Isolation, purification and bioactivity of ACE inhibitory peptides from peach kernel protein enzymatic hydrolysate
Autor(a) principal: | |
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Data de Publicação: | 2022 |
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=S0101-20612022000101042 |
Resumo: | Abstract Peaches mainly produced in China are a source of food-derived proteins, but much of it is wasted. To make full use of the peaches and peaches related resources, we extracted proteins, including albumin, globulin, gliadin, and glutelin, from defatted Tibet wild peach kernels using Osborne method to study their angiotensin I-converting enzyme (ACE) inhibiting activity, which is an active ingredient for hypertension treatment. The different enzymatic products of these extracts were further separated by ultrafiltration membranes and reversed phase high-performance liquid chromatography (RP-HPLC). The component K2 originated from globulin hydrolysate by alcalase treatment showed the highest ACE inhibiting activity (IC50 0.78 mg/mL). Through further analyzing the Mass spectrometry results of K2 and searching the BIOEP database, the specific dipeptide AH (consisted of Ala and His) has been identified as the ACE inhibitory peptide, providing a potential for using Tibet peach kernel-derived peptides as an ingredient in functional food to control hypertension. |
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Food Science and Technology (Campinas) |
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Isolation, purification and bioactivity of ACE inhibitory peptides from peach kernel protein enzymatic hydrolysatepeach kernel protein enzymatic hydrolysateACE inhibitory peptidesisolation and purificationbioactivityAbstract Peaches mainly produced in China are a source of food-derived proteins, but much of it is wasted. To make full use of the peaches and peaches related resources, we extracted proteins, including albumin, globulin, gliadin, and glutelin, from defatted Tibet wild peach kernels using Osborne method to study their angiotensin I-converting enzyme (ACE) inhibiting activity, which is an active ingredient for hypertension treatment. The different enzymatic products of these extracts were further separated by ultrafiltration membranes and reversed phase high-performance liquid chromatography (RP-HPLC). The component K2 originated from globulin hydrolysate by alcalase treatment showed the highest ACE inhibiting activity (IC50 0.78 mg/mL). Through further analyzing the Mass spectrometry results of K2 and searching the BIOEP database, the specific dipeptide AH (consisted of Ala and His) has been identified as the ACE inhibitory peptide, providing a potential for using Tibet peach kernel-derived peptides as an ingredient in functional food to control hypertension.Sociedade Brasileira de Ciência e Tecnologia de Alimentos2022-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612022000101042Food Science and Technology v.42 2022reponame:Food Science and Technology (Campinas)instname:Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)instacron:SBCTA10.1590/fst.107921info:eu-repo/semantics/openAccessWANG,LeLI,AnpingZHONG,ZhengchangTANG,YumeiLI,DongyangXIAO,Jianpingeng2022-03-15T00:00:00Zoai:scielo:S0101-20612022000101042Revistahttp://www.scielo.br/ctaONGhttps://old.scielo.br/oai/scielo-oai.php||revista@sbcta.org.br1678-457X0101-2061opendoar:2022-03-15T00:00Food Science and Technology (Campinas) - Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)false |
dc.title.none.fl_str_mv |
Isolation, purification and bioactivity of ACE inhibitory peptides from peach kernel protein enzymatic hydrolysate |
title |
Isolation, purification and bioactivity of ACE inhibitory peptides from peach kernel protein enzymatic hydrolysate |
spellingShingle |
Isolation, purification and bioactivity of ACE inhibitory peptides from peach kernel protein enzymatic hydrolysate WANG,Le peach kernel protein enzymatic hydrolysate ACE inhibitory peptides isolation and purification bioactivity |
title_short |
Isolation, purification and bioactivity of ACE inhibitory peptides from peach kernel protein enzymatic hydrolysate |
title_full |
Isolation, purification and bioactivity of ACE inhibitory peptides from peach kernel protein enzymatic hydrolysate |
title_fullStr |
Isolation, purification and bioactivity of ACE inhibitory peptides from peach kernel protein enzymatic hydrolysate |
title_full_unstemmed |
Isolation, purification and bioactivity of ACE inhibitory peptides from peach kernel protein enzymatic hydrolysate |
title_sort |
Isolation, purification and bioactivity of ACE inhibitory peptides from peach kernel protein enzymatic hydrolysate |
author |
WANG,Le |
author_facet |
WANG,Le LI,Anping ZHONG,Zhengchang TANG,Yumei LI,Dongyang XIAO,Jianping |
author_role |
author |
author2 |
LI,Anping ZHONG,Zhengchang TANG,Yumei LI,Dongyang XIAO,Jianping |
author2_role |
author author author author author |
dc.contributor.author.fl_str_mv |
WANG,Le LI,Anping ZHONG,Zhengchang TANG,Yumei LI,Dongyang XIAO,Jianping |
dc.subject.por.fl_str_mv |
peach kernel protein enzymatic hydrolysate ACE inhibitory peptides isolation and purification bioactivity |
topic |
peach kernel protein enzymatic hydrolysate ACE inhibitory peptides isolation and purification bioactivity |
description |
Abstract Peaches mainly produced in China are a source of food-derived proteins, but much of it is wasted. To make full use of the peaches and peaches related resources, we extracted proteins, including albumin, globulin, gliadin, and glutelin, from defatted Tibet wild peach kernels using Osborne method to study their angiotensin I-converting enzyme (ACE) inhibiting activity, which is an active ingredient for hypertension treatment. The different enzymatic products of these extracts were further separated by ultrafiltration membranes and reversed phase high-performance liquid chromatography (RP-HPLC). The component K2 originated from globulin hydrolysate by alcalase treatment showed the highest ACE inhibiting activity (IC50 0.78 mg/mL). Through further analyzing the Mass spectrometry results of K2 and searching the BIOEP database, the specific dipeptide AH (consisted of Ala and His) has been identified as the ACE inhibitory peptide, providing a potential for using Tibet peach kernel-derived peptides as an ingredient in functional food to control hypertension. |
publishDate |
2022 |
dc.date.none.fl_str_mv |
2022-01-01 |
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=S0101-20612022000101042 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612022000101042 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/fst.107921 |
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.42 2022 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_ |
1752126334079860736 |