Purification and characterization of angiotensin converting enzyme-inhibitory derived from crocodile blood hydrolysates

Detalhes bibliográficos
Autor(a) principal: NGO-SON,Arnon
Data de Publicação: 2019
Outros Autores: KATEKAEW,Somporn
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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spelling 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
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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)
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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)
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