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Peptides with Angiotensin I-Converting Enzyme (ACE) Inhibitory Activity from Defibrinated, Hydrolyzed Bovine Plasma
Defibrinated bovine plasma (DBP) was treated with the microbial protease Flavourzyme to obtain protein hydrolysates with various degrees of hydrolysis (DH). The angiotensin I-converting enzyme (ACE) inhibiting activity of the hydrolyzed protein was assessed with hippuryl-His-Leu as the substrate. Th...
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| Published in: | Journal of agricultural and food chemistry 2002-11, Vol.50 (24), p.6981-6988 |
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| Main Authors: | , , , , , |
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| cites | cdi_FETCH-LOGICAL-a444t-20d1d4ea0d7e315d68f483be5a1656e7372f8e8f79da57ae2b2ce754afe420df3 |
| container_end_page | 6988 |
| container_issue | 24 |
| container_start_page | 6981 |
| container_title | Journal of agricultural and food chemistry |
| container_volume | 50 |
| creator | Wanasundara, P. K. Janitha P. D Ross, Andrew R. S Amarowicz, Ryszard Ambrose, Steve J Pegg, Ronald B Shand, Phyllis J |
| description | Defibrinated bovine plasma (DBP) was treated with the microbial protease Flavourzyme to obtain protein hydrolysates with various degrees of hydrolysis (DH). The angiotensin I-converting enzyme (ACE) inhibiting activity of the hydrolyzed protein was assessed with hippuryl-His-Leu as the substrate. The amount of hippuric acid released, due to uninhibited ACE activity, was determined by high-performance liquid chromatography. ACE inhibiting (ACEI) activity was found to increase with increasing DH; the 43% DH hydrolysate exhibited the highest activity and had an IC50 of 1.08 mg/mL. Peptide fractions with high ACEI activity were isolated using size exclusion chromatography. The fraction that possessed the highest ACEI activity contained peptides with GYP, HL(I), HPY, HPGH, L(I)F, SPY, and YPH sequence motifs, as determined by reversed-phase liquid chromatography−tandem mass spectrometry using a novel immonium precursor-ion scanning technique. Some of these motifs correspond to sequences found in bovine serum albumin, a potential source of ACEI peptides in bovine plasma. Keywords: Angiotensin I-converting enzyme inhibitors; bioactive peptides; immonium precursor-ions; LC-MS; MALDI-TOF MS; plasma protein; peptide sequencing; protein hydrolysis |
| doi_str_mv | 10.1021/jf025592e |
| format | article |
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K. Janitha P. D ; Ross, Andrew R. S ; Amarowicz, Ryszard ; Ambrose, Steve J ; Pegg, Ronald B ; Shand, Phyllis J</creator><creatorcontrib>Wanasundara, P. K. Janitha P. D ; Ross, Andrew R. S ; Amarowicz, Ryszard ; Ambrose, Steve J ; Pegg, Ronald B ; Shand, Phyllis J</creatorcontrib><description>Defibrinated bovine plasma (DBP) was treated with the microbial protease Flavourzyme to obtain protein hydrolysates with various degrees of hydrolysis (DH). The angiotensin I-converting enzyme (ACE) inhibiting activity of the hydrolyzed protein was assessed with hippuryl-His-Leu as the substrate. The amount of hippuric acid released, due to uninhibited ACE activity, was determined by high-performance liquid chromatography. ACE inhibiting (ACEI) activity was found to increase with increasing DH; the 43% DH hydrolysate exhibited the highest activity and had an IC50 of 1.08 mg/mL. Peptide fractions with high ACEI activity were isolated using size exclusion chromatography. The fraction that possessed the highest ACEI activity contained peptides with GYP, HL(I), HPY, HPGH, L(I)F, SPY, and YPH sequence motifs, as determined by reversed-phase liquid chromatography−tandem mass spectrometry using a novel immonium precursor-ion scanning technique. Some of these motifs correspond to sequences found in bovine serum albumin, a potential source of ACEI peptides in bovine plasma. Keywords: Angiotensin I-converting enzyme inhibitors; bioactive peptides; immonium precursor-ions; LC-MS; MALDI-TOF MS; plasma protein; peptide sequencing; protein hydrolysis</description><identifier>ISSN: 0021-8561</identifier><identifier>EISSN: 1520-5118</identifier><identifier>DOI: 10.1021/jf025592e</identifier><identifier>PMID: 12428947</identifier><identifier>CODEN: JAFCAU</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Amino Acid Sequence ; Angiotensin-Converting Enzyme Inhibitors - pharmacology ; Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts ; Animals ; Biological and medical sciences ; Blood Proteins - metabolism ; Blood Proteins - pharmacology ; Cattle ; Chromatography, Gel ; Chromatography, High Pressure Liquid ; Endopeptidases - metabolism ; Fibrin ; Food industries ; Fundamental and applied biological sciences. Psychology ; General pharmacology ; Hippurates - analysis ; Hippurates - metabolism ; Medical sciences ; Peptides - chemistry ; Peptides - pharmacology ; Peptidyl-Dipeptidase A - metabolism ; Pharmacognosy. Homeopathy. Health food ; Pharmacology. Drug treatments ; Protein Hydrolysates - pharmacology ; Spectrometry, Mass, Electrospray Ionization ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</subject><ispartof>Journal of agricultural and food chemistry, 2002-11, Vol.50 (24), p.6981-6988</ispartof><rights>Copyright © 2002 American Chemical Society</rights><rights>2003 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a444t-20d1d4ea0d7e315d68f483be5a1656e7372f8e8f79da57ae2b2ce754afe420df3</citedby><cites>FETCH-LOGICAL-a444t-20d1d4ea0d7e315d68f483be5a1656e7372f8e8f79da57ae2b2ce754afe420df3</cites></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=14027385$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12428947$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wanasundara, P. K. Janitha P. D</creatorcontrib><creatorcontrib>Ross, Andrew R. S</creatorcontrib><creatorcontrib>Amarowicz, Ryszard</creatorcontrib><creatorcontrib>Ambrose, Steve J</creatorcontrib><creatorcontrib>Pegg, Ronald B</creatorcontrib><creatorcontrib>Shand, Phyllis J</creatorcontrib><title>Peptides with Angiotensin I-Converting Enzyme (ACE) Inhibitory Activity from Defibrinated, Hydrolyzed Bovine Plasma</title><title>Journal of agricultural and food chemistry</title><addtitle>J. Agric. Food Chem</addtitle><description>Defibrinated bovine plasma (DBP) was treated with the microbial protease Flavourzyme to obtain protein hydrolysates with various degrees of hydrolysis (DH). The angiotensin I-converting enzyme (ACE) inhibiting activity of the hydrolyzed protein was assessed with hippuryl-His-Leu as the substrate. The amount of hippuric acid released, due to uninhibited ACE activity, was determined by high-performance liquid chromatography. ACE inhibiting (ACEI) activity was found to increase with increasing DH; the 43% DH hydrolysate exhibited the highest activity and had an IC50 of 1.08 mg/mL. Peptide fractions with high ACEI activity were isolated using size exclusion chromatography. The fraction that possessed the highest ACEI activity contained peptides with GYP, HL(I), HPY, HPGH, L(I)F, SPY, and YPH sequence motifs, as determined by reversed-phase liquid chromatography−tandem mass spectrometry using a novel immonium precursor-ion scanning technique. Some of these motifs correspond to sequences found in bovine serum albumin, a potential source of ACEI peptides in bovine plasma. Keywords: Angiotensin I-converting enzyme inhibitors; bioactive peptides; immonium precursor-ions; LC-MS; MALDI-TOF MS; plasma protein; peptide sequencing; protein hydrolysis</description><subject>Amino Acid Sequence</subject><subject>Angiotensin-Converting Enzyme Inhibitors - pharmacology</subject><subject>Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Blood Proteins - metabolism</subject><subject>Blood Proteins - pharmacology</subject><subject>Cattle</subject><subject>Chromatography, Gel</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Endopeptidases - metabolism</subject><subject>Fibrin</subject><subject>Food industries</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>General pharmacology</subject><subject>Hippurates - analysis</subject><subject>Hippurates - metabolism</subject><subject>Medical sciences</subject><subject>Peptides - chemistry</subject><subject>Peptides - pharmacology</subject><subject>Peptidyl-Dipeptidase A - metabolism</subject><subject>Pharmacognosy. Homeopathy. Health food</subject><subject>Pharmacology. Drug treatments</subject><subject>Protein Hydrolysates - pharmacology</subject><subject>Spectrometry, Mass, Electrospray Ionization</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</subject><issn>0021-8561</issn><issn>1520-5118</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><recordid>eNpt0EFv0zAUB3ALgVgZHPgCyBcmJhGwHTt2jqV0rNMkKjEQN8uNnzeXxCm2W5Z9eoJarRdOPrzf--v5j9BrSj5QwujHtSNMiJrBEzShgpFCUKqeogkZh4USFT1BL1JaE0KUkOQ5OqGMM1VzOUFpCZvsLST8x-c7PA23vs8Qkg94Ucz6sIOYfbjF8_AwdIDfTWfzc7wId37lcx8HPG2y3_k8YBf7Dn8G51fRB5PBvseXg419OzyAxZ_6nQ-Al61JnXmJnjnTJnh1eE_R94v5zeyyuP76ZTGbXheGc54LRiy1HAyxEkoqbKUcV-UKhKGVqECWkjkFysnaGiENsBVrQApuHPBx15Wn6Gyfu4n97y2krDufGmhbE6DfJi1ZpVjN6QjP97CJfUoRnN5E35k4aEr0v4b1Y8OjfXMI3a46sEd5qHQEbw_ApMa0LprQ-HR0nDBZKjG6Yu98ynD_ODfxl67Gvwl9s_ymSSl_qqsftb465pom6XW_jWHs7j8H_gWbIJ76</recordid><startdate>20021120</startdate><enddate>20021120</enddate><creator>Wanasundara, P. K. Janitha P. D</creator><creator>Ross, Andrew R. S</creator><creator>Amarowicz, Ryszard</creator><creator>Ambrose, Steve J</creator><creator>Pegg, Ronald B</creator><creator>Shand, Phyllis J</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>20021120</creationdate><title>Peptides with Angiotensin I-Converting Enzyme (ACE) Inhibitory Activity from Defibrinated, Hydrolyzed Bovine Plasma</title><author>Wanasundara, P. K. Janitha P. D ; Ross, Andrew R. S ; Amarowicz, Ryszard ; Ambrose, Steve J ; Pegg, Ronald B ; Shand, Phyllis J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a444t-20d1d4ea0d7e315d68f483be5a1656e7372f8e8f79da57ae2b2ce754afe420df3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Amino Acid Sequence</topic><topic>Angiotensin-Converting Enzyme Inhibitors - pharmacology</topic><topic>Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Blood Proteins - metabolism</topic><topic>Blood Proteins - pharmacology</topic><topic>Cattle</topic><topic>Chromatography, Gel</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Endopeptidases - metabolism</topic><topic>Fibrin</topic><topic>Food industries</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>General pharmacology</topic><topic>Hippurates - analysis</topic><topic>Hippurates - metabolism</topic><topic>Medical sciences</topic><topic>Peptides - chemistry</topic><topic>Peptides - pharmacology</topic><topic>Peptidyl-Dipeptidase A - metabolism</topic><topic>Pharmacognosy. Homeopathy. Health food</topic><topic>Pharmacology. Drug treatments</topic><topic>Protein Hydrolysates - pharmacology</topic><topic>Spectrometry, Mass, Electrospray Ionization</topic><topic>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wanasundara, P. K. Janitha P. D</creatorcontrib><creatorcontrib>Ross, Andrew R. S</creatorcontrib><creatorcontrib>Amarowicz, Ryszard</creatorcontrib><creatorcontrib>Ambrose, Steve J</creatorcontrib><creatorcontrib>Pegg, Ronald B</creatorcontrib><creatorcontrib>Shand, Phyllis J</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>Wanasundara, P. K. Janitha P. D</au><au>Ross, Andrew R. S</au><au>Amarowicz, Ryszard</au><au>Ambrose, Steve J</au><au>Pegg, Ronald B</au><au>Shand, Phyllis J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Peptides with Angiotensin I-Converting Enzyme (ACE) Inhibitory Activity from Defibrinated, Hydrolyzed Bovine Plasma</atitle><jtitle>Journal of agricultural and food chemistry</jtitle><addtitle>J. Agric. Food Chem</addtitle><date>2002-11-20</date><risdate>2002</risdate><volume>50</volume><issue>24</issue><spage>6981</spage><epage>6988</epage><pages>6981-6988</pages><issn>0021-8561</issn><eissn>1520-5118</eissn><coden>JAFCAU</coden><abstract>Defibrinated bovine plasma (DBP) was treated with the microbial protease Flavourzyme to obtain protein hydrolysates with various degrees of hydrolysis (DH). The angiotensin I-converting enzyme (ACE) inhibiting activity of the hydrolyzed protein was assessed with hippuryl-His-Leu as the substrate. The amount of hippuric acid released, due to uninhibited ACE activity, was determined by high-performance liquid chromatography. ACE inhibiting (ACEI) activity was found to increase with increasing DH; the 43% DH hydrolysate exhibited the highest activity and had an IC50 of 1.08 mg/mL. Peptide fractions with high ACEI activity were isolated using size exclusion chromatography. The fraction that possessed the highest ACEI activity contained peptides with GYP, HL(I), HPY, HPGH, L(I)F, SPY, and YPH sequence motifs, as determined by reversed-phase liquid chromatography−tandem mass spectrometry using a novel immonium precursor-ion scanning technique. Some of these motifs correspond to sequences found in bovine serum albumin, a potential source of ACEI peptides in bovine plasma. Keywords: Angiotensin I-converting enzyme inhibitors; bioactive peptides; immonium precursor-ions; LC-MS; MALDI-TOF MS; plasma protein; peptide sequencing; protein hydrolysis</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>12428947</pmid><doi>10.1021/jf025592e</doi><tpages>8</tpages></addata></record> |
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| identifier | ISSN: 0021-8561 |
| ispartof | Journal of agricultural and food chemistry, 2002-11, Vol.50 (24), p.6981-6988 |
| issn | 0021-8561 1520-5118 |
| language | eng |
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| source | American Chemical Society:Jisc Collections:American Chemical Society Read & Publish Agreement 2022-2024 (Reading list) |
| subjects | Amino Acid Sequence Angiotensin-Converting Enzyme Inhibitors - pharmacology Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts Animals Biological and medical sciences Blood Proteins - metabolism Blood Proteins - pharmacology Cattle Chromatography, Gel Chromatography, High Pressure Liquid Endopeptidases - metabolism Fibrin Food industries Fundamental and applied biological sciences. Psychology General pharmacology Hippurates - analysis Hippurates - metabolism Medical sciences Peptides - chemistry Peptides - pharmacology Peptidyl-Dipeptidase A - metabolism Pharmacognosy. Homeopathy. Health food Pharmacology. Drug treatments Protein Hydrolysates - pharmacology Spectrometry, Mass, Electrospray Ionization Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization |
| title | Peptides with Angiotensin I-Converting Enzyme (ACE) Inhibitory Activity from Defibrinated, Hydrolyzed Bovine Plasma |
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