Research and Development of Functional Peptide in Foods

A special issue of Foods (ISSN 2304-8158). This special issue belongs to the section "Nutraceuticals, Functional Foods, and Novel Foods".

Deadline for manuscript submissions: closed (20 March 2023) | Viewed by 24433

Special Issue Editor

National Marine Food Engineering Technology Research Center, Dalian Polytechnic University, Dalian, China
Interests: foods; intestinal microbes; bioconversion of food resources; food-derived protein (peptide); food function and nutrition
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Functional peptides, derived from food proteins, have been studied due to their potential as health-promoting agents against numerous human health and disease conditions. These peptides can regulate important body functions through their activities, including antioxidant, antihypertensive, antimicrobial, antithrombotic, memory enhancement, immunomodulatory, and mineral binding functions. In the past few decades, a wide range of functional peptides in foods have been identified, with multiple health beneficial activities. However, the commercial application of these functional peptides has been delayed because of the absence of appropriate and scalable production methods, proper exploration of the mechanisms of action, high gastro-intestinal digestibility, and variable absorption rate. These need to be studied in depth.

In this Special Issue, original research articles and reviews are welcome. Research areas may include (but are not limited to) the structure–activity relationship of functional peptides, their digestive properties, absorption and bioavailability, and their molecular mechanisms of action.

We look forward to receiving your contributions.

Prof. Dr. Songyi Lin
Guest Editor

Manuscript Submission Information

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Keywords

  • functional peptides
  • structure–activity relationship
  • gastro-intestinal digestion
  • intestinal absorption
  • molecular mechanisms

Published Papers (12 papers)

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Research

20 pages, 10100 KiB  
Article
Synergistic Effect of Combined Walnut Peptide and Ginseng Extracts on Memory Improvement in C57BL/6 Mice and Potential Mechanism Exploration
by Junxi Fu, Wentian Song, Xiaobing Song, Li Fang, Xiyan Wang, Yue Leng, Ji Wang, Chunlei Liu and Weihong Min
Foods 2023, 12(12), 2329; https://0-doi-org.brum.beds.ac.uk/10.3390/foods12122329 - 09 Jun 2023
Cited by 3 | Viewed by 1248
Abstract
This work aimed to investigate whether there are synergistic effects between walnut peptide (WNP) and ginseng extracts (GSE) treatments to ameliorate the memory impairment caused by scopolamine (SCOP). The Morris water maze trial, hippocampal neuron morphology, neurotransmitters, and synaptic ultrastructure were examined, along [...] Read more.
This work aimed to investigate whether there are synergistic effects between walnut peptide (WNP) and ginseng extracts (GSE) treatments to ameliorate the memory impairment caused by scopolamine (SCOP). The Morris water maze trial, hippocampal neuron morphology, neurotransmitters, and synaptic ultrastructure were examined, along with brain-derived neurotrophic factor (BDNF)-related signaling pathway proteins. The results of the Morris water maze trial demonstrated that the combined administration of WNP and GSE effectively alleviated memory impairment in C57BL/6 rats caused by SCOP. Improvement in the morphology of hippocampal neurons, dendritic spines, and synaptic plasticity and upregulation of neurotransmitters AChE, ACh, ChAT, Glu, DA, and 5-HT supported the memory improvement effects of WNP + GSE. In addition, compared with the model group, WNP + GSE significantly enhanced the protein levels of VAChT, Trx-1, and the CREB/BDNF/TrkB pathway in hippocampal and PC12 cells induced by SCOP (p < 0.05). Notably, WNP + GSE boosted memory via multiple pathways, not only the BDNF/TrkB/CREB target. Full article
(This article belongs to the Special Issue Research and Development of Functional Peptide in Foods)
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11 pages, 1633 KiB  
Article
Hepatoprotective Effect of Albumin Peptide Fractions from Corn Germ Meal against Alcohol-Induced Acute Liver Injury in Mice
by Yali Yu, Shiyao Guan, Mengmeng Feng, Lijun Wang and Feng Gao
Foods 2023, 12(6), 1183; https://0-doi-org.brum.beds.ac.uk/10.3390/foods12061183 - 11 Mar 2023
Viewed by 1377
Abstract
Acute alcoholic liver disease can cause serious liver damage. This study reports on the hepatoprotective effect of albumin peptide fractions from corn germ meal (MW < 1 kDa) (APF4) on acute alcohol hepatic damage in mice. In the mice model, the results indicated [...] Read more.
Acute alcoholic liver disease can cause serious liver damage. This study reports on the hepatoprotective effect of albumin peptide fractions from corn germ meal (MW < 1 kDa) (APF4) on acute alcohol hepatic damage in mice. In the mice model, the results indicated that APF4 at a dose of 800 mg/kg/bw could markedly boost alcohol metabolism, which was shown in the reduced duration of the loss of the righting reflex; the reduced level of blood alcohol concentration (BAC), cytochrome P450 2E1 (CYP2E1), alanine aminotransferase (ALT), aminotransferase (AST), triglycerides (TG), and malondialdehyde (MDA) (p < 0.01); the enhanced activity of aldehyde dehydrogenase (ALDH); and the superoxide dismutase (SOD) and glutathione (GSH) levels being increased by up to 84.02% and 193.22% (p < 0.01) compared to the control group. The antioxidant capability and lipid peroxidation inhibition activity of APF4 may be responsible for its protective effect against liver damage induced by alcohol. The findings suggested that APF4 had the hepatoprotective property against liver damage induced by alcohol. Full article
(This article belongs to the Special Issue Research and Development of Functional Peptide in Foods)
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16 pages, 4103 KiB  
Article
Endogenous Peptides Identified in Soy Sauce Aroma Style Baijiu Which Interacts with the Main Flavor Compounds during the Distillation Process
by Xu Zhang, Xinshe Li, Yunhao Zhao, Qiang Wu, Yong Wan and Yougui Yu
Foods 2022, 11(21), 3339; https://0-doi-org.brum.beds.ac.uk/10.3390/foods11213339 - 24 Oct 2022
Cited by 2 | Viewed by 1450
Abstract
Endogenous peptides in Chinese baijiu have been recently reported. However, little information is available on their correlation with the main flavor substances. One hundred and forty-six peptides, consisting of more bitter amino acids and key amino acids responsible for bioactivity, were identified in [...] Read more.
Endogenous peptides in Chinese baijiu have been recently reported. However, little information is available on their correlation with the main flavor substances. One hundred and forty-six peptides, consisting of more bitter amino acids and key amino acids responsible for bioactivity, were identified in tail liquor using liquid chromatography-mass spectrometry/mass spectrometry (LC-MS/MS). Additionally, the content of endogenous peptides increased gradually with distillation time, showing a high negative correlation with total esters (r = −0.929) and total alcohol (r = −0.964) but presented a moderate positive correlation with the total acid content (r = 0.714). The results of the correlation analysis between them were further proved by molecular docking, which showed that these endogenous peptides in baijiu interacted with the main flavor substances via hydrogen bonds. This study clarifies the dynamic changes of endogenous peptides during distillation and provides a theoretical reference for the relationship between these peptides and the main flavor substances. Full article
(This article belongs to the Special Issue Research and Development of Functional Peptide in Foods)
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14 pages, 3229 KiB  
Article
C-Terminal Modification on the Immunomodulatory Activity, Antioxidant Activity, and Structure–Activity Relationship of Pulsed Electric Field (PEF)-Treated Pine Nut Peptide
by Shuyu Zhang, Liu Dong, Zhijie Bao and Songyi Lin
Foods 2022, 11(17), 2649; https://0-doi-org.brum.beds.ac.uk/10.3390/foods11172649 - 31 Aug 2022
Cited by 3 | Viewed by 1256
Abstract
In this study, a novel peptide VNAVL was synthesized by removing the C-terminal histidine on the basis of a bioactive peptide VNAVLH obtained from pine nut (Pinus koraiensis Sieb. et Zucc) protein. The effects of removing histidine on antioxidant activity, immunomodulatory activity, and [...] Read more.
In this study, a novel peptide VNAVL was synthesized by removing the C-terminal histidine on the basis of a bioactive peptide VNAVLH obtained from pine nut (Pinus koraiensis Sieb. et Zucc) protein. The effects of removing histidine on antioxidant activity, immunomodulatory activity, and secondary structure of the PEF-treated peptide were discussed. Compared with VNAVLH, VNAVL only exhibited lower antioxidant activity, but no immunomodulatory activity to release TNF-α, IL-6, and NO by activating RAW 264.7 cells. In addition, both antioxidant and immune activities of VNAVLH were significantly more sensitive to treatment with 40 kV/cm than other field intensities, whereas VNAVL was not sensitive to field strength changes. CD spectra and DSSP analysis verified that both peptides consisted of a β structure and random coil, but the ability of VNAVL to transform the random coil via PEF treatment is weaker than that of VNAVLH. Therefore, PEF treatment might expose the key active site located on the C-terminal histidine by altering the secondary structure of the peptide. Full article
(This article belongs to the Special Issue Research and Development of Functional Peptide in Foods)
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17 pages, 2919 KiB  
Article
Manufacture of Whey Protein Hydrolysates Using Plant Enzymes: Effect of Processing Conditions and Simulated Gastrointestinal Digestion on Angiotensin-I-Converting Enzyme (ACE) Inhibitory Activity
by Marie Peslerbes, Angélica Fellenberg, Julien Jardin, Amélie Deglaire and Rodrigo A. Ibáñez
Foods 2022, 11(16), 2429; https://0-doi-org.brum.beds.ac.uk/10.3390/foods11162429 - 12 Aug 2022
Cited by 6 | Viewed by 1618
Abstract
Hydrolysis of proteins leads to the release of bioactive peptides with positive impact on human health. Peptides exhibiting antihypertensive properties (i.e., inhibition of angiotensin-I-converting enzyme) are commonly found in whey protein hydrolysates made with enzymes of animal, plant or microbial origin. However, bioactive [...] Read more.
Hydrolysis of proteins leads to the release of bioactive peptides with positive impact on human health. Peptides exhibiting antihypertensive properties (i.e., inhibition of angiotensin-I-converting enzyme) are commonly found in whey protein hydrolysates made with enzymes of animal, plant or microbial origin. However, bioactive properties can be influenced by processing conditions and gastrointestinal digestion. In this study, we evaluated the impact of three plant enzymes (papain, bromelain and ficin) in the manufacture of whey protein hydrolysates with varying level of pH, enzyme-to-substrate ratio and time of hydrolysis, based on a central composite design, to determine the degree of hydrolysis and antihypertensive properties. Hydrolysates made on laboratory scales showed great variation in the type of enzyme used, their concentrations and the pH level of hydrolysis. However, low degrees of hydrolysis in papain and bromelain treatments were associated with increased antihypertensive properties, when compared to ficin. Simulated gastrointestinal digestion performed for selected hydrolysates showed an increase in antihypertensive properties of hydrolysates made with papain and bromelain, which was probably caused by further release of peptides. Several peptides with reported antihypertensive properties were found in all treatments. These results suggest plant enzymes used in this study can be suitable candidates to develop ingredients with bioactive properties. Full article
(This article belongs to the Special Issue Research and Development of Functional Peptide in Foods)
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20 pages, 3950 KiB  
Article
Identification of the DPP-IV Inhibitory Peptides from Donkey Blood and Regulatory Effect on the Gut Microbiota of Type 2 Diabetic Mice
by Chaoyue Ma, Dan Liu, Huifang Hao and Xiaotong Wu
Foods 2022, 11(14), 2148; https://0-doi-org.brum.beds.ac.uk/10.3390/foods11142148 - 20 Jul 2022
Cited by 7 | Viewed by 1896
Abstract
After being treated with protease K, peptides extracted from donkey blood were separated, identified, and characterized. The results showed that Sephadex G-25 medium purified with MW < 3 kDa had the highest dipeptidyl peptidase IV (DPP-IV) inhibition capacity. Three-hundred-and-thirty-four peptides were identified with [...] Read more.
After being treated with protease K, peptides extracted from donkey blood were separated, identified, and characterized. The results showed that Sephadex G-25 medium purified with MW < 3 kDa had the highest dipeptidyl peptidase IV (DPP-IV) inhibition capacity. Three-hundred-and-thirty-four peptides were identified with UPLC–MS/MS. Peptide Ranker and molecular docking analysis were used to screen active peptides, and 16 peptides were finalized out of the 334. The results showed that the lowest binding energy between P7(YPWTQ) and DPP-IV was −9.1, and the second-lowest binding energy between P1(VDPENFRLL) and DPP-IV was −8.7. The active peptides(MW < 3 kDa) could cause a reduction in the fasting blood glucose levels of type 2 diabetic mice, improve glucose tolerance, and facilitate healing of the damaged structure of diabetic murine liver and pancreas. Meanwhile, the peptides were found to ameliorate the diabetic murine intestinal micro-ecological environment to a certain extent. Full article
(This article belongs to the Special Issue Research and Development of Functional Peptide in Foods)
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15 pages, 2990 KiB  
Article
Novel Antioxidant Peptides from Grateloupia livida Hydrolysates: Purification and Identification
by Xiao Hu, Chuang Pan, Miaomiao Cai, Laihao Li, Xianqing Yang, Huan Xiang and Shengjun Chen
Foods 2022, 11(10), 1498; https://0-doi-org.brum.beds.ac.uk/10.3390/foods11101498 - 20 May 2022
Cited by 7 | Viewed by 1813
Abstract
Grateloupia livida protein was hydrolyzed with various proteases (alkaline protease, Protamex and neutral protease) to obtain anti-oxidative peptides. Antioxidant activity of the enzymatic hydrolysates was evaluated by the DPPH radical scavenging, ABTS radical scavenging and reducing power assays. The results suggested that hydrolysates [...] Read more.
Grateloupia livida protein was hydrolyzed with various proteases (alkaline protease, Protamex and neutral protease) to obtain anti-oxidative peptides. Antioxidant activity of the enzymatic hydrolysates was evaluated by the DPPH radical scavenging, ABTS radical scavenging and reducing power assays. The results suggested that hydrolysates obtained by neutral protease 1 h hydrolysis displayed the highest antioxidant activity (DPPH IC50 value of 3.96 mg/mL ± 0.41 mg/mL, ABTS IC50 value of 0.88 ± 0.13 mg/mL and reducing power of 0.531 ± 0.012 at 8 mg/mL), and had low molecular weight distribution (almost 99% below 3 kDa). Three fractions (F1–F3) were then isolated from the hydrolysates by using semi-preparative RP-HPLC, and the fraction F3 showed the highest antioxidant ability. Four antioxidant peptides were identified as LYEEMKESKVINADK, LEADNVGVVLMGDGR, LIDDSFGTDAPVPERL, and GLDELSEEDRLT from the F3 by LC-MS/MS. Online prediction showed that the four peptides possessed good water solubility, non-toxic and non-allergenic characteristics. Moreover, the LYEEMKESKVINADK exhibited the highest antioxidant ability. Molecular docking revealed that these peptides could all well bind with Kelch-like ECH-associated protein 1 (Keap1), among which LYEEMKESKVINADK had the lowest docking energy (−216.878 kcal/mol). These results demonstrated that the antioxidant peptides from Grateloupia livida could potentially be used as natural antioxidant. Full article
(This article belongs to the Special Issue Research and Development of Functional Peptide in Foods)
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11 pages, 2100 KiB  
Article
Identification and Characterization of Dipeptidyl Peptidase-IV Inhibitory Peptides from Oat Proteins
by Wei Wang, Xiaoqing Liu, Yiju Li, Haixi You, Zhipeng Yu, Liying Wang, Xuebo Liu and Long Ding
Foods 2022, 11(10), 1406; https://0-doi-org.brum.beds.ac.uk/10.3390/foods11101406 - 12 May 2022
Cited by 8 | Viewed by 2105
Abstract
In this study, flavourzyme, papain, neutrase, and alcalase, as well as gastrointestinal digestion simulated with pepsin and pancreatin, were used to hydrolyze oat protein, and the dipeptidyl peptidase-IV (DPP-IV) inhibitory activities of the oat protein hydrolysates were investigated. The results indicated that the [...] Read more.
In this study, flavourzyme, papain, neutrase, and alcalase, as well as gastrointestinal digestion simulated with pepsin and pancreatin, were used to hydrolyze oat protein, and the dipeptidyl peptidase-IV (DPP-IV) inhibitory activities of the oat protein hydrolysates were investigated. The results indicated that the oat protein hydrolysate by neutrase showed the most potent DPP-IV inhibitory property with an IC50 value of 2.55 ± 0.38 mg/mL. Using UPLC-MS/MS, ten new DPP-IV inhibitory peptides were identified from the oat protein hydrolysate by neutrase. Among these peptides, IPQHY, VPQHY, VAVVPF, and VPLGGF exhibited the strongest DPP-IV inhibitory activity with IC50 values below 50 μM, and all of them acted as mixed-type inhibitors. Molecular docking indicated that the above four oat-derived peptides were predicted to form hydrogen bonds, attractive charge, and hydrophobic interactions with the residues of the active site of DPP-IV. Therefore, our results suggest that oat is an excellent protein source for food-derived DPP-IV inhibitory peptides and it has the prospect of becoming a dietary supplement for T2DM. Full article
(This article belongs to the Special Issue Research and Development of Functional Peptide in Foods)
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12 pages, 2793 KiB  
Article
Detection of Balenine in Mouse Plasma after Administration of Opah-Derived Balenine by HPLC with PITC Pre-Column Derivatization
by Yasutaka Shigemura, Yu Iwasaki, Yoshio Sato, Tomomi Kato, Takuya Seko and Kenji Ishihara
Foods 2022, 11(4), 590; https://0-doi-org.brum.beds.ac.uk/10.3390/foods11040590 - 18 Feb 2022
Cited by 2 | Viewed by 1737
Abstract
We examined the absorption of balenine (Bal) in mouse blood after the administration of a high-purity Bal prepared from opah muscle. Using HPLC with phenyl isothiocyanate pre-column derivatization, we successfully isolated imidazole peptides and their constituents. We detected Bal and 3-methylhistidine (3-Me-His) in [...] Read more.
We examined the absorption of balenine (Bal) in mouse blood after the administration of a high-purity Bal prepared from opah muscle. Using HPLC with phenyl isothiocyanate pre-column derivatization, we successfully isolated imidazole peptides and their constituents. We detected Bal and 3-methylhistidine (3-Me-His) in mouse blood 1 h after the administration of opah-derived Bal. The concentrations of Bal and 3-Me-His significantly increased to 128.27 and 69.09 nmol/mL in plasma, respectively, but were undetectable in control and carnosine (Car)-administrated mice. In contrast, β-alanine and histidine did not increase in mouse plasma 1 h after the administration of Car and opah-derived Bal. The present study is the first report on the absorption of food-derived Bal in mouse blood and serves as a pilot study for future clinical trials. Full article
(This article belongs to the Special Issue Research and Development of Functional Peptide in Foods)
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17 pages, 7654 KiB  
Article
Gaussian Accelerated Molecular Dynamics Simulations Investigation on the Mechanism of Angiotensin-Converting Enzyme (ACE) C-Domain Inhibition by Dipeptides
by Congcong Li, Kaifeng Liu, Siao Chen, Lu Han and Weiwei Han
Foods 2022, 11(3), 327; https://doi.org/10.3390/foods11030327 - 25 Jan 2022
Cited by 6 | Viewed by 3143
Abstract
Angiotensin-converting enzyme (ACE)-inhibitory peptides extracted from food proteins can lower blood pressure by inhibiting ACE activity. A recent study showed that the inhibitory activity of IY (Ile-Tyr, a dipeptide derived from soybean protein) against ACE was much higher than that of LL (Leu-Leu), [...] Read more.
Angiotensin-converting enzyme (ACE)-inhibitory peptides extracted from food proteins can lower blood pressure by inhibiting ACE activity. A recent study showed that the inhibitory activity of IY (Ile-Tyr, a dipeptide derived from soybean protein) against ACE was much higher than that of LL (Leu-Leu), although they had similar hydrophobic and predicted activity values. It was difficult to reveal the deep molecular mechanism underlying this phenomenon by traditional experimental methods. The Apo and two complex systems (i.e., ACE–LL and ACE–IY) were therefore subjected to 1 μs long Gaussian accelerated molecular dynamics (GaMD) simulations. The results showed that the binding of IY can cause obvious contraction of the active site of ACE, mainly manifested by a significant lateral shift of α13, α14, and α15. In addition, hinge 2 and hinge 3 were more stable in the ACE–IY system, while these phenomena were not present in the ACE–LL system. Moreover, the α10 of the IY-bound ACE kept an inward state during the simulation progress, which facilitated the ACE to remain closed. However, for the LL-bound ACE, the α10 switched between two outward states. To sum up, our study provides detailed insights into inhibitor-induced conformational changes in ACE that may help in the design of specific inhibitors targeting ACE for the treatment of hypertension. Full article
(This article belongs to the Special Issue Research and Development of Functional Peptide in Foods)
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15 pages, 40573 KiB  
Article
Tricholoma matsutake-Derived Peptides Ameliorate Inflammation and Mitochondrial Dysfunction in RAW264.7 Macrophages by Modulating the NF-κB/COX-2 Pathway
by Mengqi Li, Qi Ge, Hanting Du and Songyi Lin
Foods 2021, 10(11), 2680; https://0-doi-org.brum.beds.ac.uk/10.3390/foods10112680 - 03 Nov 2021
Cited by 8 | Viewed by 2119
Abstract
Tricholoma matsutake is an edible fungus that contains various bioactive substances, some of them with immunostimulatory properties. Presently, there is limited knowledge about the functional components of T. matsutake. Our aim was to evaluate the protective effects and molecular mechanisms of two [...] Read more.
Tricholoma matsutake is an edible fungus that contains various bioactive substances, some of them with immunostimulatory properties. Presently, there is limited knowledge about the functional components of T. matsutake. Our aim was to evaluate the protective effects and molecular mechanisms of two T. matsutake-derived peptides, SDLKHFPF and SDIKHFPF, on lipopolysaccharide (LPS)-induced mitochondrial dysfunction and inflammation in RAW264.7 macrophages. Tricholoma matsutake peptides significantly ameliorated the production of inflammatory cytokines and inhibited the expression of COX-2, iNOS, IKKβ, p-IκB-α, and p-NF-κB. Immunofluorescence assays confirmed the inhibitory effect of T. matsutake peptides on NF-κB/p65 nuclear translocation. Furthermore, the treatment with T. matsutake peptides prevented the accumulation of reactive oxygen species, increased the Bcl-2/Bax ratio, reversed the loss of mitochondrial membrane potential, and rescued abnormalities in cellular energy metabolism. These findings indicate that T. matsutake peptides can effectively inhibit the activation of NF-κB/COX-2 and may confer an overall protective effect against LPS-induced cell damage. Full article
(This article belongs to the Special Issue Research and Development of Functional Peptide in Foods)
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12 pages, 2630 KiB  
Article
Elucidating the Calcium-Binding Site, Absorption Activities, and Thermal Stability of Egg White Peptide–Calcium Chelate
by Zhijie Bao, Penglin Zhang, Na Sun and Songyi Lin
Foods 2021, 10(11), 2565; https://0-doi-org.brum.beds.ac.uk/10.3390/foods10112565 - 25 Oct 2021
Cited by 13 | Viewed by 2793
Abstract
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 [...] Read more.
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 CaCl2, and the mixture of EWP and Ca (p < 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 (p < 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% (p < 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. Full article
(This article belongs to the Special Issue Research and Development of Functional Peptide in Foods)
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