Isolation and characterization of brown algal polyphenols as inhibitors of alpha-amylase, lipase and trypsin
Extracts of Ascophyllum nodosum, Fucus serratus, F. vesiculosus and Pelvetia canaliculata contain inhibitors of alpha -amylase, lipase and trypsin. The inhibitors were isolated and identified by super(1)H NMR spectroscopy as polyphenols which have apparent molecular weights in the range from 30 000...
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| Veröffentlicht in: | Journal of applied phycology 1989-12, Vol.1 (4), p.319-323 |
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| container_title | Journal of applied phycology |
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| creator | Barwell, C.J. (Portsmouth Polytechnic, Portsmouth, Hampshire (UK). School of Pharmacy and Biomedical Sciences) Blunden, G Manandhar, P.D |
| description | Extracts of Ascophyllum nodosum, Fucus serratus, F. vesiculosus and Pelvetia canaliculata contain inhibitors of alpha -amylase, lipase and trypsin. The inhibitors were isolated and identified by super(1)H NMR spectroscopy as polyphenols which have apparent molecular weights in the range from 30 000 to 100 000 daltons, as determined by ultra-filtration with Amicon membranes. These polyphenols account for the whole of the inhibitory activity in crude algal extracts. The compounds inhibit alpha -amylase and trypsin in an apparently non-competitive manner, when preincubated with the enzymes, and the inhibition is directly proportional to the concentration of the inhibitor. Starch protects alpha -amylase when added to the enzyme together with the inhibitors. Under this condition the effectiveness of the inhibitors is reduced ten-fold. |
| doi_str_mv | 10.1007/BF00003468 |
| format | Article |
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(Portsmouth Polytechnic, Portsmouth, Hampshire (UK). School of Pharmacy and Biomedical Sciences) ; Blunden, G ; Manandhar, P.D</creator><creatorcontrib>Barwell, C.J. (Portsmouth Polytechnic, Portsmouth, Hampshire (UK). School of Pharmacy and Biomedical Sciences) ; Blunden, G ; Manandhar, P.D</creatorcontrib><description>Extracts of Ascophyllum nodosum, Fucus serratus, F. vesiculosus and Pelvetia canaliculata contain inhibitors of alpha -amylase, lipase and trypsin. The inhibitors were isolated and identified by super(1)H NMR spectroscopy as polyphenols which have apparent molecular weights in the range from 30 000 to 100 000 daltons, as determined by ultra-filtration with Amicon membranes. These polyphenols account for the whole of the inhibitory activity in crude algal extracts. The compounds inhibit alpha -amylase and trypsin in an apparently non-competitive manner, when preincubated with the enzymes, and the inhibition is directly proportional to the concentration of the inhibitor. Starch protects alpha -amylase when added to the enzyme together with the inhibitors. Under this condition the effectiveness of the inhibitors is reduced ten-fold.</description><identifier>ISSN: 0921-8971</identifier><identifier>EISSN: 1573-5176</identifier><identifier>DOI: 10.1007/BF00003468</identifier><language>eng</language><publisher>Dordrecht: Springer</publisher><subject>ALFA AMILASA ; ALGAE ; ALIMENT POUR ANIMAUX ; ALIMENT SANTE ; ALIMENTOS SANOS ; ALPHA AMYLASE ; Ascophyllum nodosum ; Biological and medical sciences ; Cell biochemistry ; Cell physiology ; COMPOSE PHENOLIQUE ; COMPUESTOS FENOLICOS ; ENZYME INHIBITORS ; ESTERASAS ; ESTERASE ; ESTERASES ; FEEDS ; Fucus serratus ; Fucus vesiculosus ; Fundamental and applied biological sciences. Psychology ; HEALTH FOODS ; INHIBIDORES DE ENZIMAS ; INHIBITEUR D'ENZYME ; Marine ; Pelvetia canaliculata ; Phaeophyta ; PHENOLIC COMPOUNDS ; PIENSOS ; Plant physiology and development ; TRIPSINA ; TRYPSIN ; TRYPSINE</subject><ispartof>Journal of applied phycology, 1989-12, Vol.1 (4), p.319-323</ispartof><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c226t-f1e62ea05fd20d81ea3115dd505d62f53df11ab4c93c36842bcf1fc0d5401f593</citedby><cites>FETCH-LOGICAL-c226t-f1e62ea05fd20d81ea3115dd505d62f53df11ab4c93c36842bcf1fc0d5401f593</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27922,27923</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19286097$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Barwell, C.J. (Portsmouth Polytechnic, Portsmouth, Hampshire (UK). School of Pharmacy and Biomedical Sciences)</creatorcontrib><creatorcontrib>Blunden, G</creatorcontrib><creatorcontrib>Manandhar, P.D</creatorcontrib><title>Isolation and characterization of brown algal polyphenols as inhibitors of alpha-amylase, lipase and trypsin</title><title>Journal of applied phycology</title><description>Extracts of Ascophyllum nodosum, Fucus serratus, F. vesiculosus and Pelvetia canaliculata contain inhibitors of alpha -amylase, lipase and trypsin. The inhibitors were isolated and identified by super(1)H NMR spectroscopy as polyphenols which have apparent molecular weights in the range from 30 000 to 100 000 daltons, as determined by ultra-filtration with Amicon membranes. These polyphenols account for the whole of the inhibitory activity in crude algal extracts. The compounds inhibit alpha -amylase and trypsin in an apparently non-competitive manner, when preincubated with the enzymes, and the inhibition is directly proportional to the concentration of the inhibitor. Starch protects alpha -amylase when added to the enzyme together with the inhibitors. Under this condition the effectiveness of the inhibitors is reduced ten-fold.</description><subject>ALFA AMILASA</subject><subject>ALGAE</subject><subject>ALIMENT POUR ANIMAUX</subject><subject>ALIMENT SANTE</subject><subject>ALIMENTOS SANOS</subject><subject>ALPHA AMYLASE</subject><subject>Ascophyllum nodosum</subject><subject>Biological and medical sciences</subject><subject>Cell biochemistry</subject><subject>Cell physiology</subject><subject>COMPOSE PHENOLIQUE</subject><subject>COMPUESTOS FENOLICOS</subject><subject>ENZYME INHIBITORS</subject><subject>ESTERASAS</subject><subject>ESTERASE</subject><subject>ESTERASES</subject><subject>FEEDS</subject><subject>Fucus serratus</subject><subject>Fucus vesiculosus</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>HEALTH FOODS</subject><subject>INHIBIDORES DE ENZIMAS</subject><subject>INHIBITEUR D'ENZYME</subject><subject>Marine</subject><subject>Pelvetia canaliculata</subject><subject>Phaeophyta</subject><subject>PHENOLIC COMPOUNDS</subject><subject>PIENSOS</subject><subject>Plant physiology and development</subject><subject>TRIPSINA</subject><subject>TRYPSIN</subject><subject>TRYPSINE</subject><issn>0921-8971</issn><issn>1573-5176</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><recordid>eNpFkDFPwzAQRi0EEqWwMDJlgQER8Dlx4oxQUahUwQJzdHHs1siNg50KhV9PSir1lk-6e_eGj5BLoPdAaf7wNKfDJGkmjsgEeJ7EHPLsmExowSAWRQ6n5CyErwEqBIgJsYvgLHbGNRE2dSTX6FF2ypvfcel0VHn3M1ztCm3UOtu3a9U4GyIMkWnWpjKd82EHom3XGOOmtxjUXWRNO-S_tvN9G0xzTk402qAu9jkln_Pnj9lrvHx_Wcwel7FkLOtiDSpjCinXNaO1AIUJAK9rTnmdMc2TWgNglcoikUkmUlZJDVrSmqcUNC-SKbkZva1331sVunJjglTWYqPcNpTAuYAMduDtCErvQvBKl603G_R9CbTcFVoeCh3g670Vg0SrPTbShMNHwURGi3zgrkZOoytx5QfmbVkMEkhZ8gfxeX67</recordid><startdate>198912</startdate><enddate>198912</enddate><creator>Barwell, C.J. (Portsmouth Polytechnic, Portsmouth, Hampshire (UK). School of Pharmacy and Biomedical Sciences)</creator><creator>Blunden, G</creator><creator>Manandhar, P.D</creator><general>Springer</general><scope>FBQ</scope><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>8FD</scope><scope>F1W</scope><scope>FR3</scope><scope>H95</scope><scope>H99</scope><scope>L.F</scope><scope>L.G</scope><scope>M7N</scope><scope>P64</scope></search><sort><creationdate>198912</creationdate><title>Isolation and characterization of brown algal polyphenols as inhibitors of alpha-amylase, lipase and trypsin</title><author>Barwell, C.J. (Portsmouth Polytechnic, Portsmouth, Hampshire (UK). School of Pharmacy and Biomedical Sciences) ; Blunden, G ; Manandhar, P.D</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c226t-f1e62ea05fd20d81ea3115dd505d62f53df11ab4c93c36842bcf1fc0d5401f593</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>ALFA AMILASA</topic><topic>ALGAE</topic><topic>ALIMENT POUR ANIMAUX</topic><topic>ALIMENT SANTE</topic><topic>ALIMENTOS SANOS</topic><topic>ALPHA AMYLASE</topic><topic>Ascophyllum nodosum</topic><topic>Biological and medical sciences</topic><topic>Cell biochemistry</topic><topic>Cell physiology</topic><topic>COMPOSE PHENOLIQUE</topic><topic>COMPUESTOS FENOLICOS</topic><topic>ENZYME INHIBITORS</topic><topic>ESTERASAS</topic><topic>ESTERASE</topic><topic>ESTERASES</topic><topic>FEEDS</topic><topic>Fucus serratus</topic><topic>Fucus vesiculosus</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>HEALTH FOODS</topic><topic>INHIBIDORES DE ENZIMAS</topic><topic>INHIBITEUR D'ENZYME</topic><topic>Marine</topic><topic>Pelvetia canaliculata</topic><topic>Phaeophyta</topic><topic>PHENOLIC COMPOUNDS</topic><topic>PIENSOS</topic><topic>Plant physiology and development</topic><topic>TRIPSINA</topic><topic>TRYPSIN</topic><topic>TRYPSINE</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Barwell, C.J. (Portsmouth Polytechnic, Portsmouth, Hampshire (UK). School of Pharmacy and Biomedical Sciences)</creatorcontrib><creatorcontrib>Blunden, G</creatorcontrib><creatorcontrib>Manandhar, P.D</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Engineering Research Database</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>ASFA: Marine Biotechnology Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Marine Biotechnology Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Journal of applied phycology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Barwell, C.J. (Portsmouth Polytechnic, Portsmouth, Hampshire (UK). School of Pharmacy and Biomedical Sciences)</au><au>Blunden, G</au><au>Manandhar, P.D</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Isolation and characterization of brown algal polyphenols as inhibitors of alpha-amylase, lipase and trypsin</atitle><jtitle>Journal of applied phycology</jtitle><date>1989-12</date><risdate>1989</risdate><volume>1</volume><issue>4</issue><spage>319</spage><epage>323</epage><pages>319-323</pages><issn>0921-8971</issn><eissn>1573-5176</eissn><abstract>Extracts of Ascophyllum nodosum, Fucus serratus, F. vesiculosus and Pelvetia canaliculata contain inhibitors of alpha -amylase, lipase and trypsin. The inhibitors were isolated and identified by super(1)H NMR spectroscopy as polyphenols which have apparent molecular weights in the range from 30 000 to 100 000 daltons, as determined by ultra-filtration with Amicon membranes. These polyphenols account for the whole of the inhibitory activity in crude algal extracts. The compounds inhibit alpha -amylase and trypsin in an apparently non-competitive manner, when preincubated with the enzymes, and the inhibition is directly proportional to the concentration of the inhibitor. Starch protects alpha -amylase when added to the enzyme together with the inhibitors. Under this condition the effectiveness of the inhibitors is reduced ten-fold.</abstract><cop>Dordrecht</cop><pub>Springer</pub><doi>10.1007/BF00003468</doi><tpages>5</tpages></addata></record> |
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| ispartof | Journal of applied phycology, 1989-12, Vol.1 (4), p.319-323 |
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| subjects | ALFA AMILASA ALGAE ALIMENT POUR ANIMAUX ALIMENT SANTE ALIMENTOS SANOS ALPHA AMYLASE Ascophyllum nodosum Biological and medical sciences Cell biochemistry Cell physiology COMPOSE PHENOLIQUE COMPUESTOS FENOLICOS ENZYME INHIBITORS ESTERASAS ESTERASE ESTERASES FEEDS Fucus serratus Fucus vesiculosus Fundamental and applied biological sciences. Psychology HEALTH FOODS INHIBIDORES DE ENZIMAS INHIBITEUR D'ENZYME Marine Pelvetia canaliculata Phaeophyta PHENOLIC COMPOUNDS PIENSOS Plant physiology and development TRIPSINA TRYPSIN TRYPSINE |
| title | Isolation and characterization of brown algal polyphenols as inhibitors of alpha-amylase, lipase and trypsin |
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