Elucidating the Calcium-Binding Site, Absorption Activities, and Thermal Stability of Egg White Peptide–Calcium Chelate

With the current study, we aimed to determine the characteristics and calcium absorption capacity of egg white peptide–calcium complex (EWP-Ca) and determine the effect of sterilization on EWP-Ca to study the possibility of EWP-Ca as a new potential calcium supplement. The results of SEM and EDS sho...

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Autores principales: Zhijie Bao, Penglin Zhang, Na Sun, Songyi Lin
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Lenguaje:EN
Publicado: MDPI AG 2021
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Acceso en línea:https://doaj.org/article/7a62bc28d8f24f4281f5fa5bcc865cb2
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spelling oai:doaj.org-article:7a62bc28d8f24f4281f5fa5bcc865cb22021-11-25T17:32:42ZElucidating the Calcium-Binding Site, Absorption Activities, and Thermal Stability of Egg White Peptide–Calcium Chelate10.3390/foods101125652304-8158https://doaj.org/article/7a62bc28d8f24f4281f5fa5bcc865cb22021-10-01T00:00:00Zhttps://www.mdpi.com/2304-8158/10/11/2565https://doaj.org/toc/2304-8158With the current study, we aimed to determine the characteristics and calcium absorption capacity of egg white peptide–calcium complex (EWP-Ca) and determine the effect of sterilization on EWP-Ca to study the possibility of EWP-Ca as a new potential calcium supplement. The results of SEM and EDS showed a high calcium chelating ability between EWP and calcium, and the structure of EWP-Ca was clustered spherical particles due its combination with calcium. The FTIR and Raman spectrum results showed that EWP could chelate with calcium by carboxyl, phosphate, and amino groups, and peptide bonds may also participate in peptide–calcium binding. Moreover, the calcium absorption of EWP-Ca measured by the intestinal everted sac model in rats was 32.38 ± 6.83 μg/mL, significantly higher than the sample with CaCl<sub>2,</sub> and the mixture of EWP and Ca (<i>p <</i> 0.05) revealed appropriate calcium absorption capacity. The fluorescence spectra and CD spectra showed that sterilization caused a decrease in the content of α-helix and β-sheet and a significant increase in β-turn (<i>p <</i> 0.05). Sterilization changed the EWP-Ca structure and decreased its stability; the calcium-binding capacity of EWP-Ca after sterilization was decreased to 41.19% (<i>p <</i> 0.05). Overall, these findings showed that EWP could bind with calcium, form a peptide–calcium chelate, and serve as novel carriers for calcium supplements.Zhijie BaoPenglin ZhangNa SunSongyi LinMDPI AGarticleegg whitepeptide–calcium chelatecharacterizationthermal stabilitycalcium supplementChemical technologyTP1-1185ENFoods, Vol 10, Iss 2565, p 2565 (2021)
institution DOAJ
collection DOAJ
language EN
topic egg white
peptide–calcium chelate
characterization
thermal stability
calcium supplement
Chemical technology
TP1-1185
spellingShingle egg white
peptide–calcium chelate
characterization
thermal stability
calcium supplement
Chemical technology
TP1-1185
Zhijie Bao
Penglin Zhang
Na Sun
Songyi Lin
Elucidating the Calcium-Binding Site, Absorption Activities, and Thermal Stability of Egg White Peptide–Calcium Chelate
description With the current study, we aimed to determine the characteristics and calcium absorption capacity of egg white peptide–calcium complex (EWP-Ca) and determine the effect of sterilization on EWP-Ca to study the possibility of EWP-Ca as a new potential calcium supplement. The results of SEM and EDS showed a high calcium chelating ability between EWP and calcium, and the structure of EWP-Ca was clustered spherical particles due its combination with calcium. The FTIR and Raman spectrum results showed that EWP could chelate with calcium by carboxyl, phosphate, and amino groups, and peptide bonds may also participate in peptide–calcium binding. Moreover, the calcium absorption of EWP-Ca measured by the intestinal everted sac model in rats was 32.38 ± 6.83 μg/mL, significantly higher than the sample with CaCl<sub>2,</sub> and the mixture of EWP and Ca (<i>p <</i> 0.05) revealed appropriate calcium absorption capacity. The fluorescence spectra and CD spectra showed that sterilization caused a decrease in the content of α-helix and β-sheet and a significant increase in β-turn (<i>p <</i> 0.05). Sterilization changed the EWP-Ca structure and decreased its stability; the calcium-binding capacity of EWP-Ca after sterilization was decreased to 41.19% (<i>p <</i> 0.05). Overall, these findings showed that EWP could bind with calcium, form a peptide–calcium chelate, and serve as novel carriers for calcium supplements.
format article
author Zhijie Bao
Penglin Zhang
Na Sun
Songyi Lin
author_facet Zhijie Bao
Penglin Zhang
Na Sun
Songyi Lin
author_sort Zhijie Bao
title Elucidating the Calcium-Binding Site, Absorption Activities, and Thermal Stability of Egg White Peptide–Calcium Chelate
title_short Elucidating the Calcium-Binding Site, Absorption Activities, and Thermal Stability of Egg White Peptide–Calcium Chelate
title_full Elucidating the Calcium-Binding Site, Absorption Activities, and Thermal Stability of Egg White Peptide–Calcium Chelate
title_fullStr Elucidating the Calcium-Binding Site, Absorption Activities, and Thermal Stability of Egg White Peptide–Calcium Chelate
title_full_unstemmed Elucidating the Calcium-Binding Site, Absorption Activities, and Thermal Stability of Egg White Peptide–Calcium Chelate
title_sort elucidating the calcium-binding site, absorption activities, and thermal stability of egg white peptide–calcium chelate
publisher MDPI AG
publishDate 2021
url https://doaj.org/article/7a62bc28d8f24f4281f5fa5bcc865cb2
work_keys_str_mv AT zhijiebao elucidatingthecalciumbindingsiteabsorptionactivitiesandthermalstabilityofeggwhitepeptidecalciumchelate
AT penglinzhang elucidatingthecalciumbindingsiteabsorptionactivitiesandthermalstabilityofeggwhitepeptidecalciumchelate
AT nasun elucidatingthecalciumbindingsiteabsorptionactivitiesandthermalstabilityofeggwhitepeptidecalciumchelate
AT songyilin elucidatingthecalciumbindingsiteabsorptionactivitiesandthermalstabilityofeggwhitepeptidecalciumchelate
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