Copper chelating protein hydrolysate from Salvia hispanica L. by pepsin-pancreatin treatment

Salvia hispanica L. (Chia) seeds are good source of proteins with diverse health benefits. The seed protein was extracted through alkaline solubilisation followed by acid precipitation to separate fibres and are digested sequentially by pepsin and pancreatin. Enzyme-substrate ratio, temperature and...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Latha B V, Likhitha R, Chethan Kumar M
Formato:	article
Lenguaje:	EN
Publicado:	Elsevier 2021
Materias:	Chia seed Protein hydrolysate Copper chelating peptides Nutrition. Foods and food supply TX341-641 Food processing and manufacture TP368-456
Acceso en línea:	https://doaj.org/article/e3cdca8a685b42e3b2af940ff414bbe3
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:e3cdca8a685b42e3b2af940ff414bbe3
record_format	dspace
spelling	oai:doaj.org-article:e3cdca8a685b42e3b2af940ff414bbe32021-11-28T04:38:11ZCopper chelating protein hydrolysate from Salvia hispanica L. by pepsin-pancreatin treatment2665-927110.1016/j.crfs.2021.11.007https://doaj.org/article/e3cdca8a685b42e3b2af940ff414bbe32021-01-01T00:00:00Zhttp://www.sciencedirect.com/science/article/pii/S2665927121000964https://doaj.org/toc/2665-9271Salvia hispanica L. (Chia) seeds are good source of proteins with diverse health benefits. The seed protein was extracted through alkaline solubilisation followed by acid precipitation to separate fibres and are digested sequentially by pepsin and pancreatin. Enzyme-substrate ratio, temperature and contact time had high impact on degree of hydrolysis affecting their chelating ability. Maximum degree of hydrolysis (14.06%) and maximum copper chelation (74.98%) was obtained at 4% w/w enzyme-substrate ratio at 37 °C for 4 h. Copper chelating enzymatic hydrolysate was isolated by HiTrap chelating column and purified further by rpHPLC. Out of nine fractions obtained by rpHPLC the sixth fraction with 93.09 ± 0.16% of copper chelating activity and 82.91 ± 0.52% of antioxidant activity was further characterized as Copper chelating Chia Protein Hydrolysate (CCPH). Ultraviolet spectroscopy and fluorescence spectroscopic studies revealed the interaction of the major chelating sites of the CCPH with the copper divalent ion. The purified CCPH was subjected to LC-MS/ESI-TOF analysis from which six major intense peaks obtained with m/z value ranging from 0.4 kDa to 2.5 kDa were identified and sequenced using Mascot database. The functional behaviour and the binding capacity of these peptides were analysed by their amino acid composition. The CCPH was stable in a simulated gastric condition and its chelating ability remained unaltered. These results explored an informative bioactive peptides with varied activity and one valuable among is the copper chelating with antioxidant property. Furthermore, these Chia seed protein hydrolysates can be useful as dietary supplements to enhance mineral bioavailability.Latha B VLikhitha RChethan Kumar MElsevierarticleChia seedProtein hydrolysateCopper chelating peptidesNutrition. Foods and food supplyTX341-641Food processing and manufactureTP368-456ENCurrent Research in Food Science, Vol 4, Iss , Pp 829-839 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Chia seed Protein hydrolysate Copper chelating peptides Nutrition. Foods and food supply TX341-641 Food processing and manufacture TP368-456
spellingShingle	Chia seed Protein hydrolysate Copper chelating peptides Nutrition. Foods and food supply TX341-641 Food processing and manufacture TP368-456 Latha B V Likhitha R Chethan Kumar M Copper chelating protein hydrolysate from Salvia hispanica L. by pepsin-pancreatin treatment
description	Salvia hispanica L. (Chia) seeds are good source of proteins with diverse health benefits. The seed protein was extracted through alkaline solubilisation followed by acid precipitation to separate fibres and are digested sequentially by pepsin and pancreatin. Enzyme-substrate ratio, temperature and contact time had high impact on degree of hydrolysis affecting their chelating ability. Maximum degree of hydrolysis (14.06%) and maximum copper chelation (74.98%) was obtained at 4% w/w enzyme-substrate ratio at 37 °C for 4 h. Copper chelating enzymatic hydrolysate was isolated by HiTrap chelating column and purified further by rpHPLC. Out of nine fractions obtained by rpHPLC the sixth fraction with 93.09 ± 0.16% of copper chelating activity and 82.91 ± 0.52% of antioxidant activity was further characterized as Copper chelating Chia Protein Hydrolysate (CCPH). Ultraviolet spectroscopy and fluorescence spectroscopic studies revealed the interaction of the major chelating sites of the CCPH with the copper divalent ion. The purified CCPH was subjected to LC-MS/ESI-TOF analysis from which six major intense peaks obtained with m/z value ranging from 0.4 kDa to 2.5 kDa were identified and sequenced using Mascot database. The functional behaviour and the binding capacity of these peptides were analysed by their amino acid composition. The CCPH was stable in a simulated gastric condition and its chelating ability remained unaltered. These results explored an informative bioactive peptides with varied activity and one valuable among is the copper chelating with antioxidant property. Furthermore, these Chia seed protein hydrolysates can be useful as dietary supplements to enhance mineral bioavailability.
format	article
author	Latha B V Likhitha R Chethan Kumar M
author_facet	Latha B V Likhitha R Chethan Kumar M
author_sort	Latha B V
title	Copper chelating protein hydrolysate from Salvia hispanica L. by pepsin-pancreatin treatment
title_short	Copper chelating protein hydrolysate from Salvia hispanica L. by pepsin-pancreatin treatment
title_full	Copper chelating protein hydrolysate from Salvia hispanica L. by pepsin-pancreatin treatment
title_fullStr	Copper chelating protein hydrolysate from Salvia hispanica L. by pepsin-pancreatin treatment
title_full_unstemmed	Copper chelating protein hydrolysate from Salvia hispanica L. by pepsin-pancreatin treatment
title_sort	copper chelating protein hydrolysate from salvia hispanica l. by pepsin-pancreatin treatment
publisher	Elsevier
publishDate	2021
url	https://doaj.org/article/e3cdca8a685b42e3b2af940ff414bbe3
work_keys_str_mv	AT lathabv copperchelatingproteinhydrolysatefromsalviahispanicalbypepsinpancreatintreatment AT likhithar copperchelatingproteinhydrolysatefromsalviahispanicalbypepsinpancreatintreatment AT chethankumarm copperchelatingproteinhydrolysatefromsalviahispanicalbypepsinpancreatintreatment
_version_	1718408291108782080

Copper chelating protein hydrolysate from Salvia hispanica L. by pepsin-pancreatin treatment

Ejemplares similares