Soybean peptide aggregates improved calcium binding capacity

Liu, He; Lv, Ying; Xu, Jingting; Guo, Shuntang

doi:10.1016/j.lwt.2015.11.046

Cited by 28 publications

(17 citation statements)

References 46 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Amino acid analysis showed that the amino acids compositions in SP and FSP were similar. Asparagine and glutamic acid were major amino acids in both SP and FSP (Dilshat, Parida, Nurmuhammat, Kimono, & Nobuo, 2012;Liu, Lv, Xu, & Guo, 2016). In this study, the contents of isoleucine, leucine, methionine, and valine in FSP were increased by 34.74%, 47.31%, 109.80%, and 30.4%, respectively, compared to SP (Table 3).…”

Section: Amino Acids Composition Of Peptides In Fsbmmentioning

confidence: 48%

Peptides derived from fermented soybean meal suppresses intestinal inflammation and enhances epithelial barrier function in piglets

Chen

Zong

Shi

et al. 2019

Food and Agricultural Immunology

View full text Add to dashboard Cite

This study was to investigate the effects of peptides derived from fermented soybean meal (FSP) on intestinal inflammation and epithelial barrier function of the piglets. Compared to fed soybean meal, piglets fed with fermented soybean meal (FSBM) exhibit lower serum levels of IL-6, IL-1β and D-lactate, and reduced ileum macrophage infiltration. Besides, the FSBM upregulated (p < 0.05) expression of mucins and tight junction (TJ) proteins in the jejunum and ileum of piglets. The FSP were prepared with alkali extraction and a 3-kDa molecular weight cut-off membrane system. In vitro, FSP reducing the mRNA expression of IL-6, IL-1β, IL-8 and attenuated Escherichia coli K88induced inflammation in the intestinal porcine epithelial cells-J2 (IPEC-J2). Furthermore, FSP increased (p < 0.05) the expression of TJ proteins and transepithelial electrical resistance in IPEC-J2 cells. These results suggest that FSP could improve small intestinal health by enhancing epithelial barrier function and suppressing inflammation.

show abstract

Section: Amino Acids Composition Of Peptides In Fsbmmentioning

confidence: 48%

Peptides derived from fermented soybean meal suppresses intestinal inflammation and enhances epithelial barrier function in piglets

Chen

Zong

Shi

et al. 2019

Food and Agricultural Immunology

View full text Add to dashboard Cite

show abstract

“…However, calcium deficiency is still widespread due to insufficient absorption of the intake calcium and low bioavailability [57,58,59,60]. Currently, organic calcium (especially the peptide-calcium complex) as a new type of calcium supplement has become a hot research topic, due to its good therapeutic effects in clinical practice [61,62]. In the present study, we investigated whether CPPH + CaCO 3 and CPPH-Ca promoted calcium absorption and how such an effect might impair kidney gene expression and gut microbiota.…”

Section: Discussionmentioning

confidence: 99%

Effect of Chlorella Pyrenoidosa Protein Hydrolysate-Calcium Chelate on Calcium Absorption Metabolism and Gut Microbiota Composition in Low-Calcium Diet-Fed Rats

Hua

Xiong

et al. 2019

Marine Drugs

View full text Add to dashboard Cite

In our current investigation, we evaluated the effect of Chlorella pyrenoidosa protein hydrolysate (CPPH) and Chlorella pyrenoidosa protein hydrolysate-calcium chelate (CPPH-Ca) on calcium absorption and gut microbiota composition, as well as their in vivo regulatory mechanism in SD rats fed low-calcium diets. Potent major compounds in CPPH were characterized by HPLC-MS/MS, and the calcium-binding mechanism was investigated through ultraviolet and infrared spectroscopy. Using high-throughput next-generation 16S rRNA gene sequencing, we analyzed the composition of gut microbiota in rats. Our study showed that HCPPH-Ca increased the levels of body weight gain, serum Ca, bone activity, bone mineral density (BMD) and bone mineral content (BMC), while decreased serum alkaline phosphatase (ALP) and inhibited the morphological changes of bone. HCPPH-Ca up-regulated the gene expressions of transient receptor potential cation V5 (TRPV5), TRPV6, calcium-binding protein-D9k (CaBP-D9k) and a calcium pump (plasma membrane Ca-ATPase, PMCA1b). It also improved the abundances of Firmicutes and Lactobacillus. Bifidobacterium and Sutterella were both positively correlated with calcium absorption. Collectively, these findings illustrate the potential of HCPPH-Ca as an effective calcium supplement.

show abstract

“…SSP 4 -P 1 and PP 1 -P 1 are unadsorbed proteolytic peptides without the ability to bind to calcium. Liu et al 16 found that unadsorbed soybean peptides have Ca-binding abilities when Ca-MCAC was used to separate soybean peptides. This phenomenon can be explained by the spatial mass model.…”

Section: Wileyonlinelibrarycom/jsfamentioning

confidence: 99%

“…This effect is difficult to avoid and could result in unadsorbed component containing some peptides with Ca-binding abilities. 16 Peptides that promote Ca absorption have been widely reported, and several calcium-binding peptides from food proteins have been isolated and identified. Daengprok et al 27 reported the mechanism of eggshell matrix proteins with respect to promoting calcium transport in intestinal cells; the mechanism may be related to the presence of glutamate and aspartate.…”

Section: Wileyonlinelibrarycom/jsfamentioning

confidence: 99%

Structural characterization of calcium‐binding sunflower seed and peanut peptides and enhanced calcium transport by calcium complexes in Caco‐2 cells

et al. 2020

View full text Add to dashboard Cite

BACKGROUND: Peptide-Ca complexes can promote Ca absorption. The present study aimed to determine the transport mechanism and structural characteristics of sunflower seed and peanut peptides with high Ca binding capacity with respect to developing third-generation Ca supplements and functional food ingredients. RESULTS: High Ca-binding fractions of 1-3 kDa sunflower seed peptide (SSP 4) and ≥ 10 kDa peanut peptide (PP 1) had higher amount of Ca transported than CaCl 2 and two hydrolyzed proteins in Caco-2 cells. SSP 4 and PP 1 were separated by Ca ion metal chelate affinity chromatography, and high Ca-binding fractions were observed for SSP 4-P 2 and PP 1-P 2. The amino acid sequences of SSP 4-P 2 and PP 1-P 2 were characterized by high-performance liquid chromatography-electrospray ionization-time of flight mass spectrometry. Seven and eight peptides were identified from SSP 4-P 2 and PP 1-P 2 , respectively. These peptides had molecular weights ranging from 1500 Da to 2500 Da and a large number of characteristic amino acid sequences, such as EEEQQQ, EQ-QQQ-QQ, QQ-QQQQQ, E-EEE, EE-EEQ, RR, Q-QQ-QQQ, EE-EQ-EE-Q, QQ-QQQQ, and Q-QQQQ, where 'E' is glutamic acid and 'Q' is glutamine. CONCLUSION: SSP 4 and PP 1 can promote Ca transport in Caco-2 cells without affecting cell permeability. The amino acid sequences of SSP 4-P 2 and PP 1-P 2 with high Ca-binding abilities contain characteristic sequences, such as continuous glutamic acid and glutamine, and have low molecular weights.

show abstract

Soybean peptide aggregates improved calcium binding capacity

Cited by 28 publications

References 46 publications

Peptides derived from fermented soybean meal suppresses intestinal inflammation and enhances epithelial barrier function in piglets

Peptides derived from fermented soybean meal suppresses intestinal inflammation and enhances epithelial barrier function in piglets

Effect of Chlorella Pyrenoidosa Protein Hydrolysate-Calcium Chelate on Calcium Absorption Metabolism and Gut Microbiota Composition in Low-Calcium Diet-Fed Rats

Structural characterization of calcium‐binding sunflower seed and peanut peptides and enhanced calcium transport by calcium complexes in Caco‐2 cells

Contact Info

Product

Resources

About