Selenium-enriched peptides identified from selenium-enriched soybean protein hydrolysate: protective effects against heat damage in Caco-2 cells

Chen, Xinwei; Liu, Wanlu; Zhang, Jian; He, Li; Liu, Xinqi

doi:10.1039/d3fo01103h

Cited by 9 publications

(4 citation statements)

References 55 publications

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“…Three indicators, root mean square deviation (RMSD), solvent accessible surface area (SASA), and root mean square fluctuation (RMSF), were chosen to analyze the stability of these complexes. As shown in Figure 4 A–C, the RMSD values of the four systems (α-amylase, three peptide-enzyme complexes) almost reached equilibrium at 100 ns of the simulation, indicating that all the simulated systems reached a steady state, so the kinetic simulation results are reliable and can be used for subsequent kinetic simulation analysis [ 32 ]. The RMSD values of all three peptide–enzyme complexes can reach a steady state faster and with less fluctuation than α-amylase alone, indicating that the binding of peptides to important residues of α-amylase can make α-amylase reach equilibrium more readily and have better stability [ 33 ].…”

Section: Resultsmentioning

confidence: 99%

Statistical Characterization of Food-Derived α-Amylase Inhibitory Peptides: Computer Simulation and Partial Least Squares Regression Analysis

Li,

Yang,

et al. 2024

Molecules

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α-Amylase inhibitory peptides are used to treat diabetes, but few studies have statistically characterized their interaction with α-amylase. This study performed the molecular docking of α-amylase with inhibitory peptides from published papers. The key sites, side chain chargeability, and hydrogen bond distribution characteristics were analyzed. Molecular dynamics simulated the role of key sites in complex stability. Moreover, partial least squares regression (PLSR) was used to analyze the contribution of different amino acids in the peptides to inhibition. The results showed that, for the α-amylase molecule, His201 and Gln63, with the highest interaction numbers (INs, 15, 15) and hydrogen bond values (HBVs, 11.50, 10.33), are the key sites on α-amylase, and amino acids with positively charged side chains were important for inhibitory activity. For the inhibitory peptides, Asp and Arg had the highest HBVs, and amino acids with charged side chains were more likely to form hydrogen bonds and exert inhibitory activity. In molecular dynamics simulations, peptides involving key binding sites formed more stable complexes with α-amylase than α-amylase alone, suggesting enhanced inhibitory effects. Further, PLSR results showed that amino acids close to the N-terminus of the inhibitory peptide, located in the third and fifth positions, were significantly correlated with its inhibitory activity. In conclusion, this study provides a new approach to developing and screening α-amylase inhibitors.

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Section: Resultsmentioning

confidence: 99%

Statistical Characterization of Food-Derived α-Amylase Inhibitory Peptides: Computer Simulation and Partial Least Squares Regression Analysis

Li,

Yang,

et al. 2024

Molecules

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“…The soybean peptides were configured as a 1 mg mL −1 solution and purified using an Akta Pure protein purifier (Cytiva Biotechnology, USA) loaded with a Superdex 30 Increase 10/300 GL gel column. 17 The sample volume was 500 μL per sample, and isocratic elution was performed using ultrapure water at a flow rate of 0.5 mL min −1 . The eluate was detected by UV absorbance at 220 nm.…”

Section: Methodsmentioning

confidence: 99%

“…The eluate was detected by UV absorbance at 220 nm. 17 The collector was set to collect 1 mL of eluate per tube. A total of 1.5 times the column volume of eluate was collected.…”

Section: Methodsmentioning

confidence: 99%

Evaluating the capability of soybean peptides as calcium ion carriers: a study through sequence analysis and molecular dynamics simulations

An,

Wang,

et al. 2024

RSC Adv.

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“…Microalgae are rich in protein, making them capable of producing the organic Se in the form of selenoproteins, which is conducive to humans and animals, and it is a promising resource to develop nutraceuticals [13][14][15][16]. Chlorella spp., rich in essential amino acids, fatty acids, proteins, and vitamins [17], is listed on the Generally Recognized as Safe (GRAS) inventory, a regulatory framework for substances intended for use in human food or animal food, established by the FDA (https://www.fda.gov/food/gras-notice-inventory/recentlypublished-gras-notices-and-fda-letters accessed on 5 December 2023).…”

Section: Introductionmentioning

confidence: 99%

Heterotrophic Selenium Incorporation into Chlorella vulgaris K-01: Selenium Tolerance, Assimilation, and Removal through Microalgal Cells

Zhang,

Hua

et al. 2024

Foods

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Chlorella has been applied in the production of selenium (Se) enriched organic biomass. However, limited information exists regarding heterotrophic selenium tolerance and its incorporation into Chlorella. This study aimed to investigate the potential of using Chlorella vulgaris K-01 for selenium biotransformation. To assess the dose-response effect of Se stress on the strain, time-series growth curves were recorded, growth productivity parameters were calculated, and Gaussian process (GP) regression analysis was performed. The strain’s carbon and energy metabolism were evaluated by measuring residual glucose in the medium. Characterization of different forms of intracellular Se and residual Se in the medium was conducted using inductively coupled plasma-mass spectrometry (ICP-MS) and inductively coupled plasma optical emission spectrometer (ICP-OES). The EC50 value for the strain in response to Se stress was 38.08 mg/L. The maximum biomass productivity was 0.26 g/L/d. GP regression analysis revealed that low-level Se treatment could increase the biomass accumulation and the carrying capacity of Chlorella vulgaris K-01 in a heterotrophic culture. The maximum organic Se in biomass was 154.00 μg/g DW. These findings lay the groundwork for understanding heterotrophic microalgal production of Se-containing nutraceuticals, offering valuable insights into Se tolerance, growth dynamics, and metabolic responses in Chlorella vulgaris K-01.

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Selenium-enriched peptides identified from selenium-enriched soybean protein hydrolysate: protective effects against heat damage in Caco-2 cells

Abstract: Our previous study evaluated the antioxidant and anti-inflammatory activities of selenium-enriched soybean peptides (SePPs) in vivo. In this study, we purified SePPs via gel filtration chromatography and obtained five fractions...

Cited by 9 publications

References 55 publications

Statistical Characterization of Food-Derived α-Amylase Inhibitory Peptides: Computer Simulation and Partial Least Squares Regression Analysis

Statistical Characterization of Food-Derived α-Amylase Inhibitory Peptides: Computer Simulation and Partial Least Squares Regression Analysis

Evaluating the capability of soybean peptides as calcium ion carriers: a study through sequence analysis and molecular dynamics simulations

Heterotrophic Selenium Incorporation into Chlorella vulgaris K-01: Selenium Tolerance, Assimilation, and Removal through Microalgal Cells

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