LC-Q-TOF/MS based identification and in silico verification of ACE-inhibitory peptides in Giresun (Turkey) hazelnut cakes
Hazelnut ( Corylus avellana L.) cakes represent are a rich source of proteins. In an effort to valorize industrially cold-pressed hazelnut cakes, angiotensin-converting enzyme (ACE) inhibitory characteristics of hazelnut protein hydrolysates were evaluated. Trypsin, chymotrypsin and thermolysin hydr...
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| Veröffentlicht in: | European food research & technology 2021-05, Vol.247 (5), p.1189-1198 |
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| creator | Çağlar, Ahmet Furkan Çakır, Bilal Gülseren, İbrahim |
| description | Hazelnut (
Corylus avellana
L.) cakes represent are a rich source of proteins. In an effort to valorize industrially cold-pressed hazelnut cakes, angiotensin-converting enzyme (ACE) inhibitory characteristics of hazelnut protein hydrolysates were evaluated. Trypsin, chymotrypsin and thermolysin hydrolysates of hazelnut protein isolates were fractionated using Fast Protein Liquid Chromatography (FPLC). The hydrolysate fractions were tested for ACE inhibitory characteristics and inhibitor peptide identification was based on Liquid Chromatography Quadrupole Time-of-Flight Mass Spectrometry (LC-Q-TOF/MS). Finally, in vitro ACE inhibitory activity was verified using in silico tools. In all cases, some hydrolysate fractions demonstrated ACE inhibitory characteristics, while inhibitory activity widely varied (7–95%) depending on proteolysis conditions. In ACE inhibitory fractions, 179 different peptides were identified. Their potential inhibitory activity was verified in silico for 22 different peptides generated by thermolysin, 3 for chymotrypsin and 4 for trypsin. While the half maximal inhibitory concentration (IC
50
) (0.13–4.83 mg ml
−1
) values were comparable to the previous literature, currently identified sequences were different than ACE inhibitory peptides purified from Asian hazelnuts. The peptides with the highest PeptideRanker scores for each treatment (i.e., SPLAGR, VPHW and PGHF) were studied for their potential ACE binding, Absorption, Distribution, Metabolism, Excretion and Toxicity (ADMET) and circulatory half-life characteristics demonstrating limited pharmokinetic interference, low toxicity as well as comparable short circulation and stronger binding compared to a reference inhibitor peptide (i.e., VPP). Geographical attributes and proteolytic treatments could have a bearing on ACE inhibitory potential of peptides, while hazelnut cakes can be regarded as a valuable resource for ACE inhibitor peptides. |
| doi_str_mv | 10.1007/s00217-021-03700-6 |
| format | Article |
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Corylus avellana
L.) cakes represent are a rich source of proteins. In an effort to valorize industrially cold-pressed hazelnut cakes, angiotensin-converting enzyme (ACE) inhibitory characteristics of hazelnut protein hydrolysates were evaluated. Trypsin, chymotrypsin and thermolysin hydrolysates of hazelnut protein isolates were fractionated using Fast Protein Liquid Chromatography (FPLC). The hydrolysate fractions were tested for ACE inhibitory characteristics and inhibitor peptide identification was based on Liquid Chromatography Quadrupole Time-of-Flight Mass Spectrometry (LC-Q-TOF/MS). Finally, in vitro ACE inhibitory activity was verified using in silico tools. In all cases, some hydrolysate fractions demonstrated ACE inhibitory characteristics, while inhibitory activity widely varied (7–95%) depending on proteolysis conditions. In ACE inhibitory fractions, 179 different peptides were identified. Their potential inhibitory activity was verified in silico for 22 different peptides generated by thermolysin, 3 for chymotrypsin and 4 for trypsin. While the half maximal inhibitory concentration (IC
50
) (0.13–4.83 mg ml
−1
) values were comparable to the previous literature, currently identified sequences were different than ACE inhibitory peptides purified from Asian hazelnuts. The peptides with the highest PeptideRanker scores for each treatment (i.e., SPLAGR, VPHW and PGHF) were studied for their potential ACE binding, Absorption, Distribution, Metabolism, Excretion and Toxicity (ADMET) and circulatory half-life characteristics demonstrating limited pharmokinetic interference, low toxicity as well as comparable short circulation and stronger binding compared to a reference inhibitor peptide (i.e., VPP). Geographical attributes and proteolytic treatments could have a bearing on ACE inhibitory potential of peptides, while hazelnut cakes can be regarded as a valuable resource for ACE inhibitor peptides.</description><identifier>ISSN: 1438-2377</identifier><identifier>EISSN: 1438-2385</identifier><identifier>DOI: 10.1007/s00217-021-03700-6</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Agriculture ; Analytical Chemistry ; Angiotensin ; Binding ; Biotechnology ; Cakes ; Chemistry ; Chemistry and Materials Science ; Chromatography ; Chymotrypsin ; Food Science ; Forestry ; Hazelnuts ; Hydrolysates ; Liquid chromatography ; Mass spectrometry ; Mass spectroscopy ; Original Paper ; Peptides ; Peptidyl-dipeptidase A ; Proteins ; Proteolysis ; Quadrupoles ; Thermolysin ; Toxicity ; Trypsin</subject><ispartof>European food research & technology, 2021-05, Vol.247 (5), p.1189-1198</ispartof><rights>The Author(s), under exclusive licence to Springer-Verlag GmbH, DE part of Springer Nature 2021</rights><rights>The Author(s), under exclusive licence to Springer-Verlag GmbH, DE part of Springer Nature 2021.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c319t-b2a409a2f1693a1dd3f7c6cd56555efe8413b094f0a22617c6d52dde178876c13</citedby><cites>FETCH-LOGICAL-c319t-b2a409a2f1693a1dd3f7c6cd56555efe8413b094f0a22617c6d52dde178876c13</cites><orcidid>0000-0002-7339-1159</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00217-021-03700-6$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00217-021-03700-6$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids></links><search><creatorcontrib>Çağlar, Ahmet Furkan</creatorcontrib><creatorcontrib>Çakır, Bilal</creatorcontrib><creatorcontrib>Gülseren, İbrahim</creatorcontrib><title>LC-Q-TOF/MS based identification and in silico verification of ACE-inhibitory peptides in Giresun (Turkey) hazelnut cakes</title><title>European food research & technology</title><addtitle>Eur Food Res Technol</addtitle><description>Hazelnut (
Corylus avellana
L.) cakes represent are a rich source of proteins. In an effort to valorize industrially cold-pressed hazelnut cakes, angiotensin-converting enzyme (ACE) inhibitory characteristics of hazelnut protein hydrolysates were evaluated. Trypsin, chymotrypsin and thermolysin hydrolysates of hazelnut protein isolates were fractionated using Fast Protein Liquid Chromatography (FPLC). The hydrolysate fractions were tested for ACE inhibitory characteristics and inhibitor peptide identification was based on Liquid Chromatography Quadrupole Time-of-Flight Mass Spectrometry (LC-Q-TOF/MS). Finally, in vitro ACE inhibitory activity was verified using in silico tools. In all cases, some hydrolysate fractions demonstrated ACE inhibitory characteristics, while inhibitory activity widely varied (7–95%) depending on proteolysis conditions. In ACE inhibitory fractions, 179 different peptides were identified. Their potential inhibitory activity was verified in silico for 22 different peptides generated by thermolysin, 3 for chymotrypsin and 4 for trypsin. While the half maximal inhibitory concentration (IC
50
) (0.13–4.83 mg ml
−1
) values were comparable to the previous literature, currently identified sequences were different than ACE inhibitory peptides purified from Asian hazelnuts. The peptides with the highest PeptideRanker scores for each treatment (i.e., SPLAGR, VPHW and PGHF) were studied for their potential ACE binding, Absorption, Distribution, Metabolism, Excretion and Toxicity (ADMET) and circulatory half-life characteristics demonstrating limited pharmokinetic interference, low toxicity as well as comparable short circulation and stronger binding compared to a reference inhibitor peptide (i.e., VPP). Geographical attributes and proteolytic treatments could have a bearing on ACE inhibitory potential of peptides, while hazelnut cakes can be regarded as a valuable resource for ACE inhibitor peptides.</description><subject>Agriculture</subject><subject>Analytical Chemistry</subject><subject>Angiotensin</subject><subject>Binding</subject><subject>Biotechnology</subject><subject>Cakes</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Chromatography</subject><subject>Chymotrypsin</subject><subject>Food Science</subject><subject>Forestry</subject><subject>Hazelnuts</subject><subject>Hydrolysates</subject><subject>Liquid chromatography</subject><subject>Mass spectrometry</subject><subject>Mass spectroscopy</subject><subject>Original Paper</subject><subject>Peptides</subject><subject>Peptidyl-dipeptidase A</subject><subject>Proteins</subject><subject>Proteolysis</subject><subject>Quadrupoles</subject><subject>Thermolysin</subject><subject>Toxicity</subject><subject>Trypsin</subject><issn>1438-2377</issn><issn>1438-2385</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp9kM1OwzAQhCMEEqXwApwscYGDqX8SOzlWUVuQiipEOVuO41C3xQl2ghSeHpcgeuOyu9qdb1aaKLrG6B4jxCceIYI5DAUiyhGC7CQa4ZimkNA0Of2bOT-PLrzfIpRkDMejqF_m8BmuV_PJ0wsopNclMKW2ramMkq2pLZA2rCzwZm9UDT61O57qCkzzGTR2YwrT1q4HjW7awPsDsTBO-86C23Xndrq_Axv5pfe2a4GSO-0vo7NK7r2--u3j6HU-W-cPcLlaPObTJVQUZy0siIxRJkmFWUYlLktaccVUmbAkSXSl0xjTAmVxhSQhDIdbmZCy1JinKWcK03F0M_g2rv7otG_Ftu6cDS8FSXCMOUOIBRUZVMrV3jtdicaZd-l6gZE4RCyGiEUo4idicYDoAPkgtm_aHa3_ob4BhUd-KQ</recordid><startdate>20210501</startdate><enddate>20210501</enddate><creator>Çağlar, Ahmet Furkan</creator><creator>Çakır, Bilal</creator><creator>Gülseren, İbrahim</creator><general>Springer Berlin Heidelberg</general><general>Springer Nature B.V</general><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QO</scope><scope>7QR</scope><scope>7RQ</scope><scope>7T7</scope><scope>7WY</scope><scope>7WZ</scope><scope>7X2</scope><scope>7XB</scope><scope>87Z</scope><scope>88I</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FK</scope><scope>8FL</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>BEZIV</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FRNLG</scope><scope>F~G</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K60</scope><scope>K6~</scope><scope>L.-</scope><scope>L6V</scope><scope>M0C</scope><scope>M0K</scope><scope>M2P</scope><scope>M7S</scope><scope>P64</scope><scope>PQBIZ</scope><scope>PQBZA</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PTHSS</scope><scope>Q9U</scope><orcidid>https://orcid.org/0000-0002-7339-1159</orcidid></search><sort><creationdate>20210501</creationdate><title>LC-Q-TOF/MS based identification and in silico verification of ACE-inhibitory peptides in Giresun (Turkey) hazelnut cakes</title><author>Çağlar, Ahmet Furkan ; Çakır, Bilal ; Gülseren, İbrahim</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c319t-b2a409a2f1693a1dd3f7c6cd56555efe8413b094f0a22617c6d52dde178876c13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Agriculture</topic><topic>Analytical Chemistry</topic><topic>Angiotensin</topic><topic>Binding</topic><topic>Biotechnology</topic><topic>Cakes</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Chromatography</topic><topic>Chymotrypsin</topic><topic>Food Science</topic><topic>Forestry</topic><topic>Hazelnuts</topic><topic>Hydrolysates</topic><topic>Liquid chromatography</topic><topic>Mass spectrometry</topic><topic>Mass spectroscopy</topic><topic>Original Paper</topic><topic>Peptides</topic><topic>Peptidyl-dipeptidase A</topic><topic>Proteins</topic><topic>Proteolysis</topic><topic>Quadrupoles</topic><topic>Thermolysin</topic><topic>Toxicity</topic><topic>Trypsin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Çağlar, Ahmet Furkan</creatorcontrib><creatorcontrib>Çakır, Bilal</creatorcontrib><creatorcontrib>Gülseren, İbrahim</creatorcontrib><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Biotechnology Research Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Career & Technical Education Database</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>ABI/INFORM Collection</collection><collection>ABI/INFORM Global (PDF only)</collection><collection>Agricultural Science Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>ABI/INFORM Global (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ABI/INFORM Collection (Alumni Edition)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>Business Premium Collection</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Business Premium Collection (Alumni)</collection><collection>ABI/INFORM Global (Corporate)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Business Collection (Alumni Edition)</collection><collection>ProQuest Business Collection</collection><collection>ABI/INFORM Professional Advanced</collection><collection>ProQuest Engineering Collection</collection><collection>ABI/INFORM Global</collection><collection>Agricultural Science Database</collection><collection>Science Database</collection><collection>Engineering Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Business</collection><collection>ProQuest One Business (Alumni)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Engineering Collection</collection><collection>ProQuest Central Basic</collection><jtitle>European food research & technology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Çağlar, Ahmet Furkan</au><au>Çakır, Bilal</au><au>Gülseren, İbrahim</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>LC-Q-TOF/MS based identification and in silico verification of ACE-inhibitory peptides in Giresun (Turkey) hazelnut cakes</atitle><jtitle>European food research & technology</jtitle><stitle>Eur Food Res Technol</stitle><date>2021-05-01</date><risdate>2021</risdate><volume>247</volume><issue>5</issue><spage>1189</spage><epage>1198</epage><pages>1189-1198</pages><issn>1438-2377</issn><eissn>1438-2385</eissn><abstract>Hazelnut (
Corylus avellana
L.) cakes represent are a rich source of proteins. In an effort to valorize industrially cold-pressed hazelnut cakes, angiotensin-converting enzyme (ACE) inhibitory characteristics of hazelnut protein hydrolysates were evaluated. Trypsin, chymotrypsin and thermolysin hydrolysates of hazelnut protein isolates were fractionated using Fast Protein Liquid Chromatography (FPLC). The hydrolysate fractions were tested for ACE inhibitory characteristics and inhibitor peptide identification was based on Liquid Chromatography Quadrupole Time-of-Flight Mass Spectrometry (LC-Q-TOF/MS). Finally, in vitro ACE inhibitory activity was verified using in silico tools. In all cases, some hydrolysate fractions demonstrated ACE inhibitory characteristics, while inhibitory activity widely varied (7–95%) depending on proteolysis conditions. In ACE inhibitory fractions, 179 different peptides were identified. Their potential inhibitory activity was verified in silico for 22 different peptides generated by thermolysin, 3 for chymotrypsin and 4 for trypsin. While the half maximal inhibitory concentration (IC
50
) (0.13–4.83 mg ml
−1
) values were comparable to the previous literature, currently identified sequences were different than ACE inhibitory peptides purified from Asian hazelnuts. The peptides with the highest PeptideRanker scores for each treatment (i.e., SPLAGR, VPHW and PGHF) were studied for their potential ACE binding, Absorption, Distribution, Metabolism, Excretion and Toxicity (ADMET) and circulatory half-life characteristics demonstrating limited pharmokinetic interference, low toxicity as well as comparable short circulation and stronger binding compared to a reference inhibitor peptide (i.e., VPP). Geographical attributes and proteolytic treatments could have a bearing on ACE inhibitory potential of peptides, while hazelnut cakes can be regarded as a valuable resource for ACE inhibitor peptides.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><doi>10.1007/s00217-021-03700-6</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0002-7339-1159</orcidid></addata></record> |
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| subjects | Agriculture Analytical Chemistry Angiotensin Binding Biotechnology Cakes Chemistry Chemistry and Materials Science Chromatography Chymotrypsin Food Science Forestry Hazelnuts Hydrolysates Liquid chromatography Mass spectrometry Mass spectroscopy Original Paper Peptides Peptidyl-dipeptidase A Proteins Proteolysis Quadrupoles Thermolysin Toxicity Trypsin |
| title | LC-Q-TOF/MS based identification and in silico verification of ACE-inhibitory peptides in Giresun (Turkey) hazelnut cakes |
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