Physico-chemical properties, antioxidant activities and angiotensin-I converting enzyme inhibitory of protein hydrolysates from Mung bean (Vigna radiate)
•A potent ACE inhibitory from Mung bean protein hydrolysate was generated.•Alcalase hydrolysates presented better DH and TCA-NSI.•Characterization of MBPHs and its fractions were identified by UV, CD and FTIR.•MBPH-I exhibited better antioxidant properties and ACE-inhibitory activity. Mung bean Prot...
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| Veröffentlicht in: | Food chemistry 2019-01, Vol.270, p.243-250 |
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| creator | Xie, Jianhua Du, Mengxia Shen, Mingyue Wu, Ting Lin, Lihua |
| description | •A potent ACE inhibitory from Mung bean protein hydrolysate was generated.•Alcalase hydrolysates presented better DH and TCA-NSI.•Characterization of MBPHs and its fractions were identified by UV, CD and FTIR.•MBPH-I exhibited better antioxidant properties and ACE-inhibitory activity.
Mung bean Protein hydrolyses (MBPHs) have attracted a great deal of attention due to their variety of biological activities. In present study, MBPHs were fractionate according to the molecular mass into three fractions of MBPHs-I (10 kDa). Their antioxidant activity and angiotensin-I converting enzyme (ACE) inhibitory of were investigated in vitro. Results showed that the alcalase-derived hydrolysate exhibited the highest degree of hydrolysis (DH) and trichloroacetic acid–nitrogen soluble index (TCA-NSI) versus those of other enzyme hydrolysates. MBPHs-I presented the best scavenge DPPH, hydroxyl radicals, superoxide radicals, Fe2+ chelating activities, and the best ACE inhibitory activity (IC50 = 4.66 μg/mL) than that of MBPHs and MBPHs-III. And MBPHs-I rich in hydrophobic and aromatic amino acids, and its secondary structure mainly contain α-helix, β-sheet and irregular coiled. Results indicated that MBPHs-I has a great potential as natural functional materials for supplement. |
| doi_str_mv | 10.1016/j.foodchem.2018.07.103 |
| format | Article |
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Mung bean Protein hydrolyses (MBPHs) have attracted a great deal of attention due to their variety of biological activities. In present study, MBPHs were fractionate according to the molecular mass into three fractions of MBPHs-I (<3 kDa), MBPHs-II (3–10 kDa) and MBPHs-III (>10 kDa). Their antioxidant activity and angiotensin-I converting enzyme (ACE) inhibitory of were investigated in vitro. Results showed that the alcalase-derived hydrolysate exhibited the highest degree of hydrolysis (DH) and trichloroacetic acid–nitrogen soluble index (TCA-NSI) versus those of other enzyme hydrolysates. MBPHs-I presented the best scavenge DPPH, hydroxyl radicals, superoxide radicals, Fe2+ chelating activities, and the best ACE inhibitory activity (IC50 = 4.66 μg/mL) than that of MBPHs and MBPHs-III. And MBPHs-I rich in hydrophobic and aromatic amino acids, and its secondary structure mainly contain α-helix, β-sheet and irregular coiled. Results indicated that MBPHs-I has a great potential as natural functional materials for supplement.</description><identifier>ISSN: 0308-8146</identifier><identifier>EISSN: 1873-7072</identifier><identifier>DOI: 10.1016/j.foodchem.2018.07.103</identifier><identifier>PMID: 30174041</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>ACE inhibitory activity ; Amino acid ; Angiotensin-Converting Enzyme Inhibitors - chemistry ; Antioxidant activity ; Fabaceae ; Hydrolysates ; Hydrolysis ; Mung bean protein ; Peptides ; Peptidyl-Dipeptidase A - metabolism ; Protein Hydrolysates - chemistry ; Secondary structure ; Vigna - chemistry ; Vigna - enzymology</subject><ispartof>Food chemistry, 2019-01, Vol.270, p.243-250</ispartof><rights>2018 Elsevier Ltd</rights><rights>Copyright © 2018 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c405t-6f91bf507130530a9d654fc3aee4d5a49e23521cfb721fa6b45ca1d733550cff3</citedby><cites>FETCH-LOGICAL-c405t-6f91bf507130530a9d654fc3aee4d5a49e23521cfb721fa6b45ca1d733550cff3</cites><orcidid>0000-0002-3906-1260</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.foodchem.2018.07.103$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,782,786,3552,27931,27932,46002</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/30174041$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Xie, Jianhua</creatorcontrib><creatorcontrib>Du, Mengxia</creatorcontrib><creatorcontrib>Shen, Mingyue</creatorcontrib><creatorcontrib>Wu, Ting</creatorcontrib><creatorcontrib>Lin, Lihua</creatorcontrib><title>Physico-chemical properties, antioxidant activities and angiotensin-I converting enzyme inhibitory of protein hydrolysates from Mung bean (Vigna radiate)</title><title>Food chemistry</title><addtitle>Food Chem</addtitle><description>•A potent ACE inhibitory from Mung bean protein hydrolysate was generated.•Alcalase hydrolysates presented better DH and TCA-NSI.•Characterization of MBPHs and its fractions were identified by UV, CD and FTIR.•MBPH-I exhibited better antioxidant properties and ACE-inhibitory activity.
Mung bean Protein hydrolyses (MBPHs) have attracted a great deal of attention due to their variety of biological activities. In present study, MBPHs were fractionate according to the molecular mass into three fractions of MBPHs-I (<3 kDa), MBPHs-II (3–10 kDa) and MBPHs-III (>10 kDa). Their antioxidant activity and angiotensin-I converting enzyme (ACE) inhibitory of were investigated in vitro. Results showed that the alcalase-derived hydrolysate exhibited the highest degree of hydrolysis (DH) and trichloroacetic acid–nitrogen soluble index (TCA-NSI) versus those of other enzyme hydrolysates. MBPHs-I presented the best scavenge DPPH, hydroxyl radicals, superoxide radicals, Fe2+ chelating activities, and the best ACE inhibitory activity (IC50 = 4.66 μg/mL) than that of MBPHs and MBPHs-III. And MBPHs-I rich in hydrophobic and aromatic amino acids, and its secondary structure mainly contain α-helix, β-sheet and irregular coiled. Results indicated that MBPHs-I has a great potential as natural functional materials for supplement.</description><subject>ACE inhibitory activity</subject><subject>Amino acid</subject><subject>Angiotensin-Converting Enzyme Inhibitors - chemistry</subject><subject>Antioxidant activity</subject><subject>Fabaceae</subject><subject>Hydrolysates</subject><subject>Hydrolysis</subject><subject>Mung bean protein</subject><subject>Peptides</subject><subject>Peptidyl-Dipeptidase A - metabolism</subject><subject>Protein Hydrolysates - chemistry</subject><subject>Secondary structure</subject><subject>Vigna - chemistry</subject><subject>Vigna - enzymology</subject><issn>0308-8146</issn><issn>1873-7072</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUU2P0zAQtRCILQt_YeXjIpEyjvPR3ECrBVZaBAfgajn2uJ0qsYudVoR_wr_FUXe5chiN9Pzem_E8xq4ErAWI5u1-7UKwZofjugSxWUObcfmErcSmlUULbfmUrUDCptiIqrlgL1LaA8DCfc4uJIi2gkqs2J-vuzmRCcViRUYP_BDDAeNEmN5w7ScKv8jmzrWZ6EQLnmGba0thQp_IF3fcBH9aRH7L0f-eR-Tkd9TTFOLMg1tMJyTPd7ONYZiTnrKNi2Hkn49Z06P2_PoHbb3mUVvKz69fsmdODwlfPfRL9v3D7bebT8X9l493N-_vC1NBPRWN60TvamiFhFqC7mxTV85IjVjZWlcdlrIuhXF9Wwqnm76qjRa2lbKuwTgnL9n12Tfv-POIaVIjJYPDoD2GY1IldB1UZdWITG3OVBNDShGdOkQadZyVALXEovbqMRa1nFpBm3GZhVcPM479iPaf7DGHTHh3JmD-6YkwqmQIvUFLEc2kbKD_zfgLGAGlyg</recordid><startdate>20190101</startdate><enddate>20190101</enddate><creator>Xie, Jianhua</creator><creator>Du, Mengxia</creator><creator>Shen, Mingyue</creator><creator>Wu, Ting</creator><creator>Lin, Lihua</creator><general>Elsevier Ltd</general><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><orcidid>https://orcid.org/0000-0002-3906-1260</orcidid></search><sort><creationdate>20190101</creationdate><title>Physico-chemical properties, antioxidant activities and angiotensin-I converting enzyme inhibitory of protein hydrolysates from Mung bean (Vigna radiate)</title><author>Xie, Jianhua ; Du, Mengxia ; Shen, Mingyue ; Wu, Ting ; Lin, Lihua</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c405t-6f91bf507130530a9d654fc3aee4d5a49e23521cfb721fa6b45ca1d733550cff3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>ACE inhibitory activity</topic><topic>Amino acid</topic><topic>Angiotensin-Converting Enzyme Inhibitors - chemistry</topic><topic>Antioxidant activity</topic><topic>Fabaceae</topic><topic>Hydrolysates</topic><topic>Hydrolysis</topic><topic>Mung bean protein</topic><topic>Peptides</topic><topic>Peptidyl-Dipeptidase A - metabolism</topic><topic>Protein Hydrolysates - chemistry</topic><topic>Secondary structure</topic><topic>Vigna - chemistry</topic><topic>Vigna - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Xie, Jianhua</creatorcontrib><creatorcontrib>Du, Mengxia</creatorcontrib><creatorcontrib>Shen, Mingyue</creatorcontrib><creatorcontrib>Wu, Ting</creatorcontrib><creatorcontrib>Lin, Lihua</creatorcontrib><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>Food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Xie, Jianhua</au><au>Du, Mengxia</au><au>Shen, Mingyue</au><au>Wu, Ting</au><au>Lin, Lihua</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Physico-chemical properties, antioxidant activities and angiotensin-I converting enzyme inhibitory of protein hydrolysates from Mung bean (Vigna radiate)</atitle><jtitle>Food chemistry</jtitle><addtitle>Food Chem</addtitle><date>2019-01-01</date><risdate>2019</risdate><volume>270</volume><spage>243</spage><epage>250</epage><pages>243-250</pages><issn>0308-8146</issn><eissn>1873-7072</eissn><abstract>•A potent ACE inhibitory from Mung bean protein hydrolysate was generated.•Alcalase hydrolysates presented better DH and TCA-NSI.•Characterization of MBPHs and its fractions were identified by UV, CD and FTIR.•MBPH-I exhibited better antioxidant properties and ACE-inhibitory activity.
Mung bean Protein hydrolyses (MBPHs) have attracted a great deal of attention due to their variety of biological activities. In present study, MBPHs were fractionate according to the molecular mass into three fractions of MBPHs-I (<3 kDa), MBPHs-II (3–10 kDa) and MBPHs-III (>10 kDa). Their antioxidant activity and angiotensin-I converting enzyme (ACE) inhibitory of were investigated in vitro. Results showed that the alcalase-derived hydrolysate exhibited the highest degree of hydrolysis (DH) and trichloroacetic acid–nitrogen soluble index (TCA-NSI) versus those of other enzyme hydrolysates. MBPHs-I presented the best scavenge DPPH, hydroxyl radicals, superoxide radicals, Fe2+ chelating activities, and the best ACE inhibitory activity (IC50 = 4.66 μg/mL) than that of MBPHs and MBPHs-III. And MBPHs-I rich in hydrophobic and aromatic amino acids, and its secondary structure mainly contain α-helix, β-sheet and irregular coiled. Results indicated that MBPHs-I has a great potential as natural functional materials for supplement.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>30174041</pmid><doi>10.1016/j.foodchem.2018.07.103</doi><tpages>8</tpages><orcidid>https://orcid.org/0000-0002-3906-1260</orcidid></addata></record> |
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| subjects | ACE inhibitory activity Amino acid Angiotensin-Converting Enzyme Inhibitors - chemistry Antioxidant activity Fabaceae Hydrolysates Hydrolysis Mung bean protein Peptides Peptidyl-Dipeptidase A - metabolism Protein Hydrolysates - chemistry Secondary structure Vigna - chemistry Vigna - enzymology |
| title | Physico-chemical properties, antioxidant activities and angiotensin-I converting enzyme inhibitory of protein hydrolysates from Mung bean (Vigna radiate) |
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