Identification and characterization of cholesterol esterase and lipase inhibitory peptides from amaranth protein hydrolysates

Human diet is undergoing a shift towards plant-based diet as a sustainable source of protein compared to animal-derived protein. In this study, cholesterol esterase (CEase) and pancreatic lipase (PL) inhibitory activities of amaranth protein hydrolysates (APHs) were studied. Bromelain, chymotrypsin,...

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Autores principales:	Feyisola Fisayo Ajayi, Priti Mudgil, Chee-Yuen Gan, Sajid Maqsood
Formato:	article
Lenguaje:	EN
Publicado:	Elsevier 2021
Materias:	Amaranth hydrolysates Bioactive peptides Pancreatic lipase Cholesterol esterase HPLC Nutrition. Foods and food supply TX341-641 Food processing and manufacture TP368-456
Acceso en línea:	https://doaj.org/article/e41ee6f5000b4ef8acc32306231a590f
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spelling	oai:doaj.org-article:e41ee6f5000b4ef8acc32306231a590f2021-11-28T04:37:50ZIdentification and characterization of cholesterol esterase and lipase inhibitory peptides from amaranth protein hydrolysates2590-157510.1016/j.fochx.2021.100165https://doaj.org/article/e41ee6f5000b4ef8acc32306231a590f2021-12-01T00:00:00Zhttp://www.sciencedirect.com/science/article/pii/S2590157521000535https://doaj.org/toc/2590-1575Human diet is undergoing a shift towards plant-based diet as a sustainable source of protein compared to animal-derived protein. In this study, cholesterol esterase (CEase) and pancreatic lipase (PL) inhibitory activities of amaranth protein hydrolysates (APHs) were studied. Bromelain, chymotrypsin, and actinase E were used for generating APHs at 2, 4 & 6 h of hydrolysis. Higher PL inhibiting potential were observed in bromelain-derived APHs (IC50 = 0.38–0.66 mg/mL) in comparison to intact amaranth proteins (IC50 = 3.93 mg/mL). Bromelain-4 h hydrolysates (AB4) demonstrated significant inhibitory potential for both CEase (IC50 = 0.47 mg/mL) and PL (IC50 = 0.48 mg/mL) activity. Peptide identification in AB-4 hydrolysate revealed that among 17 bioactive peptides, three peptides (FPFPPTLGY, FGAPR, and FPFVPAPT) were predicted as potential PL inhibitors and only one peptide (FPFVPAPT) was predicted as CEase inhibitor based on the number of substrate binding sites on active site of the enzymes. This is the first study providing insights into amaranth protein derived bioactive peptide possessing CEase and LIP inhibitory potential.Feyisola Fisayo AjayiPriti MudgilChee-Yuen GanSajid MaqsoodElsevierarticleAmaranth hydrolysatesBioactive peptidesPancreatic lipaseCholesterol esteraseHPLCNutrition. Foods and food supplyTX341-641Food processing and manufactureTP368-456ENFood Chemistry: X, Vol 12, Iss , Pp 100165- (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Amaranth hydrolysates Bioactive peptides Pancreatic lipase Cholesterol esterase HPLC Nutrition. Foods and food supply TX341-641 Food processing and manufacture TP368-456
spellingShingle	Amaranth hydrolysates Bioactive peptides Pancreatic lipase Cholesterol esterase HPLC Nutrition. Foods and food supply TX341-641 Food processing and manufacture TP368-456 Feyisola Fisayo Ajayi Priti Mudgil Chee-Yuen Gan Sajid Maqsood Identification and characterization of cholesterol esterase and lipase inhibitory peptides from amaranth protein hydrolysates
description	Human diet is undergoing a shift towards plant-based diet as a sustainable source of protein compared to animal-derived protein. In this study, cholesterol esterase (CEase) and pancreatic lipase (PL) inhibitory activities of amaranth protein hydrolysates (APHs) were studied. Bromelain, chymotrypsin, and actinase E were used for generating APHs at 2, 4 & 6 h of hydrolysis. Higher PL inhibiting potential were observed in bromelain-derived APHs (IC50 = 0.38–0.66 mg/mL) in comparison to intact amaranth proteins (IC50 = 3.93 mg/mL). Bromelain-4 h hydrolysates (AB4) demonstrated significant inhibitory potential for both CEase (IC50 = 0.47 mg/mL) and PL (IC50 = 0.48 mg/mL) activity. Peptide identification in AB-4 hydrolysate revealed that among 17 bioactive peptides, three peptides (FPFPPTLGY, FGAPR, and FPFVPAPT) were predicted as potential PL inhibitors and only one peptide (FPFVPAPT) was predicted as CEase inhibitor based on the number of substrate binding sites on active site of the enzymes. This is the first study providing insights into amaranth protein derived bioactive peptide possessing CEase and LIP inhibitory potential.
format	article
author	Feyisola Fisayo Ajayi Priti Mudgil Chee-Yuen Gan Sajid Maqsood
author_facet	Feyisola Fisayo Ajayi Priti Mudgil Chee-Yuen Gan Sajid Maqsood
author_sort	Feyisola Fisayo Ajayi
title	Identification and characterization of cholesterol esterase and lipase inhibitory peptides from amaranth protein hydrolysates
title_short	Identification and characterization of cholesterol esterase and lipase inhibitory peptides from amaranth protein hydrolysates
title_full	Identification and characterization of cholesterol esterase and lipase inhibitory peptides from amaranth protein hydrolysates
title_fullStr	Identification and characterization of cholesterol esterase and lipase inhibitory peptides from amaranth protein hydrolysates
title_full_unstemmed	Identification and characterization of cholesterol esterase and lipase inhibitory peptides from amaranth protein hydrolysates
title_sort	identification and characterization of cholesterol esterase and lipase inhibitory peptides from amaranth protein hydrolysates
publisher	Elsevier
publishDate	2021
url	https://doaj.org/article/e41ee6f5000b4ef8acc32306231a590f
work_keys_str_mv	AT feyisolafisayoajayi identificationandcharacterizationofcholesterolesteraseandlipaseinhibitorypeptidesfromamaranthproteinhydrolysates AT pritimudgil identificationandcharacterizationofcholesterolesteraseandlipaseinhibitorypeptidesfromamaranthproteinhydrolysates AT cheeyuengan identificationandcharacterizationofcholesterolesteraseandlipaseinhibitorypeptidesfromamaranthproteinhydrolysates AT sajidmaqsood identificationandcharacterizationofcholesterolesteraseandlipaseinhibitorypeptidesfromamaranthproteinhydrolysates
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Identification and characterization of cholesterol esterase and lipase inhibitory peptides from amaranth protein hydrolysates

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