Preparation and identification of novel inhibitory angiotensin-I-converting enzyme peptides from tilapia skin gelatin hydrolysates: inhibition kinetics and molecular docking
Tilapia skin gelatin was hydrolyzed by successive simulated gastrointestinal digestion, and the hydrolysates were further separated by transport across a Caco-2 cell monolayer. Angiotensin-I-converting enzyme inhibitory (ACEI) peptides were separated by successive chromatographic steps from the tran...
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| Published in | Food & function Vol. 9; no. 1; pp. 5251 - 5259 |
|---|---|
| Main Authors | , , |
| Format | Journal Article |
| Language | English |
| Published |
England
Royal Society of Chemistry
17.10.2018
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| Subjects | |
| Online Access | Get full text |
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| Abstract | Tilapia skin gelatin was hydrolyzed by successive simulated gastrointestinal digestion, and the hydrolysates were further separated by transport across a Caco-2 cell monolayer. Angiotensin-I-converting enzyme inhibitory (ACEI) peptides were separated by successive chromatographic steps from the transport hydrolysates. We have identified two key ACEI peptides, namely VGLPNSR (741.4133 Da) and QAGLSPVR (826.4661 Da) with IC
50
values of ACEI activity of 80.90 and 68.35 μM, respectively. Lineweaver-Burk plots indicated that the inhibitory ACE kinetics of the two peptides were noncompetitive. Molecular docking simulation showed that the two peptides could interact with the ACE site
via
hydrogen bonds with high binding power. However, the hydrogen bonds were not formed with the key amino acid residues in the active site of ACE. This finding was in accordance with the noncompetitive inhibition. This study established a novel approach to identify key ACEI peptides and suggested the use of tilapia peptides as functional food ingredients to prevent hypertension.
Tilapia skin gelatin was hydrolyzed by successive simulated gastrointestinal digestion, and the hydrolysates were further separated by transport across a Caco-2 cell monolayer. |
|---|---|
| AbstractList | Tilapia skin gelatin was hydrolyzed by successive simulated gastrointestinal digestion, and the hydrolysates were further separated by transport across a Caco-2 cell monolayer. Angiotensin-I-converting enzyme inhibitory (ACEI) peptides were separated by successive chromatographic steps from the transport hydrolysates. We have identified two key ACEI peptides, namely VGLPNSR (741.4133 Da) and QAGLSPVR (826.4661 Da) with IC₅₀ values of ACEI activity of 80.90 and 68.35 μM, respectively. Lineweaver–Burk plots indicated that the inhibitory ACE kinetics of the two peptides were noncompetitive. Molecular docking simulation showed that the two peptides could interact with the ACE site via hydrogen bonds with high binding power. However, the hydrogen bonds were not formed with the key amino acid residues in the active site of ACE. This finding was in accordance with the noncompetitive inhibition. This study established a novel approach to identify key ACEI peptides and suggested the use of tilapia peptides as functional food ingredients to prevent hypertension. Tilapia skin gelatin was hydrolyzed by successive simulated gastrointestinal digestion, and the hydrolysates were further separated by transport across a Caco-2 cell monolayer. Angiotensin-I-converting enzyme inhibitory (ACEI) peptides were separated by successive chromatographic steps from the transport hydrolysates. We have identified two key ACEI peptides, namely VGLPNSR (741.4133 Da) and QAGLSPVR (826.4661 Da) with IC50 values of ACEI activity of 80.90 and 68.35 μM, respectively. Lineweaver–Burk plots indicated that the inhibitory ACE kinetics of the two peptides were noncompetitive. Molecular docking simulation showed that the two peptides could interact with the ACE site via hydrogen bonds with high binding power. However, the hydrogen bonds were not formed with the key amino acid residues in the active site of ACE. This finding was in accordance with the noncompetitive inhibition. This study established a novel approach to identify key ACEI peptides and suggested the use of tilapia peptides as functional food ingredients to prevent hypertension. Tilapia skin gelatin was hydrolyzed by successive simulated gastrointestinal digestion, and the hydrolysates were further separated by transport across a Caco-2 cell monolayer. Angiotensin-I-converting enzyme inhibitory (ACEI) peptides were separated by successive chromatographic steps from the transport hydrolysates. We have identified two key ACEI peptides, namely VGLPNSR (741.4133 Da) and QAGLSPVR (826.4661 Da) with IC 50 values of ACEI activity of 80.90 and 68.35 μM, respectively. Lineweaver-Burk plots indicated that the inhibitory ACE kinetics of the two peptides were noncompetitive. Molecular docking simulation showed that the two peptides could interact with the ACE site via hydrogen bonds with high binding power. However, the hydrogen bonds were not formed with the key amino acid residues in the active site of ACE. This finding was in accordance with the noncompetitive inhibition. This study established a novel approach to identify key ACEI peptides and suggested the use of tilapia peptides as functional food ingredients to prevent hypertension. Tilapia skin gelatin was hydrolyzed by successive simulated gastrointestinal digestion, and the hydrolysates were further separated by transport across a Caco-2 cell monolayer. Tilapia skin gelatin was hydrolyzed by successive simulated gastrointestinal digestion, and the hydrolysates were further separated by transport across a Caco-2 cell monolayer. Angiotensin-I-converting enzyme inhibitory (ACEI) peptides were separated by successive chromatographic steps from the transport hydrolysates. We have identified two key ACEI peptides, namely VGLPNSR (741.4133 Da) and QAGLSPVR (826.4661 Da) with IC 50 values of ACEI activity of 80.90 and 68.35 μM, respectively. Lineweaver–Burk plots indicated that the inhibitory ACE kinetics of the two peptides were noncompetitive. Molecular docking simulation showed that the two peptides could interact with the ACE site via hydrogen bonds with high binding power. However, the hydrogen bonds were not formed with the key amino acid residues in the active site of ACE. This finding was in accordance with the noncompetitive inhibition. This study established a novel approach to identify key ACEI peptides and suggested the use of tilapia peptides as functional food ingredients to prevent hypertension. Tilapia skin gelatin was hydrolyzed by successive simulated gastrointestinal digestion, and the hydrolysates were further separated by transport across a Caco-2 cell monolayer. Angiotensin-I-converting enzyme inhibitory (ACEI) peptides were separated by successive chromatographic steps from the transport hydrolysates. We have identified two key ACEI peptides, namely VGLPNSR (741.4133 Da) and QAGLSPVR (826.4661 Da) with IC50 values of ACEI activity of 80.90 and 68.35 μM, respectively. Lineweaver-Burk plots indicated that the inhibitory ACE kinetics of the two peptides were noncompetitive. Molecular docking simulation showed that the two peptides could interact with the ACE site via hydrogen bonds with high binding power. However, the hydrogen bonds were not formed with the key amino acid residues in the active site of ACE. This finding was in accordance with the noncompetitive inhibition. This study established a novel approach to identify key ACEI peptides and suggested the use of tilapia peptides as functional food ingredients to prevent hypertension.Tilapia skin gelatin was hydrolyzed by successive simulated gastrointestinal digestion, and the hydrolysates were further separated by transport across a Caco-2 cell monolayer. Angiotensin-I-converting enzyme inhibitory (ACEI) peptides were separated by successive chromatographic steps from the transport hydrolysates. We have identified two key ACEI peptides, namely VGLPNSR (741.4133 Da) and QAGLSPVR (826.4661 Da) with IC50 values of ACEI activity of 80.90 and 68.35 μM, respectively. Lineweaver-Burk plots indicated that the inhibitory ACE kinetics of the two peptides were noncompetitive. Molecular docking simulation showed that the two peptides could interact with the ACE site via hydrogen bonds with high binding power. However, the hydrogen bonds were not formed with the key amino acid residues in the active site of ACE. This finding was in accordance with the noncompetitive inhibition. This study established a novel approach to identify key ACEI peptides and suggested the use of tilapia peptides as functional food ingredients to prevent hypertension. |
| Author | Liping, Sun Yongliang, Zhuang Ling, Yuan |
| AuthorAffiliation | Kunming University of Science and Technology Yunnan Institute of Food Safety |
| AuthorAffiliation_xml | – sequence: 0 name: Yunnan Institute of Food Safety – sequence: 0 name: Kunming University of Science and Technology |
| Author_xml | – sequence: 1 givenname: Yuan surname: Ling fullname: Ling, Yuan – sequence: 2 givenname: Sun surname: Liping fullname: Liping, Sun – sequence: 3 givenname: Zhuang surname: Yongliang fullname: Yongliang, Zhuang |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/30229250$$D View this record in MEDLINE/PubMed |
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| Cites_doi | 10.1016/j.ijbiomac.2017.03.054 10.1016/j.jff.2015.11.046 10.1016/j.peptides.2011.11.006 10.1271/bbb.60.1353 10.1016/j.jchromb.2017.02.015 10.1021/acs.jafc.7b04196 10.1021/acs.jafc.7b04562 10.1016/j.foodchem.2009.11.018 10.1016/j.foodres.2017.06.002 10.1016/j.idairyj.2017.07.003 10.1016/j.foodchem.2010.09.039 10.1016/j.jff.2012.12.003 10.1021/jf405639w 10.1016/j.procbio.2016.07.006 10.1021/acs.jafc.7b04522 10.1016/j.foodchem.2015.02.004 10.1016/j.jff.2015.06.062 10.1021/acs.jafc.7b04043 10.1016/j.foodchem.2009.04.086 10.1016/j.foodchem.2011.06.051 10.1016/j.foodchem.2017.10.095 10.1016/j.foodchem.2016.10.087 10.1007/s11947-010-0439-9 10.1016/j.phymed.2017.09.013 10.1016/j.jff.2017.03.008 10.1016/j.carbon.2016.05.062 10.1016/0006-2952(71)90292-9 10.3390/md10051066 10.1002/mnfr.200700503 10.1016/j.jff.2015.10.025 10.1016/j.jff.2013.03.008 10.1016/j.lwt.2010.09.009 10.1016/j.jff.2017.06.049 10.1016/j.peptides.2012.08.014 10.1016/j.foodchem.2016.05.087 10.1016/j.foodchem.2017.06.112 10.1016/j.jff.2012.09.006 10.1021/acs.jafc.5b01824 10.1016/j.foodres.2010.02.013 10.1271/bbb.80189 10.1016/j.molcatb.2005.09.002 10.1038/srep00717 10.1016/j.jff.2015.01.050 10.3390/md14100186 10.1021/jf900494d 10.1016/j.ifset.2016.03.014 10.1016/j.foodchem.2015.06.066 10.1016/j.idairyj.2007.09.006 |
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| References | Garcia-Moreno (C8FO00569A-(cit36)/*[position()=1]) 2015; 18 Zhuang (C8FO00569A-(cit6)/*[position()=1]) 2010; 48 Toopcham (C8FO00569A-(cit2)/*[position()=1]) 2015; 14 Miguel (C8FO00569A-(cit42)/*[position()=1]) 2008; 52 Wako (C8FO00569A-(cit32)/*[position()=1]) 1996; 60 Orio (C8FO00569A-(cit39)/*[position()=1]) 2017; 65 Balti (C8FO00569A-(cit44)/*[position()=1]) 2010; 43 Shen (C8FO00569A-(cit31)/*[position()=1]) 2005; 37 Lin (C8FO00569A-(cit33)/*[position()=1]) 2017; 32 Masuyer (C8FO00569A-(cit37)/*[position()=1]) 2012; 2 Liang (C8FO00569A-(cit16)/*[position()=1]) 2017; 66 Du (C8FO00569A-(cit47)/*[position()=1]) 2013; 5 Saiga-Egusa (C8FO00569A-(cit9)/*[position()=1]) 2009; 73 Sun (C8FO00569A-(cit22)/*[position()=1]) 2018; 66 Chen (C8FO00569A-(cit46)/*[position()=1]) 2012; 33 Fu (C8FO00569A-(cit4)/*[position()=1]) 2017; 101 Zhuang (C8FO00569A-(cit12)/*[position()=1]) 2012; 5 Quirós (C8FO00569A-(cit43)/*[position()=1]) 2008; 18 Sun (C8FO00569A-(cit15)/*[position()=1]) 2016; 14 Sun (C8FO00569A-(cit10)/*[position()=1]) 2013; 5 Ngo (C8FO00569A-(cit11)/*[position()=1]) 2016; 51 Lee (C8FO00569A-(cit34)/*[position()=1]) 2011; 125 Huang (C8FO00569A-(cit14)/*[position()=1]) 2016; 190 Ding (C8FO00569A-(cit27)/*[position()=1]) 2014; 62 Ghassem (C8FO00569A-(cit35)/*[position()=1]) 2011; 129 Hippauf (C8FO00569A-(cit1)/*[position()=1]) 2016; 107 García-Mora (C8FO00569A-(cit8)/*[position()=1]) 2017; 221 Liu (C8FO00569A-(cit5)/*[position()=1]) 2018; 245 Zhang (C8FO00569A-(cit24)/*[position()=1]) 2017; 36 Georgalaki (C8FO00569A-(cit7)/*[position()=1]) 2017; 75 Hayes (C8FO00569A-(cit3)/*[position()=1]) 2016; 37 Sun (C8FO00569A-(cit49)/*[position()=1]) 2017; 65 Wu (C8FO00569A-(cit40)/*[position()=1]) 2012; 10 Grootaert (C8FO00569A-(cit41)/*[position()=1]) 2017; 99 Xin (C8FO00569A-(cit29)/*[position()=1]) 2013; 5 Sanghoon (C8FO00569A-(cit30)/*[position()=1]) 2010; 118 Ayub Nawaz (C8FO00569A-(cit48)/*[position()=1]) 2017; 36 Zhang (C8FO00569A-(cit18)/*[position()=1]) 2012; 38 Forghani (C8FO00569A-(cit21)/*[position()=1]) 2016; 20 Ding (C8FO00569A-(cit25)/*[position()=1]) 2015; 63 Hou (C8FO00569A-(cit17)/*[position()=1]) 2011; 44 Abdelhedi (C8FO00569A-(cit28)/*[position()=1]) 2018; 239 Pan (C8FO00569A-(cit45)/*[position()=1]) 2016; 211 Guang (C8FO00569A-(cit38)/*[position()=1]) 2009; 57 Lan (C8FO00569A-(cit20)/*[position()=1]) 2015; 182 Gallego (C8FO00569A-(cit26)/*[position()=1]) 2016; 21 Yesmine (C8FO00569A-(cit13)/*[position()=1]) 2017; 1052 Cushman (C8FO00569A-(cit19)/*[position()=1]) 1971; 20 You (C8FO00569A-(cit23)/*[position()=1]) 2010; 120 |
| References_xml | – volume: 101 start-page: 207 year: 2017 ident: C8FO00569A-(cit4)/*[position()=1] publication-title: Int. J. Biol. Macromol. doi: 10.1016/j.ijbiomac.2017.03.054 – volume: 21 start-page: 388 year: 2016 ident: C8FO00569A-(cit26)/*[position()=1] publication-title: J. Funct. Foods doi: 10.1016/j.jff.2015.11.046 – volume: 33 start-page: 52 year: 2012 ident: C8FO00569A-(cit46)/*[position()=1] publication-title: Peptides doi: 10.1016/j.peptides.2011.11.006 – volume: 60 start-page: 1353 year: 1996 ident: C8FO00569A-(cit32)/*[position()=1] publication-title: Biosci., Biotechnol., Biochem. doi: 10.1271/bbb.60.1353 – volume: 1052 start-page: 43 year: 2017 ident: C8FO00569A-(cit13)/*[position()=1] publication-title: J. Chromatogr. B: Anal. Technol. Biomed. Life Sci. doi: 10.1016/j.jchromb.2017.02.015 – volume: 66 start-page: 593 year: 2018 ident: C8FO00569A-(cit22)/*[position()=1] publication-title: J. Agric. Food Chem. doi: 10.1021/acs.jafc.7b04196 – volume: 66 start-page: 1114 year: 2017 ident: C8FO00569A-(cit16)/*[position()=1] publication-title: J. Agric. Food Chem. doi: 10.1021/acs.jafc.7b04562 – volume: 120 start-page: 810 year: 2010 ident: C8FO00569A-(cit23)/*[position()=1] publication-title: Food Chem. doi: 10.1016/j.foodchem.2009.11.018 – volume: 99 start-page: 531 year: 2017 ident: C8FO00569A-(cit41)/*[position()=1] publication-title: Food Res. Int. doi: 10.1016/j.foodres.2017.06.002 – volume: 75 start-page: 10 year: 2017 ident: C8FO00569A-(cit7)/*[position()=1] publication-title: Int. Dairy J. doi: 10.1016/j.idairyj.2017.07.003 – volume: 125 start-page: 495 year: 2011 ident: C8FO00569A-(cit34)/*[position()=1] publication-title: Food Chem. doi: 10.1016/j.foodchem.2010.09.039 – volume: 5 start-page: 475 year: 2013 ident: C8FO00569A-(cit47)/*[position()=1] publication-title: J. Funct. Foods doi: 10.1016/j.jff.2012.12.003 – volume: 62 start-page: 3177 year: 2014 ident: C8FO00569A-(cit27)/*[position()=1] publication-title: J. Agric. Food Chem. doi: 10.1021/jf405639w – volume: 51 start-page: 1622 year: 2016 ident: C8FO00569A-(cit11)/*[position()=1] publication-title: Process Biochem. doi: 10.1016/j.procbio.2016.07.006 – volume: 65 start-page: 10482 year: 2017 ident: C8FO00569A-(cit39)/*[position()=1] publication-title: J. Agric. Food Chem. doi: 10.1021/acs.jafc.7b04522 – volume: 182 start-page: 136 year: 2015 ident: C8FO00569A-(cit20)/*[position()=1] publication-title: Food Chem. doi: 10.1016/j.foodchem.2015.02.004 – volume: 18 start-page: 95 year: 2015 ident: C8FO00569A-(cit36)/*[position()=1] publication-title: J. Funct. Foods doi: 10.1016/j.jff.2015.06.062 – volume: 65 start-page: 10020 year: 2017 ident: C8FO00569A-(cit49)/*[position()=1] publication-title: J. Agric. Food Chem. doi: 10.1021/acs.jafc.7b04043 – volume: 118 start-page: 96 year: 2010 ident: C8FO00569A-(cit30)/*[position()=1] publication-title: Food Chem. doi: 10.1016/j.foodchem.2009.04.086 – volume: 129 start-page: 1770 year: 2011 ident: C8FO00569A-(cit35)/*[position()=1] publication-title: Food Chem. doi: 10.1016/j.foodchem.2011.06.051 – volume: 245 start-page: 471 year: 2018 ident: C8FO00569A-(cit5)/*[position()=1] publication-title: Food Chem. doi: 10.1016/j.foodchem.2017.10.095 – volume: 221 start-page: 464 year: 2017 ident: C8FO00569A-(cit8)/*[position()=1] publication-title: Food Chem. doi: 10.1016/j.foodchem.2016.10.087 – volume: 5 start-page: 1622 year: 2012 ident: C8FO00569A-(cit12)/*[position()=1] publication-title: Food Bioprocess Technol. doi: 10.1007/s11947-010-0439-9 – volume: 36 start-page: 1 year: 2017 ident: C8FO00569A-(cit48)/*[position()=1] publication-title: Phytomedicine doi: 10.1016/j.phymed.2017.09.013 – volume: 32 start-page: 266 year: 2017 ident: C8FO00569A-(cit33)/*[position()=1] publication-title: J. Funct. Foods doi: 10.1016/j.jff.2017.03.008 – volume: 107 start-page: 116 year: 2016 ident: C8FO00569A-(cit1)/*[position()=1] publication-title: Carbon doi: 10.1016/j.carbon.2016.05.062 – volume: 20 start-page: 1637 year: 1971 ident: C8FO00569A-(cit19)/*[position()=1] publication-title: Biochem. Pharmacol. doi: 10.1016/0006-2952(71)90292-9 – volume: 10 start-page: 1066 year: 2012 ident: C8FO00569A-(cit40)/*[position()=1] publication-title: Mar. Drugs doi: 10.3390/md10051066 – volume: 52 start-page: 1507 year: 2008 ident: C8FO00569A-(cit42)/*[position()=1] publication-title: Mol. Nutr. Food Res. doi: 10.1002/mnfr.200700503 – volume: 20 start-page: 276 year: 2016 ident: C8FO00569A-(cit21)/*[position()=1] publication-title: J. Funct. Foods doi: 10.1016/j.jff.2015.10.025 – volume: 5 start-page: 1116 year: 2013 ident: C8FO00569A-(cit29)/*[position()=1] publication-title: J. Funct. Foods doi: 10.1016/j.jff.2013.03.008 – volume: 44 start-page: 421 year: 2011 ident: C8FO00569A-(cit17)/*[position()=1] publication-title: LWT–Food Sci. Technol. doi: 10.1016/j.lwt.2010.09.009 – volume: 36 start-page: 72 year: 2017 ident: C8FO00569A-(cit24)/*[position()=1] publication-title: J. Funct. Foods doi: 10.1016/j.jff.2017.06.049 – volume: 38 start-page: 13 year: 2012 ident: C8FO00569A-(cit18)/*[position()=1] publication-title: Peptides doi: 10.1016/j.peptides.2012.08.014 – volume: 211 start-page: 423 year: 2016 ident: C8FO00569A-(cit45)/*[position()=1] publication-title: Food Chem. doi: 10.1016/j.foodchem.2016.05.087 – volume: 239 start-page: 453 year: 2018 ident: C8FO00569A-(cit28)/*[position()=1] publication-title: Food Chem. doi: 10.1016/j.foodchem.2017.06.112 – volume: 5 start-page: 154 year: 2013 ident: C8FO00569A-(cit10)/*[position()=1] publication-title: J. Funct. Foods doi: 10.1016/j.jff.2012.09.006 – volume: 63 start-page: 8143 year: 2015 ident: C8FO00569A-(cit25)/*[position()=1] publication-title: J. Agric. Food Chem. doi: 10.1021/acs.jafc.5b01824 – volume: 43 start-page: 1136 year: 2010 ident: C8FO00569A-(cit44)/*[position()=1] publication-title: Food Res. Int. doi: 10.1016/j.foodres.2010.02.013 – volume: 73 start-page: 422 year: 2009 ident: C8FO00569A-(cit9)/*[position()=1] publication-title: Biosci., Biotechnol., Biochem. doi: 10.1271/bbb.80189 – volume: 37 start-page: 26 year: 2005 ident: C8FO00569A-(cit31)/*[position()=1] publication-title: J. Mol. Catal. B: Enzym. doi: 10.1016/j.molcatb.2005.09.002 – volume: 2 start-page: 717 year: 2012 ident: C8FO00569A-(cit37)/*[position()=1] publication-title: Sci. Rep. doi: 10.1038/srep00717 – volume: 14 start-page: 435 year: 2015 ident: C8FO00569A-(cit2)/*[position()=1] publication-title: J. Funct. Foods doi: 10.1016/j.jff.2015.01.050 – volume: 14 start-page: 186 year: 2016 ident: C8FO00569A-(cit15)/*[position()=1] publication-title: Mar. Drugs doi: 10.3390/md14100186 – volume: 57 start-page: 5113 year: 2009 ident: C8FO00569A-(cit38)/*[position()=1] publication-title: J. Agric. Food Chem. doi: 10.1021/jf900494d – volume: 48 start-page: 222 year: 2010 ident: C8FO00569A-(cit6)/*[position()=1] publication-title: Food Technol. Biotechnol. – volume: 37 start-page: 253 year: 2016 ident: C8FO00569A-(cit3)/*[position()=1] publication-title: Innovative Food Sci. Emerging Technol. doi: 10.1016/j.ifset.2016.03.014 – volume: 190 start-page: 997 year: 2016 ident: C8FO00569A-(cit14)/*[position()=1] publication-title: Food Chem. doi: 10.1016/j.foodchem.2015.06.066 – volume: 18 start-page: 279 year: 2008 ident: C8FO00569A-(cit43)/*[position()=1] publication-title: Int. Dairy J. doi: 10.1016/j.idairyj.2007.09.006 |
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| SubjectTerms | active sites Amino acids Angiotensin Angiotensin-Converting Enzyme Inhibitors - chemistry Angiotensin-Converting Enzyme Inhibitors - isolation & purification Angiotensin-Converting Enzyme Inhibitors - metabolism Animals Biological Transport Caco-2 Cells chromatography computer simulation Conversion Digestive system Enzymes Fish Proteins - chemistry Fish Proteins - isolation & purification Fish Proteins - metabolism functional foods Functional foods & nutraceuticals gastrointestinal system Gastrointestinal tract Gelatin Gelatin - chemistry human cell lines Humans Hydrogen Bonding Hydrogen bonds Hydrolysates Hydrolysis Hypertension in vitro digestion ingredients inhibitory concentration 50 Kinetics Molecular docking Molecular Docking Simulation Peptide Mapping Peptides Peptides - chemistry Peptides - isolation & purification Peptides - metabolism Peptidyl-Dipeptidase A - chemistry Peptidyl-Dipeptidase A - metabolism Protein Hydrolysates - chemistry Skin Skin - chemistry Skin preparations Tilapia Transport |
| Title | Preparation and identification of novel inhibitory angiotensin-I-converting enzyme peptides from tilapia skin gelatin hydrolysates: inhibition kinetics and molecular docking |
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