Inhibition of β-Fructofuranosidases and α-Glucosidases by Synthetic Thio-fructofuranoside
A synthetic β-thio-fructofuranoside of mercaptoethanol inhibited not only β-fructofuranosidases but also α-glucosidases. The compound was hardly hydrolyzed by the glycosidases. The thio-fructoside competitively inhibited β-fructofuranosidases from Aspergillus niger, Candida sp., and Saccharomyces ce...
Gespeichert in:
| Veröffentlicht in: | Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2003-01, Vol.67 (8), p.1719-1724 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1724 |
|---|---|
| container_issue | 8 |
| container_start_page | 1719 |
| container_title | Bioscience, biotechnology, and biochemistry |
| container_volume | 67 |
| creator | KISO, Taro HAMAYASU, Kenichi FUJITA, Koki HARA, Kozo KITAHATA, Sumio NAKANO, Hirofumi |
| description | A synthetic β-thio-fructofuranoside of mercaptoethanol inhibited not only β-fructofuranosidases but also α-glucosidases. The compound was hardly hydrolyzed by the glycosidases. The thio-fructoside competitively inhibited β-fructofuranosidases from Aspergillus niger, Candida sp., and Saccharomyces cerevisiae, but not Arthrobacter β-fructofuranosidase at all. Sucrase activity of rat intestinal sucrase/isomaltase complex was also suppressed in the presence of the thio-fructoside. The thio-fructoside showed noncompetitive inhibition toward maltase activity of the rat intestinal enzyme complex and Saccharomyces sp. α-glucosidase. Inhibition against the Bacillus stearothermophilus α-glucosidase, Rhizopus glucoamylase, and porcine kidney trehalase were more slight than that against these two α-glucosidases. |
| doi_str_mv | 10.1271/bbb.67.1719 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmed_primary_12951505</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>73614987</sourcerecordid><originalsourceid>FETCH-LOGICAL-c566t-cbb36a5ebf39e7a5fa11c9fd9f21e1751582cae9a37349f55c6a6053449fa4413</originalsourceid><addsrcrecordid>eNptkMFKAzEQhoMoWqsn77IXvcjWnWaTNEcpVgXBg3ryECbZhEa2G012kT6WPojP5JZWRfA0zM83_8z8hBxBMYKxgHOt9YiLEQiQW2QAtBQ5l6XYJoNCAs8nJYM9sp_Sc1H0AoNdsgdjyYAVbECebpq51771ocmCyz4_8lnsTBtcF7EJyVeYbMqwqbLP9_yq7syPppfZ_bJp57b1JnuY-5C7v5P2gOw4rJM93NQheZxdPkyv89u7q5vpxW1uGOdtbrSmHJnVjkorkDkEMNJV0o3BgugPnYwNWolU0FI6xgxHXjBa9g2WJdAhOV37vsTw2tnUqoVPxtY1NjZ0SQnKoZQT0YNna9DEkFK0Tr1Ev8C4VFCoVZaqz1JxoVZZ9vTxxrbTC1v9spvweuBkA2AyWLv-b-PTL8dgQkGs1vI15xsX4gLfQqwr1eKyDvF7iP53wRcxnpHE</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>73614987</pqid></control><display><type>article</type><title>Inhibition of β-Fructofuranosidases and α-Glucosidases by Synthetic Thio-fructofuranoside</title><source>J-STAGE Free</source><source>MEDLINE</source><source>Oxford University Press Journals All Titles (1996-Current)</source><source>Open Access Titles of Japan</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Free Full-Text Journals in Chemistry</source><creator>KISO, Taro ; HAMAYASU, Kenichi ; FUJITA, Koki ; HARA, Kozo ; KITAHATA, Sumio ; NAKANO, Hirofumi</creator><creatorcontrib>KISO, Taro ; HAMAYASU, Kenichi ; FUJITA, Koki ; HARA, Kozo ; KITAHATA, Sumio ; NAKANO, Hirofumi</creatorcontrib><description>A synthetic β-thio-fructofuranoside of mercaptoethanol inhibited not only β-fructofuranosidases but also α-glucosidases. The compound was hardly hydrolyzed by the glycosidases. The thio-fructoside competitively inhibited β-fructofuranosidases from Aspergillus niger, Candida sp., and Saccharomyces cerevisiae, but not Arthrobacter β-fructofuranosidase at all. Sucrase activity of rat intestinal sucrase/isomaltase complex was also suppressed in the presence of the thio-fructoside. The thio-fructoside showed noncompetitive inhibition toward maltase activity of the rat intestinal enzyme complex and Saccharomyces sp. α-glucosidase. Inhibition against the Bacillus stearothermophilus α-glucosidase, Rhizopus glucoamylase, and porcine kidney trehalase were more slight than that against these two α-glucosidases.</description><identifier>ISSN: 0916-8451</identifier><identifier>EISSN: 1347-6947</identifier><identifier>DOI: 10.1271/bbb.67.1719</identifier><identifier>PMID: 12951505</identifier><language>eng</language><publisher>Tokyo: Japan Society for Bioscience, Biotechnology, and Agrochemistry</publisher><subject>Animals ; Arthrobacter - enzymology ; Aspergillus niger - enzymology ; beta-Fructofuranosidase - antagonists & inhibitors ; Binding, Competitive ; Biological and medical sciences ; Candida - enzymology ; Enzyme Inhibitors - chemistry ; Enzyme Inhibitors - metabolism ; Enzyme Inhibitors - pharmacology ; Fructose - analogs & derivatives ; Fructose - metabolism ; Fructose - pharmacology ; Fundamental and applied biological sciences. Psychology ; Geobacillus stearothermophilus - enzymology ; Glucan 1,4-alpha-Glucosidase - metabolism ; Glycoside Hydrolase Inhibitors ; Hydrolysis ; inhibition ; Intestines - enzymology ; Kinetics ; Maltose - metabolism ; Rats ; Rhizopus - enzymology ; Saccharomyces cerevisiae - enzymology ; Sucrase - metabolism ; Sucrose - metabolism ; Sulfides - chemistry ; Sulfides - metabolism ; Sulfides - pharmacology ; Swine ; thio-fructoside ; Trehalase - metabolism ; α-glucosidase ; β-fructofuranosidase</subject><ispartof>Bioscience, biotechnology, and biochemistry, 2003-01, Vol.67 (8), p.1719-1724</ispartof><rights>2003 by Japan Society for Bioscience, Biotechnology, and Agrochemistry 2003</rights><rights>2004 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c566t-cbb36a5ebf39e7a5fa11c9fd9f21e1751582cae9a37349f55c6a6053449fa4413</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=15183177$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12951505$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>KISO, Taro</creatorcontrib><creatorcontrib>HAMAYASU, Kenichi</creatorcontrib><creatorcontrib>FUJITA, Koki</creatorcontrib><creatorcontrib>HARA, Kozo</creatorcontrib><creatorcontrib>KITAHATA, Sumio</creatorcontrib><creatorcontrib>NAKANO, Hirofumi</creatorcontrib><title>Inhibition of β-Fructofuranosidases and α-Glucosidases by Synthetic Thio-fructofuranoside</title><title>Bioscience, biotechnology, and biochemistry</title><addtitle>Biosci Biotechnol Biochem</addtitle><description>A synthetic β-thio-fructofuranoside of mercaptoethanol inhibited not only β-fructofuranosidases but also α-glucosidases. The compound was hardly hydrolyzed by the glycosidases. The thio-fructoside competitively inhibited β-fructofuranosidases from Aspergillus niger, Candida sp., and Saccharomyces cerevisiae, but not Arthrobacter β-fructofuranosidase at all. Sucrase activity of rat intestinal sucrase/isomaltase complex was also suppressed in the presence of the thio-fructoside. The thio-fructoside showed noncompetitive inhibition toward maltase activity of the rat intestinal enzyme complex and Saccharomyces sp. α-glucosidase. Inhibition against the Bacillus stearothermophilus α-glucosidase, Rhizopus glucoamylase, and porcine kidney trehalase were more slight than that against these two α-glucosidases.</description><subject>Animals</subject><subject>Arthrobacter - enzymology</subject><subject>Aspergillus niger - enzymology</subject><subject>beta-Fructofuranosidase - antagonists & inhibitors</subject><subject>Binding, Competitive</subject><subject>Biological and medical sciences</subject><subject>Candida - enzymology</subject><subject>Enzyme Inhibitors - chemistry</subject><subject>Enzyme Inhibitors - metabolism</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Fructose - analogs & derivatives</subject><subject>Fructose - metabolism</subject><subject>Fructose - pharmacology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Geobacillus stearothermophilus - enzymology</subject><subject>Glucan 1,4-alpha-Glucosidase - metabolism</subject><subject>Glycoside Hydrolase Inhibitors</subject><subject>Hydrolysis</subject><subject>inhibition</subject><subject>Intestines - enzymology</subject><subject>Kinetics</subject><subject>Maltose - metabolism</subject><subject>Rats</subject><subject>Rhizopus - enzymology</subject><subject>Saccharomyces cerevisiae - enzymology</subject><subject>Sucrase - metabolism</subject><subject>Sucrose - metabolism</subject><subject>Sulfides - chemistry</subject><subject>Sulfides - metabolism</subject><subject>Sulfides - pharmacology</subject><subject>Swine</subject><subject>thio-fructoside</subject><subject>Trehalase - metabolism</subject><subject>α-glucosidase</subject><subject>β-fructofuranosidase</subject><issn>0916-8451</issn><issn>1347-6947</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkMFKAzEQhoMoWqsn77IXvcjWnWaTNEcpVgXBg3ryECbZhEa2G012kT6WPojP5JZWRfA0zM83_8z8hBxBMYKxgHOt9YiLEQiQW2QAtBQ5l6XYJoNCAs8nJYM9sp_Sc1H0AoNdsgdjyYAVbECebpq51771ocmCyz4_8lnsTBtcF7EJyVeYbMqwqbLP9_yq7syPppfZ_bJp57b1JnuY-5C7v5P2gOw4rJM93NQheZxdPkyv89u7q5vpxW1uGOdtbrSmHJnVjkorkDkEMNJV0o3BgugPnYwNWolU0FI6xgxHXjBa9g2WJdAhOV37vsTw2tnUqoVPxtY1NjZ0SQnKoZQT0YNna9DEkFK0Tr1Ev8C4VFCoVZaqz1JxoVZZ9vTxxrbTC1v9spvweuBkA2AyWLv-b-PTL8dgQkGs1vI15xsX4gLfQqwr1eKyDvF7iP53wRcxnpHE</recordid><startdate>20030101</startdate><enddate>20030101</enddate><creator>KISO, Taro</creator><creator>HAMAYASU, Kenichi</creator><creator>FUJITA, Koki</creator><creator>HARA, Kozo</creator><creator>KITAHATA, Sumio</creator><creator>NAKANO, Hirofumi</creator><general>Japan Society for Bioscience, Biotechnology, and Agrochemistry</general><general>Japan Society for Bioscience Biotechnology and Agrochemistry</general><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>7X8</scope></search><sort><creationdate>20030101</creationdate><title>Inhibition of β-Fructofuranosidases and α-Glucosidases by Synthetic Thio-fructofuranoside</title><author>KISO, Taro ; HAMAYASU, Kenichi ; FUJITA, Koki ; HARA, Kozo ; KITAHATA, Sumio ; NAKANO, Hirofumi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c566t-cbb36a5ebf39e7a5fa11c9fd9f21e1751582cae9a37349f55c6a6053449fa4413</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Animals</topic><topic>Arthrobacter - enzymology</topic><topic>Aspergillus niger - enzymology</topic><topic>beta-Fructofuranosidase - antagonists & inhibitors</topic><topic>Binding, Competitive</topic><topic>Biological and medical sciences</topic><topic>Candida - enzymology</topic><topic>Enzyme Inhibitors - chemistry</topic><topic>Enzyme Inhibitors - metabolism</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Fructose - analogs & derivatives</topic><topic>Fructose - metabolism</topic><topic>Fructose - pharmacology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Geobacillus stearothermophilus - enzymology</topic><topic>Glucan 1,4-alpha-Glucosidase - metabolism</topic><topic>Glycoside Hydrolase Inhibitors</topic><topic>Hydrolysis</topic><topic>inhibition</topic><topic>Intestines - enzymology</topic><topic>Kinetics</topic><topic>Maltose - metabolism</topic><topic>Rats</topic><topic>Rhizopus - enzymology</topic><topic>Saccharomyces cerevisiae - enzymology</topic><topic>Sucrase - metabolism</topic><topic>Sucrose - metabolism</topic><topic>Sulfides - chemistry</topic><topic>Sulfides - metabolism</topic><topic>Sulfides - pharmacology</topic><topic>Swine</topic><topic>thio-fructoside</topic><topic>Trehalase - metabolism</topic><topic>α-glucosidase</topic><topic>β-fructofuranosidase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>KISO, Taro</creatorcontrib><creatorcontrib>HAMAYASU, Kenichi</creatorcontrib><creatorcontrib>FUJITA, Koki</creatorcontrib><creatorcontrib>HARA, Kozo</creatorcontrib><creatorcontrib>KITAHATA, Sumio</creatorcontrib><creatorcontrib>NAKANO, Hirofumi</creatorcontrib><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>MEDLINE - Academic</collection><jtitle>Bioscience, biotechnology, and biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>KISO, Taro</au><au>HAMAYASU, Kenichi</au><au>FUJITA, Koki</au><au>HARA, Kozo</au><au>KITAHATA, Sumio</au><au>NAKANO, Hirofumi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Inhibition of β-Fructofuranosidases and α-Glucosidases by Synthetic Thio-fructofuranoside</atitle><jtitle>Bioscience, biotechnology, and biochemistry</jtitle><addtitle>Biosci Biotechnol Biochem</addtitle><date>2003-01-01</date><risdate>2003</risdate><volume>67</volume><issue>8</issue><spage>1719</spage><epage>1724</epage><pages>1719-1724</pages><issn>0916-8451</issn><eissn>1347-6947</eissn><abstract>A synthetic β-thio-fructofuranoside of mercaptoethanol inhibited not only β-fructofuranosidases but also α-glucosidases. The compound was hardly hydrolyzed by the glycosidases. The thio-fructoside competitively inhibited β-fructofuranosidases from Aspergillus niger, Candida sp., and Saccharomyces cerevisiae, but not Arthrobacter β-fructofuranosidase at all. Sucrase activity of rat intestinal sucrase/isomaltase complex was also suppressed in the presence of the thio-fructoside. The thio-fructoside showed noncompetitive inhibition toward maltase activity of the rat intestinal enzyme complex and Saccharomyces sp. α-glucosidase. Inhibition against the Bacillus stearothermophilus α-glucosidase, Rhizopus glucoamylase, and porcine kidney trehalase were more slight than that against these two α-glucosidases.</abstract><cop>Tokyo</cop><pub>Japan Society for Bioscience, Biotechnology, and Agrochemistry</pub><pmid>12951505</pmid><doi>10.1271/bbb.67.1719</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0916-8451 |
| ispartof | Bioscience, biotechnology, and biochemistry, 2003-01, Vol.67 (8), p.1719-1724 |
| issn | 0916-8451 1347-6947 |
| language | eng |
| recordid | cdi_pubmed_primary_12951505 |
| source | J-STAGE Free; MEDLINE; Oxford University Press Journals All Titles (1996-Current); Open Access Titles of Japan; EZB-FREE-00999 freely available EZB journals; Free Full-Text Journals in Chemistry |
| subjects | Animals Arthrobacter - enzymology Aspergillus niger - enzymology beta-Fructofuranosidase - antagonists & inhibitors Binding, Competitive Biological and medical sciences Candida - enzymology Enzyme Inhibitors - chemistry Enzyme Inhibitors - metabolism Enzyme Inhibitors - pharmacology Fructose - analogs & derivatives Fructose - metabolism Fructose - pharmacology Fundamental and applied biological sciences. Psychology Geobacillus stearothermophilus - enzymology Glucan 1,4-alpha-Glucosidase - metabolism Glycoside Hydrolase Inhibitors Hydrolysis inhibition Intestines - enzymology Kinetics Maltose - metabolism Rats Rhizopus - enzymology Saccharomyces cerevisiae - enzymology Sucrase - metabolism Sucrose - metabolism Sulfides - chemistry Sulfides - metabolism Sulfides - pharmacology Swine thio-fructoside Trehalase - metabolism α-glucosidase β-fructofuranosidase |
| title | Inhibition of β-Fructofuranosidases and α-Glucosidases by Synthetic Thio-fructofuranoside |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-03T13%3A24%3A38IST&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=Inhibition%20of%20%CE%B2-Fructofuranosidases%20and%20%CE%B1-Glucosidases%20by%20Synthetic%20Thio-fructofuranoside&rft.jtitle=Bioscience,%20biotechnology,%20and%20biochemistry&rft.au=KISO,%20Taro&rft.date=2003-01-01&rft.volume=67&rft.issue=8&rft.spage=1719&rft.epage=1724&rft.pages=1719-1724&rft.issn=0916-8451&rft.eissn=1347-6947&rft_id=info:doi/10.1271/bbb.67.1719&rft_dat=%3Cproquest_pubme%3E73614987%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=73614987&rft_id=info:pmid/12951505&rfr_iscdi=true |