the maximum activities at 40.0 °C. Under the controlled condition using Bifidobacterium longum RD47, ginsenoside Rb2, and Rc were converted to ginsenoside Rd.</description><identifier>ISSN: 1738-2203</identifier><identifier>ISSN: 2468-0834</identifier><identifier>EISSN: 2234-344X</identifier><identifier>EISSN: 2468-0842</identifier><identifier>DOI: 10.1007/s13765-015-0113-z</identifier><identifier>PMID: 26612991</identifier><language>eng</language><publisher>Seoul: The Korean Society for Applied Biological Chemistry</publisher><subject>Acids ; alpha-N-arabinofuranosidase ; Applied Microbiology ; Arabinofuranosidase ; Ascorbic acid ; Bifidobacterium longum ; Bioconversion ; Biological Techniques ; Bioorganic Chemistry ; biotransformation ; Broths ; Cell disruption ; Chemistry ; Chemistry and Materials Science ; Enzymatic activity ; enzyme activity ; Enzymes ; Ginsenosides ; hydrolysis ; Ingredients ; L-Arabinofuranosidase ; Microorganisms ; Vitamin C</subject><ispartof>Applied biological chemistry, 2015-12, Vol.58 (6), p.857-865</ispartof><rights>The Author(s) 2015</rights><rights>The Author(s) 2015. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c494t-eb6e9aa4006f27d232cbf23417206f03313dd60ef73bc12f568fff1d90f2ad033</citedby><cites>FETCH-LOGICAL-c494t-eb6e9aa4006f27d232cbf23417206f03313dd60ef73bc12f568fff1d90f2ad033</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,881,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26612991$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ku, Seockmo</creatorcontrib><creatorcontrib>You, Hyun Ju</creatorcontrib><creatorcontrib>Park, Myeong Soo</creatorcontrib><creatorcontrib>Ji, Geun Eog</creatorcontrib><title>Effects of ascorbic acid on α-L-arabinofuranosidase and α-L-arabinopyranosidase activities from Bifidobacterium longum RD47 and its application to whole cell bioconversion of ginsenoside</title><title>Applied biological chemistry</title><addtitle>J Korean Soc Appl Biol Chem</addtitle><addtitle>J Korean Soc Appl Biol Chem</addtitle><description>Bifidobacterium longum RD47 was cultured in 24 kinds of modified MRS broths containing various ingredients to select the most promising source that induces microbial enzymes. Among the various ingredients, ascorbic acid significantly enhanced α-L-arabinofuranosidase and α-L-arabinopyranosidase activities in Bifidobacterium longum RD47. Addition of 2 % ascorbic acid (w/v) to MRS showed the maximum enzyme activities. Both whole cell and disrupted cell homogenates showed efficient ρ-nitrophenyl-β-D-glucopyranoside and ρ-nitrophenyl-β-D-glucofuranoside hydrolysis activities. The initially enhanced α-L-arabinopyranosidase and α-L-arabinofuranosidase activities by ascorbic acid were maintained over the cell disruption process. The optimal pH of α-L-arabinofuranosidase and α-L-arabinopyranosidase was 5.0 and 7.0, respectively. Both enzymes showed the maximum activities at 40.0 °C. Under the controlled condition using Bifidobacterium longum RD47, ginsenoside Rb2, and Rc were converted to ginsenoside Rd.</description><subject>Acids</subject><subject>alpha-N-arabinofuranosidase</subject><subject>Applied Microbiology</subject><subject>Arabinofuranosidase</subject><subject>Ascorbic acid</subject><subject>Bifidobacterium longum</subject><subject>Bioconversion</subject><subject>Biological Techniques</subject><subject>Bioorganic Chemistry</subject><subject>biotransformation</subject><subject>Broths</subject><subject>Cell disruption</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Enzymatic activity</subject><subject>enzyme activity</subject><subject>Enzymes</subject><subject>Ginsenosides</subject><subject>hydrolysis</subject><subject>Ingredients</subject><subject>L-Arabinofuranosidase</subject><subject>Microorganisms</subject><subject>Vitamin C</subject><issn>1738-2203</issn><issn>2468-0834</issn><issn>2234-344X</issn><issn>2468-0842</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>BENPR</sourceid><recordid>eNp9Ustu1TAQtRCIXi58ABuwxIZNwK8b32yQoJSHdCUkoBI7y3HsdKrETu3kovav2PMNfBNOU0rLgoU90pyZc2bsg9BjSl5QQuTLRLksNwWh86G8uLiDVoxxUXAhvt1FKyr5tmCM8AP0IKVTQkohqLiPDlhZUlZVdIV-HjlnzZhwcFgnE2INBmsDDQ4e__pR7AoddQ0-uClqHxI0OlmsfXMLHM5vgmaEPYxgE3Yx9PgNOGhCndM2wtTjLvg2h89vhbwkgqyuh6EDo0fIqmPA309CZ7GxXYdrCCb4vY1pxvKULfhkL8XsQ3TP6S7ZR1dxjY7fHX09_FDsPr3_ePh6VxhRibGwdWkrrUXe3zHZMM5M7fIzUclyhnBOedOUxDrJa0OZ25Rb5xxtKuKYbjK-Rq8W3mGqe9sY68eoOzVE6HU8V0GDuo14OFFt2CtRim0lq0zw_IoghrPJplH1kOb1tLdhSopuSR5iI_O1Rs_-KT0NU_R5PcV4_jJJBZsnokuViSGlaN31MJSo2Rtq8YbK3lCzN9RF7nlyc4vrjj9myAVsKUgZ8q2Nf6X_x_p0aXI6KN1GSOr4CyO0JISyDSEV_w2QXtSs</recordid><startdate>20151201</startdate><enddate>20151201</enddate><creator>Ku, Seockmo</creator><creator>You, Hyun Ju</creator><creator>Park, Myeong Soo</creator><creator>Ji, Geun Eog</creator><general>The Korean Society for Applied Biological Chemistry</general><general>Springer Nature B.V</general><scope>FBQ</scope><scope>C6C</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X2</scope><scope>8FE</scope><scope>8FH</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>LK8</scope><scope>M0K</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7S9</scope><scope>L.6</scope><scope>5PM</scope></search><sort><creationdate>20151201</creationdate><title>Effects of ascorbic acid on α-L-arabinofuranosidase and α-L-arabinopyranosidase activities from Bifidobacterium longum RD47 and its application to whole cell bioconversion of ginsenoside</title><author>Ku, Seockmo ; You, Hyun Ju ; Park, Myeong Soo ; Ji, Geun Eog</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c494t-eb6e9aa4006f27d232cbf23417206f03313dd60ef73bc12f568fff1d90f2ad033</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Acids</topic><topic>alpha-N-arabinofuranosidase</topic><topic>Applied Microbiology</topic><topic>Arabinofuranosidase</topic><topic>Ascorbic acid</topic><topic>Bifidobacterium longum</topic><topic>Bioconversion</topic><topic>Biological Techniques</topic><topic>Bioorganic Chemistry</topic><topic>biotransformation</topic><topic>Broths</topic><topic>Cell disruption</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Enzymatic activity</topic><topic>enzyme activity</topic><topic>Enzymes</topic><topic>Ginsenosides</topic><topic>hydrolysis</topic><topic>Ingredients</topic><topic>L-Arabinofuranosidase</topic><topic>Microorganisms</topic><topic>Vitamin C</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ku, Seockmo</creatorcontrib><creatorcontrib>You, Hyun Ju</creatorcontrib><creatorcontrib>Park, Myeong Soo</creatorcontrib><creatorcontrib>Ji, Geun Eog</creatorcontrib><collection>AGRIS</collection><collection>Springer Nature OA Free Journals</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Agricultural Science Collection</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Biological Science Database</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Applied biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ku, Seockmo</au><au>You, Hyun Ju</au><au>Park, Myeong Soo</au><au>Ji, Geun Eog</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effects of ascorbic acid on α-L-arabinofuranosidase and α-L-arabinopyranosidase activities from Bifidobacterium longum RD47 and its application to whole cell bioconversion of ginsenoside</atitle><jtitle>Applied biological chemistry</jtitle><stitle>J Korean Soc Appl Biol Chem</stitle><addtitle>J Korean Soc Appl Biol Chem</addtitle><date>2015-12-01</date><risdate>2015</risdate><volume>58</volume><issue>6</issue><spage>857</spage><epage>865</epage><pages>857-865</pages><issn>1738-2203</issn><issn>2468-0834</issn><eissn>2234-344X</eissn><eissn>2468-0842</eissn><abstract>Bifidobacterium longum RD47 was cultured in 24 kinds of modified MRS broths containing various ingredients to select the most promising source that induces microbial enzymes. Among the various ingredients, ascorbic acid significantly enhanced α-L-arabinofuranosidase and α-L-arabinopyranosidase activities in Bifidobacterium longum RD47. Addition of 2 % ascorbic acid (w/v) to MRS showed the maximum enzyme activities. Both whole cell and disrupted cell homogenates showed efficient ρ-nitrophenyl-β-D-glucopyranoside and ρ-nitrophenyl-β-D-glucofuranoside hydrolysis activities. The initially enhanced α-L-arabinopyranosidase and α-L-arabinofuranosidase activities by ascorbic acid were maintained over the cell disruption process. The optimal pH of α-L-arabinofuranosidase and α-L-arabinopyranosidase was 5.0 and 7.0, respectively. Both enzymes showed the maximum activities at 40.0 °C. Under the controlled condition using Bifidobacterium longum RD47, ginsenoside Rb2, and Rc were converted to ginsenoside Rd.</abstract><cop>Seoul</cop><pub>The Korean Society for Applied Biological Chemistry</pub><pmid>26612991</pmid><doi>10.1007/s13765-015-0113-z</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 1738-2203 |
ispartof | Applied biological chemistry, 2015-12, Vol.58 (6), p.857-865 |
issn | 1738-2203 2468-0834 2234-344X 2468-0842 |
language | eng |
recordid | cdi_proquest_journals_2399171423 |
source | SpringerLink Journals |
subjects | Acids alpha-N-arabinofuranosidase Applied Microbiology Arabinofuranosidase Ascorbic acid Bifidobacterium longum Bioconversion Biological Techniques Bioorganic Chemistry biotransformation Broths Cell disruption Chemistry Chemistry and Materials Science Enzymatic activity enzyme activity Enzymes Ginsenosides hydrolysis Ingredients L-Arabinofuranosidase Microorganisms Vitamin C |
title | Effects of ascorbic acid on α-L-arabinofuranosidase and α-L-arabinopyranosidase activities from Bifidobacterium longum RD47 and its application to whole cell bioconversion of ginsenoside |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-11T10%3A17%3A50IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Effects%20of%20ascorbic%20acid%20on%20%CE%B1-L-arabinofuranosidase%20and%20%CE%B1-L-arabinopyranosidase%20activities%20from%20Bifidobacterium%20longum%20RD47%20and%20its%20application%20to%20whole%20cell%20bioconversion%20of%20ginsenoside&rft.jtitle=Applied%20biological%20chemistry&rft.au=Ku,%20Seockmo&rft.date=2015-12-01&rft.volume=58&rft.issue=6&rft.spage=857&rft.epage=865&rft.pages=857-865&rft.issn=1738-2203&rft.eissn=2234-344X&rft_id=info:doi/10.1007/s13765-015-0113-z&rft_dat=%3Cproquest_pubme%3E2399171423%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2399171423&rft_id=info:pmid/26612991&rfr_iscdi=true |