Purification and characterization of angiotensin converting enzyme-inhibitory derived from crocodile blood hydrolysates
Autor(a) principal: | |
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Data de Publicação: | 2019 |
Outros Autores: | |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Food Science and Technology (Campinas) |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612019000400818 |
Resumo: | Abstract Various enzyme types were used to hydrolyze crocodile blood peptides showing an Angiotensin I-converting enzyme (ACE) inhibitory activity. Alcalase hydrolysates (ALH) and Protease G6 hydrolysates (PG6H) showed the highest degree of hydrolysis (P<0.05). However, PG6H was significantly observed to have an effective ACE-inhibitory (ACE-I) activity (94.23%) with an IC50 of 0.021±0.02 mg/mL. An unbound fraction of PG6H showed the highest ACE-I activity and was then subjected to two steps RP-HPLC process. The potent fractions including RC1 and RC2 exhibiting the highest ACE-I activity (88.33 & 84.54%, respectively) were identified using LC-MS/MS. Two novel ACE-inhibitory peptides were identified as GVAAN (431.25 Da) and LHALLL (679.52 Da), and characterized by GRAVY were 60 and 83%, respectively. The crocodile blood hydrolysate obtained by Protease G6 could serve as a source of ACE-inhibitory activity for physiological benefits. |
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Food Science and Technology (Campinas) |
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Purification and characterization of angiotensin converting enzyme-inhibitory derived from crocodile blood hydrolysatesACE inhibitory peptidesantihypertensioncrocodile blood hydrolysateAbstract Various enzyme types were used to hydrolyze crocodile blood peptides showing an Angiotensin I-converting enzyme (ACE) inhibitory activity. Alcalase hydrolysates (ALH) and Protease G6 hydrolysates (PG6H) showed the highest degree of hydrolysis (P<0.05). However, PG6H was significantly observed to have an effective ACE-inhibitory (ACE-I) activity (94.23%) with an IC50 of 0.021±0.02 mg/mL. An unbound fraction of PG6H showed the highest ACE-I activity and was then subjected to two steps RP-HPLC process. The potent fractions including RC1 and RC2 exhibiting the highest ACE-I activity (88.33 & 84.54%, respectively) were identified using LC-MS/MS. Two novel ACE-inhibitory peptides were identified as GVAAN (431.25 Da) and LHALLL (679.52 Da), and characterized by GRAVY were 60 and 83%, respectively. The crocodile blood hydrolysate obtained by Protease G6 could serve as a source of ACE-inhibitory activity for physiological benefits.Sociedade Brasileira de Ciência e Tecnologia de Alimentos2019-12-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612019000400818Food Science and Technology v.39 n.4 2019reponame:Food Science and Technology (Campinas)instname:Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)instacron:SBCTA10.1590/fst.08318info:eu-repo/semantics/openAccessNGO-SON,ArnonKATEKAEW,Somporneng2019-11-25T00:00:00Zoai:scielo:S0101-20612019000400818Revistahttp://www.scielo.br/ctaONGhttps://old.scielo.br/oai/scielo-oai.php||revista@sbcta.org.br1678-457X0101-2061opendoar:2019-11-25T00:00Food Science and Technology (Campinas) - Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)false |
dc.title.none.fl_str_mv |
Purification and characterization of angiotensin converting enzyme-inhibitory derived from crocodile blood hydrolysates |
title |
Purification and characterization of angiotensin converting enzyme-inhibitory derived from crocodile blood hydrolysates |
spellingShingle |
Purification and characterization of angiotensin converting enzyme-inhibitory derived from crocodile blood hydrolysates NGO-SON,Arnon ACE inhibitory peptides antihypertension crocodile blood hydrolysate |
title_short |
Purification and characterization of angiotensin converting enzyme-inhibitory derived from crocodile blood hydrolysates |
title_full |
Purification and characterization of angiotensin converting enzyme-inhibitory derived from crocodile blood hydrolysates |
title_fullStr |
Purification and characterization of angiotensin converting enzyme-inhibitory derived from crocodile blood hydrolysates |
title_full_unstemmed |
Purification and characterization of angiotensin converting enzyme-inhibitory derived from crocodile blood hydrolysates |
title_sort |
Purification and characterization of angiotensin converting enzyme-inhibitory derived from crocodile blood hydrolysates |
author |
NGO-SON,Arnon |
author_facet |
NGO-SON,Arnon KATEKAEW,Somporn |
author_role |
author |
author2 |
KATEKAEW,Somporn |
author2_role |
author |
dc.contributor.author.fl_str_mv |
NGO-SON,Arnon KATEKAEW,Somporn |
dc.subject.por.fl_str_mv |
ACE inhibitory peptides antihypertension crocodile blood hydrolysate |
topic |
ACE inhibitory peptides antihypertension crocodile blood hydrolysate |
description |
Abstract Various enzyme types were used to hydrolyze crocodile blood peptides showing an Angiotensin I-converting enzyme (ACE) inhibitory activity. Alcalase hydrolysates (ALH) and Protease G6 hydrolysates (PG6H) showed the highest degree of hydrolysis (P<0.05). However, PG6H was significantly observed to have an effective ACE-inhibitory (ACE-I) activity (94.23%) with an IC50 of 0.021±0.02 mg/mL. An unbound fraction of PG6H showed the highest ACE-I activity and was then subjected to two steps RP-HPLC process. The potent fractions including RC1 and RC2 exhibiting the highest ACE-I activity (88.33 & 84.54%, respectively) were identified using LC-MS/MS. Two novel ACE-inhibitory peptides were identified as GVAAN (431.25 Da) and LHALLL (679.52 Da), and characterized by GRAVY were 60 and 83%, respectively. The crocodile blood hydrolysate obtained by Protease G6 could serve as a source of ACE-inhibitory activity for physiological benefits. |
publishDate |
2019 |
dc.date.none.fl_str_mv |
2019-12-01 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612019000400818 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612019000400818 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/fst.08318 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
text/html |
dc.publisher.none.fl_str_mv |
Sociedade Brasileira de Ciência e Tecnologia de Alimentos |
publisher.none.fl_str_mv |
Sociedade Brasileira de Ciência e Tecnologia de Alimentos |
dc.source.none.fl_str_mv |
Food Science and Technology v.39 n.4 2019 reponame:Food Science and Technology (Campinas) instname:Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA) instacron:SBCTA |
instname_str |
Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA) |
instacron_str |
SBCTA |
institution |
SBCTA |
reponame_str |
Food Science and Technology (Campinas) |
collection |
Food Science and Technology (Campinas) |
repository.name.fl_str_mv |
Food Science and Technology (Campinas) - Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA) |
repository.mail.fl_str_mv |
||revista@sbcta.org.br |
_version_ |
1752126325095661568 |