Water distribution and moisture-absorption in egg-white derived peptides: Effects on their physicochemical, conformational, thermostable, and self-assembled properties.

Three egg-white derived peptides (DHTKE, MPDAHL, and FFGFN) were characterized with hydrophilia and water distributions. The effect of moisture exposure on their properties at 75% relative humidity for 30 h were further investigated. LF-NMR tests revealed that strong bound-water (relaxation time < 10 ms) accounted for more than 80% of total water in peptides after moisture-absorption. The absorbed water led to the pH of three peptides increase, antioxidant activities in vitro decrease, and diverse changes in their functional group vibrations, molecular hydrophobicity, and phase transformation properties. Compared to dried samples, the hydrated-DHTKE was pyrolyzed and hydrated-MPDAHL was oxidized over 160 °C, while the glass transition, melting, and crosslink temperatures of FFGFN all decreased after moisture-absorption. Moreover, the results indicated that moisture-absorption in FFGFN powder enhanced the surface-hydrophobicity of FFGFN-hydrogel and accelerated its self-organizations. This study provides a comprehensive understanding of moisture-absorption effects on peptides, with these changes potentially impacting storage recommendations and scientific interpretations.

Skimmed milk structural dynamics during high hydrostatic pressure processing from in situ SAXS.

Understanding the changes in milk at a nanostructural level during high-pressure (HP) treatment can provide new insights to improve the safety and functionality of dairy products. In this study, modifications of milk nanostructure during HP were studied in situ by small-angle X-ray scattering (SAXS). Skimmed milk was pressurized to 200 or 400 MPa at 25, 40 or 60 °C and held for 5 or 10 min, and the effect of single- and double-HP treatment was also investigated. In most cases, the SAXS patterns of skimmed milk are well fitted with a three-population model: a low-q micellar feature reflecting the overall micelle size (~0.002 Å-1), a small casein cluster contribution at intermediate-q (around 0.01 Å-1) and a high-q (0.08-0.1 Å-1) population of milk protein inhomogeneities. However, at 60 °C a scattering feature of colloidal calcium phosphate (CCP) which is normally only seen with neutron scattering, was observed at 0.035 Å-1. By varying the pressure, temperature, holding and depressurization times, as well as performing cycled pressure treatment, we followed the dynamic structural changes in the skimmed milk protein structure at different length scales, which depending on the processing conditions, were irreversible or reversible within the timescales investigated. Pressure and temperature of the HP process have major effects, not only on size of casein micelles, but also on "protein inhomogeneities" within their internal structure. Under HP, increasing processing time at 200 MPa induced re-association of the micelles, however, the changes in the internal structure were more pressure-dependent than time dependent.

Moisture-Absorption and Water Dynamics in the Powder of Egg Albumen Peptide, Met-Pro-Asp-Ala-His-Leu.

Moisture absorbed into the powder of Met-Pro-Asp-Ala-His-Leu (MPDAHL)-a novel egg albumen antioxidant peptide-profoundly affects its properties. In this study, we elucidated water dynamics in MPDAHL using DVS, DSC, and low-field 1 H NMR. Based on the DVS data, we found that MPDAHL sorption kinetics obey a parallel exponential model. DSC results indicated that both water and heating could change the microstructure of MPDAHL. The T2 parameters of NMR reflected the different phases of moisture absorption revealed that there were 4 categories of water with different states or mobility in the MPDAHL during the moisture absorption process. The fastest fraction T2b mainly dominated the hygroscopicity of MPDAHL and the absorbed water significantly changed the proton distribution and structure of MPDAHL. Thus, this study shows that DVS, DSC, and low-field 1 H NMR are effective methods for monitoring water mobility and distribution in synthetic peptides. It can be used to improve the quality assurance of functional peptides.

Water dynamics of Ser-His-Glu-Cys-Asn powder and effects of moisture absorption on its chemical properties.

BACKGROUND: This study has elucidated moisture dynamics in the soybean peptide, Ser-His-Glu-Cys-Asn (SHECN) powder by using dynamic vapor sorption (DVS) and nuclear magnetic resonance (NMR). We also tried to investigate the effects of moisture absorption on the biological activity and chemical properties of SHECN with some effective methods such as mid-infrared (MIR) spectroscopy and gas chromatography-mass spectrometry (GC-MS). RESULTS: DVS results showed that the moisture absorption of SHECN could reach a maximum of 33%, and the SHECN powder after synthesis actually existed in a trihydrate state of SHECN.3H2 O. Low-field NMR revealed that three water proportions including strong combined water, binding water and bulk water were involved in SHECN moisture absorption and absored water dominantly existed in the form of combined water. Magnetic resonance imaging (MRI) and MIR spectroscopy results indicated that moisture absorption could change the morphology and structure of SHECN. After moisture absorption at 50% and 75% relative humidity, 19 volatiles were identified by GC-MS analysis. Additionally, this study showed that a part of reductive groups in SHECN was oxidized and its antioxidant ability declined significantly (P < 0.05) after moisture absorption. CONCLUSION: Water absorbed into SHECN powder can significantly change its microstructure and cause its activity to decrease. We must prevent SHECN from absorbing moisture during storage because the water can accelerate the oxidation of samples and promote microbial reactions. © 2016 Society of Chemical Industry.

Water Dynamics in Egg White Peptide, Asp-His-Thr-Lys-Glu, Powder Monitored by Dynamic Vapor Sorption and LF-NMR.

Water absorbed into the bulk amorphous structure of peptides can have profound effects on their properties. Here, we elucidated water dynamics in Asp-His-Thr-Lys-Glu (DHTKE), an antioxidant peptide derived from egg white ovalbumin, using water dynamic vapor sorption (DVS) and low-field nuclear magnetic resonance (LF-NMR). The DVS results indicated that parallel exponential kinetics model fitted well to the data of sorption kinetics behavior of DHTKE. Four different proton fractions with different mobilities were identified based on the degree of interaction between peptide and water. The water could significantly change the proton distribution and structure of the sample. The different phases of moisture absorption were reflected in the T2 parameters. In addition, the combined water content was dominant in the hygroscopicity of DHTKE. This study provides an effective real-time monitoring method for water mobility and distribution in synthetic peptides, and this method may have applications in promoting peptide quality assurance.

Dynamics of water mobility and distribution in soybean antioxidant peptide powders monitored by LF-NMR.

In this study, we aimed to elucidate the characteristics of water mobility and distribution in soybean antioxidant peptide powders (SAPPs) using low-field nuclear magnetic resonance (LF-NMR). SAPPs of three different molecular weights (MWs) were exposed to a room temperature environment with a relative humidity of 45%, and the dynamics of water mobility and distribution were monitored by LF-NMR. Results revealed that there were four transverse relaxation time fractions in SAPPs. The major (over 90%) fraction was bound water, and the distribution of water in samples with different MWs was different. The moisture absorption capacity of SAPPs with MWs of less than 1 kDa was the strongest, and all T2 fractions/water population contents in SAPPs with MWs of 1-3 kDa were the lowest. This study provided an effective real-time monitoring method for water mobility and distribution in SAPPs and may have applications for promoting peptides quality assurance.

Analysis of DPPH inhibition and structure change of corn peptides treated by pulsed electric field technology.

In this study, the effects on antioxidant activity and structure change of corn peptides (CPS) with 10 to 30 kDa molecular weight (MW) treated by pulsed electric field (PEF) technology were investigated. 2, 2-diphenyl-1-picrylhydrazyl (DPPH) inhibition was used to evaluate the antioxidant activity of CPS. Response surface methodology (RSM) was used to investigate the effects of PEF treatment parameters on antioxidant activity of CPS. The optimal conditions were as follows: concentration of CPS 10 mg mL(-1), electric field intensity 15 kV cm(-1), and pulse frequency 2,000 Hz. Under the optimized conditions, the DPPH inhibition of CPS increased 32.1 %, compared to the sample untreated. And mid-infrared spectroscopy (MIR) was used for analyzing the structure change of CPS. The results showed that PEF technology could obviously increase the DPPH inhibition of CPS under the optimized conditions (P < 0.05).