Characterization, antioxidant, ACE inhibition and toxicity evaluations of palm kernel cake-derived Alcalase® hydrolysate

Detalhes bibliográficos
Autor(a) principal: NG,Khar-Ling
Data de Publicação: 2022
Outros Autores: TAN,Yen-Nee, OSMAN,Md. Anuar, RAJAB,Nor Fadilah, EE,Kah-Yaw
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=S0101-20612022000100790
Resumo: Abstract Palm (Elaeis guineensis Jacquin) kernel cake protein (PKCP) was extracted and hydrolyzed using Alcalase® 2.4L to obtain hydrolysate (PKCPH), then fractionated using size exclusion chromatography. PKCPH consisted of predominantly fraction one (PKCPH1), containing two peptides (4.9 kDa and 6.3 kDa) with functional amide (6.75–7.04 ppm) and amine (1.5–2.0 ppm) groups. PKCP and PKCPH shared similar amino acid profiles. PKCPH1 had moderate amounts of hydrophobic (23.60%) and antioxidant (26.10%) amino acids, with high hydrophobicity index (Ho 79.60), thus exhibiting the highest antioxidant activity in mostly all the antioxidant assays. On the other hand, fraction two, PKCPH2 (58.8 kDa), possessed strong angiotensin converting enzyme (ACE) inhibitory activity (77.29%), but undetectable antioxidant activity. Furthermore, high viability (87–92%) and negligible cytotoxic activity were revealed with the highest dosages of PKCPH (2 mg/mL) and PKCPH1 (1 mg/mL) in 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT), Salmonella reverse mutation (AMES), alkaline comet and micronucleus (MNi) assays. Besides, in vivo acute oral toxicity test on PKCPH using Sprague Dawley albino rats showed negative outcome according to the consistent body and organ weights as well as normal morbidity. In short, PKCPH is safe for potential applications in the formulation of functional food and nutraceutical products with health benefits.
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spelling Characterization, antioxidant, ACE inhibition and toxicity evaluations of palm kernel cake-derived Alcalase® hydrolysateprotein hydrolysatecharacterizationantioxidantACE inhibitiontoxicity analysesAbstract Palm (Elaeis guineensis Jacquin) kernel cake protein (PKCP) was extracted and hydrolyzed using Alcalase® 2.4L to obtain hydrolysate (PKCPH), then fractionated using size exclusion chromatography. PKCPH consisted of predominantly fraction one (PKCPH1), containing two peptides (4.9 kDa and 6.3 kDa) with functional amide (6.75–7.04 ppm) and amine (1.5–2.0 ppm) groups. PKCP and PKCPH shared similar amino acid profiles. PKCPH1 had moderate amounts of hydrophobic (23.60%) and antioxidant (26.10%) amino acids, with high hydrophobicity index (Ho 79.60), thus exhibiting the highest antioxidant activity in mostly all the antioxidant assays. On the other hand, fraction two, PKCPH2 (58.8 kDa), possessed strong angiotensin converting enzyme (ACE) inhibitory activity (77.29%), but undetectable antioxidant activity. Furthermore, high viability (87–92%) and negligible cytotoxic activity were revealed with the highest dosages of PKCPH (2 mg/mL) and PKCPH1 (1 mg/mL) in 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT), Salmonella reverse mutation (AMES), alkaline comet and micronucleus (MNi) assays. Besides, in vivo acute oral toxicity test on PKCPH using Sprague Dawley albino rats showed negative outcome according to the consistent body and organ weights as well as normal morbidity. In short, PKCPH is safe for potential applications in the formulation of functional food and nutraceutical products with health benefits.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=S0101-20612022000100790Food 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.80421info:eu-repo/semantics/openAccessNG,Khar-LingTAN,Yen-NeeOSMAN,Md. AnuarRAJAB,Nor FadilahEE,Kah-Yaweng2022-03-22T00:00:00Zoai:scielo:S0101-20612022000100790Revistahttp://www.scielo.br/ctaONGhttps://old.scielo.br/oai/scielo-oai.php||revista@sbcta.org.br1678-457X0101-2061opendoar:2022-03-22T00:00Food Science and Technology (Campinas) - Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)false
dc.title.none.fl_str_mv Characterization, antioxidant, ACE inhibition and toxicity evaluations of palm kernel cake-derived Alcalase® hydrolysate
title Characterization, antioxidant, ACE inhibition and toxicity evaluations of palm kernel cake-derived Alcalase® hydrolysate
spellingShingle Characterization, antioxidant, ACE inhibition and toxicity evaluations of palm kernel cake-derived Alcalase® hydrolysate
NG,Khar-Ling
protein hydrolysate
characterization
antioxidant
ACE inhibition
toxicity analyses
title_short Characterization, antioxidant, ACE inhibition and toxicity evaluations of palm kernel cake-derived Alcalase® hydrolysate
title_full Characterization, antioxidant, ACE inhibition and toxicity evaluations of palm kernel cake-derived Alcalase® hydrolysate
title_fullStr Characterization, antioxidant, ACE inhibition and toxicity evaluations of palm kernel cake-derived Alcalase® hydrolysate
title_full_unstemmed Characterization, antioxidant, ACE inhibition and toxicity evaluations of palm kernel cake-derived Alcalase® hydrolysate
title_sort Characterization, antioxidant, ACE inhibition and toxicity evaluations of palm kernel cake-derived Alcalase® hydrolysate
author NG,Khar-Ling
author_facet NG,Khar-Ling
TAN,Yen-Nee
OSMAN,Md. Anuar
RAJAB,Nor Fadilah
EE,Kah-Yaw
author_role author
author2 TAN,Yen-Nee
OSMAN,Md. Anuar
RAJAB,Nor Fadilah
EE,Kah-Yaw
author2_role author
author
author
author
dc.contributor.author.fl_str_mv NG,Khar-Ling
TAN,Yen-Nee
OSMAN,Md. Anuar
RAJAB,Nor Fadilah
EE,Kah-Yaw
dc.subject.por.fl_str_mv protein hydrolysate
characterization
antioxidant
ACE inhibition
toxicity analyses
topic protein hydrolysate
characterization
antioxidant
ACE inhibition
toxicity analyses
description Abstract Palm (Elaeis guineensis Jacquin) kernel cake protein (PKCP) was extracted and hydrolyzed using Alcalase® 2.4L to obtain hydrolysate (PKCPH), then fractionated using size exclusion chromatography. PKCPH consisted of predominantly fraction one (PKCPH1), containing two peptides (4.9 kDa and 6.3 kDa) with functional amide (6.75–7.04 ppm) and amine (1.5–2.0 ppm) groups. PKCP and PKCPH shared similar amino acid profiles. PKCPH1 had moderate amounts of hydrophobic (23.60%) and antioxidant (26.10%) amino acids, with high hydrophobicity index (Ho 79.60), thus exhibiting the highest antioxidant activity in mostly all the antioxidant assays. On the other hand, fraction two, PKCPH2 (58.8 kDa), possessed strong angiotensin converting enzyme (ACE) inhibitory activity (77.29%), but undetectable antioxidant activity. Furthermore, high viability (87–92%) and negligible cytotoxic activity were revealed with the highest dosages of PKCPH (2 mg/mL) and PKCPH1 (1 mg/mL) in 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT), Salmonella reverse mutation (AMES), alkaline comet and micronucleus (MNi) assays. Besides, in vivo acute oral toxicity test on PKCPH using Sprague Dawley albino rats showed negative outcome according to the consistent body and organ weights as well as normal morbidity. In short, PKCPH is safe for potential applications in the formulation of functional food and nutraceutical products with health benefits.
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=S0101-20612022000100790
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612022000100790
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/fst.80421
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
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