Inhibitory Effects of Plant Phenols on the Activity of Selected Enzymes
Selected enzymes (α-amylase, trypsin, and lysozyme) were allowed to react with some simple phenolic and related compounds (caffeic acid, chlorogenic acid, ferulic acid, gallic acid, m-, o-, and p-dihydroxybenzenes, quinic acid, and p-benzoquinone). The derivatized enzymes obtained were characterized...
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| Veröffentlicht in: | Journal of agricultural and food chemistry 2002-06, Vol.50 (12), p.3566-3571 |
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| container_issue | 12 |
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| container_title | Journal of agricultural and food chemistry |
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| creator | Rohn, Sascha Rawel, Harshadrai M Kroll, Jürgen |
| description | Selected enzymes (α-amylase, trypsin, and lysozyme) were allowed to react with some simple phenolic and related compounds (caffeic acid, chlorogenic acid, ferulic acid, gallic acid, m-, o-, and p-dihydroxybenzenes, quinic acid, and p-benzoquinone). The derivatized enzymes obtained were characterized in terms of their activity. In vitro experiments showed that the enzymatic activity of the derivatives was adversely affected. This enzyme inhibition depended on the reactivity of the phenolic and related substances tested as well as on the kind of substrate applied. The decrease in the activity was accompanied by a reduction in the amount of free amino and thiol groups, as well as tryptophan residues, which resulted from the covalent attachment of the phenolic and related compounds to these reactive nucleophilic sites in the enzymes. The enzyme inhibition correlates well with the blocking of the mentioned amino acid side chains. Keywords: Enzyme activity; plant phenolic substances; α-amylase; trypsin; lysozyme |
| doi_str_mv | 10.1021/jf011714b |
| format | Article |
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The derivatized enzymes obtained were characterized in terms of their activity. In vitro experiments showed that the enzymatic activity of the derivatives was adversely affected. This enzyme inhibition depended on the reactivity of the phenolic and related substances tested as well as on the kind of substrate applied. The decrease in the activity was accompanied by a reduction in the amount of free amino and thiol groups, as well as tryptophan residues, which resulted from the covalent attachment of the phenolic and related compounds to these reactive nucleophilic sites in the enzymes. The enzyme inhibition correlates well with the blocking of the mentioned amino acid side chains. Keywords: Enzyme activity; plant phenolic substances; α-amylase; trypsin; lysozyme</description><identifier>ISSN: 0021-8561</identifier><identifier>EISSN: 1520-5118</identifier><identifier>DOI: 10.1021/jf011714b</identifier><identifier>PMID: 12033830</identifier><identifier>CODEN: JAFCAU</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>alpha-Amylases - antagonists & inhibitors ; alpha-Amylases - chemistry ; alpha-Amylases - metabolism ; Analytical, structural and metabolic biochemistry ; Benzoquinones - pharmacology ; Biological and medical sciences ; Caffeic Acids - pharmacology ; Chlorogenic Acid - pharmacology ; Coumaric Acids - pharmacology ; Enzyme Inhibitors - pharmacology ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Gallic Acid - pharmacology ; Hydrolases ; Hydroquinones - pharmacology ; Muramidase - antagonists & inhibitors ; Muramidase - chemistry ; Muramidase - metabolism ; Phenols - chemistry ; Phenols - pharmacology ; Plants - chemistry ; Quinic Acid - pharmacology ; Trypsin - chemistry ; Trypsin - metabolism ; Trypsin Inhibitors - pharmacology</subject><ispartof>Journal of agricultural and food chemistry, 2002-06, Vol.50 (12), p.3566-3571</ispartof><rights>Copyright © 2002 American Chemical Society</rights><rights>2002 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a445t-44da1dd04685c05ed54c47d8cee3c932ee480ef259c1b28495c608852b6d84813</citedby><cites>FETCH-LOGICAL-a445t-44da1dd04685c05ed54c47d8cee3c932ee480ef259c1b28495c608852b6d84813</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/jf011714b$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/jf011714b$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=13696488$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12033830$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rohn, Sascha</creatorcontrib><creatorcontrib>Rawel, Harshadrai M</creatorcontrib><creatorcontrib>Kroll, Jürgen</creatorcontrib><title>Inhibitory Effects of Plant Phenols on the Activity of Selected Enzymes</title><title>Journal of agricultural and food chemistry</title><addtitle>J. Agric. Food Chem</addtitle><description>Selected enzymes (α-amylase, trypsin, and lysozyme) were allowed to react with some simple phenolic and related compounds (caffeic acid, chlorogenic acid, ferulic acid, gallic acid, m-, o-, and p-dihydroxybenzenes, quinic acid, and p-benzoquinone). The derivatized enzymes obtained were characterized in terms of their activity. In vitro experiments showed that the enzymatic activity of the derivatives was adversely affected. This enzyme inhibition depended on the reactivity of the phenolic and related substances tested as well as on the kind of substrate applied. The decrease in the activity was accompanied by a reduction in the amount of free amino and thiol groups, as well as tryptophan residues, which resulted from the covalent attachment of the phenolic and related compounds to these reactive nucleophilic sites in the enzymes. The enzyme inhibition correlates well with the blocking of the mentioned amino acid side chains. Keywords: Enzyme activity; plant phenolic substances; α-amylase; trypsin; lysozyme</description><subject>alpha-Amylases - antagonists & inhibitors</subject><subject>alpha-Amylases - chemistry</subject><subject>alpha-Amylases - metabolism</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Benzoquinones - pharmacology</subject><subject>Biological and medical sciences</subject><subject>Caffeic Acids - pharmacology</subject><subject>Chlorogenic Acid - pharmacology</subject><subject>Coumaric Acids - pharmacology</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gallic Acid - pharmacology</subject><subject>Hydrolases</subject><subject>Hydroquinones - pharmacology</subject><subject>Muramidase - antagonists & inhibitors</subject><subject>Muramidase - chemistry</subject><subject>Muramidase - metabolism</subject><subject>Phenols - chemistry</subject><subject>Phenols - pharmacology</subject><subject>Plants - chemistry</subject><subject>Quinic Acid - pharmacology</subject><subject>Trypsin - chemistry</subject><subject>Trypsin - metabolism</subject><subject>Trypsin Inhibitors - pharmacology</subject><issn>0021-8561</issn><issn>1520-5118</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpt0EFLwzAUB_AgipvTg19AelHwUE2apE2Po8xtMnCyiceQpq-ss2tnkonz05ux4S6eHrz348_jj9A1wQ8ER-RxWWJCEsLyE9QlPMIhJ0Scoi72x1DwmHTQhbVLjLHgCT5HHRJhSgXFXTQcN4sqr1xrtsGgLEE7G7RlMK1V44LpApq29osmcAsI-tpVX5Xb7sAMam-hCAbNz3YF9hKdlaq2cHWYPfT2NJhno3DyMhxn_UmoGOMuZKxQpCgwiwXXmEPBmWZJITQA1SmNAJjAUEY81SSPBEu5jrEQPMrjQjBBaA_d7XPXpv3cgHVyVVkNtf8X2o2VCUkYo1Hs4f0eatNaa6CUa1OtlNlKguWuNfnXmrc3h9BNvoLiKA81eXB7AMpqVZdGNbqyR0fjNGZCeBfuXWUdfP_dlfmQcUITLufTmcyeZ6_DdJTJ92Ou0lYu241pfHf_PPgLXS-N9Q</recordid><startdate>20020605</startdate><enddate>20020605</enddate><creator>Rohn, Sascha</creator><creator>Rawel, Harshadrai M</creator><creator>Kroll, Jürgen</creator><general>American Chemical Society</general><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>7X8</scope></search><sort><creationdate>20020605</creationdate><title>Inhibitory Effects of Plant Phenols on the Activity of Selected Enzymes</title><author>Rohn, Sascha ; Rawel, Harshadrai M ; Kroll, Jürgen</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a445t-44da1dd04685c05ed54c47d8cee3c932ee480ef259c1b28495c608852b6d84813</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>alpha-Amylases - antagonists & inhibitors</topic><topic>alpha-Amylases - chemistry</topic><topic>alpha-Amylases - metabolism</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Benzoquinones - pharmacology</topic><topic>Biological and medical sciences</topic><topic>Caffeic Acids - pharmacology</topic><topic>Chlorogenic Acid - pharmacology</topic><topic>Coumaric Acids - pharmacology</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gallic Acid - pharmacology</topic><topic>Hydrolases</topic><topic>Hydroquinones - pharmacology</topic><topic>Muramidase - antagonists & inhibitors</topic><topic>Muramidase - chemistry</topic><topic>Muramidase - metabolism</topic><topic>Phenols - chemistry</topic><topic>Phenols - pharmacology</topic><topic>Plants - chemistry</topic><topic>Quinic Acid - pharmacology</topic><topic>Trypsin - chemistry</topic><topic>Trypsin - metabolism</topic><topic>Trypsin Inhibitors - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rohn, Sascha</creatorcontrib><creatorcontrib>Rawel, Harshadrai M</creatorcontrib><creatorcontrib>Kroll, Jürgen</creatorcontrib><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>MEDLINE - Academic</collection><jtitle>Journal of agricultural and food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rohn, Sascha</au><au>Rawel, Harshadrai M</au><au>Kroll, Jürgen</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Inhibitory Effects of Plant Phenols on the Activity of Selected Enzymes</atitle><jtitle>Journal of agricultural and food chemistry</jtitle><addtitle>J. Agric. Food Chem</addtitle><date>2002-06-05</date><risdate>2002</risdate><volume>50</volume><issue>12</issue><spage>3566</spage><epage>3571</epage><pages>3566-3571</pages><issn>0021-8561</issn><eissn>1520-5118</eissn><coden>JAFCAU</coden><abstract>Selected enzymes (α-amylase, trypsin, and lysozyme) were allowed to react with some simple phenolic and related compounds (caffeic acid, chlorogenic acid, ferulic acid, gallic acid, m-, o-, and p-dihydroxybenzenes, quinic acid, and p-benzoquinone). The derivatized enzymes obtained were characterized in terms of their activity. In vitro experiments showed that the enzymatic activity of the derivatives was adversely affected. This enzyme inhibition depended on the reactivity of the phenolic and related substances tested as well as on the kind of substrate applied. The decrease in the activity was accompanied by a reduction in the amount of free amino and thiol groups, as well as tryptophan residues, which resulted from the covalent attachment of the phenolic and related compounds to these reactive nucleophilic sites in the enzymes. The enzyme inhibition correlates well with the blocking of the mentioned amino acid side chains. Keywords: Enzyme activity; plant phenolic substances; α-amylase; trypsin; lysozyme</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>12033830</pmid><doi>10.1021/jf011714b</doi><tpages>6</tpages></addata></record> |
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| subjects | alpha-Amylases - antagonists & inhibitors alpha-Amylases - chemistry alpha-Amylases - metabolism Analytical, structural and metabolic biochemistry Benzoquinones - pharmacology Biological and medical sciences Caffeic Acids - pharmacology Chlorogenic Acid - pharmacology Coumaric Acids - pharmacology Enzyme Inhibitors - pharmacology Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Gallic Acid - pharmacology Hydrolases Hydroquinones - pharmacology Muramidase - antagonists & inhibitors Muramidase - chemistry Muramidase - metabolism Phenols - chemistry Phenols - pharmacology Plants - chemistry Quinic Acid - pharmacology Trypsin - chemistry Trypsin - metabolism Trypsin Inhibitors - pharmacology |
| title | Inhibitory Effects of Plant Phenols on the Activity of Selected Enzymes |
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