Chaoying Qiu

Influence of protein type on oxidation and digestibility of fish oil-in-water emulsions: gliadin, caseinate, and whey protein.

The influence of three surface-active proteins on the oxidative stability and lipase digestibility of emulsified ω-3 oils was examined: deamidated wheat gliadin (gliadin); sodium caseinate (CN); whey protein isolate (WPI). Gliadin and WPI were more effective at inhibiting lipid oxidation (hydroperoxides and TBARS) of fish oil-in-water emulsions than CN. Protein oxidation during storage was determined by measuring the loss of tryptophan fluorescence. The CN-emulsions exhibited the highest loss of tryptophan fluorescence during aging, as well as the highest amount of lipid oxidation. Potential reasons for the differences in oxidative stability of the emulsions with different proteins include differences in interfacial film thickness, protein chelating ability, and antioxidant amino acids profiles. During in vitro digestion, gliadin-stabilized emulsions had the lowest digestion rate of the three proteins. These results have important implications for using proteins to fabricate emulsion-based delivery systems for ω-3 oils.

Changes in lipid composition, fatty acid profile and lipid oxidative stability during Cantonese sausage processing

Lipid composition, fatty acid profile and lipid oxidative stability were evaluated during Cantonese sausage processing. Free fatty acids increased with concomitant decrease of phospholipids. Total content of free fatty acids at 72 h in muscle and adipose tissue was 7.341 mg/g and 3.067 mg/g, respectively. Total amount of saturated, monounsaturated and polyunsaturated fatty acids (SFA, MUFA, and PUFA) in neutral lipid exhibited a little change during processing, while the proportion of PUFA significantly decreased in the PL fraction. The main triacylglycerols were POO+SLO+OOO, PSO (P = palmitic acid, O = oleic acid, L = linoleic acid, S = stearic acid), and a preferential hydrolysis of palmitic, oleic and linoleic acid was observed. Phosphatidylcholines (PC) and phosphatidylethanolamines (PE) were the main components of phospholipids and PE exhibited the most significant degradation during processing. Thiobarbituric acid values (TBARS) increased while peroxide values and hexanal contents varied during processing.

Influence of anionic dietary fibers (xanthan gum and pectin) on oxidative stability and lipid digestibility of wheat protein-stabilized fish oil-in-water emulsion

The influence of two anionic dietary fibers (xanthan gum and pectin) on the oxidative stability and lipid digestibility of fish oil emulsions stabilized by wheat protein (gliadin) was investigated. Lipid oxidation was determined by measuring lipid hydroperoxides and TBARS of the emulsions during storage, while protein oxidation was measured using fluorescence spectroscopy. Lipid and protein oxidation was faster at pH3.5 than at pH7, which may have been due to increased iron solubility under acidic conditions. Xanthan gum inhibited lipid and protein oxidation, which was attributed to its ability to bind iron ions. Conversely, pectin promoted oxidation, which was attributed to the presence of endogenous transition metals in the polysaccharide ingredient. In vitro digestion was carried out to evaluate the digestibility of oil droplets in emulsions with or without polysaccharides. Both xanthan gum and pectin significantly increased the rate of lipid digestion, which was attributed to their ability to inhibit droplet aggregation under gastrointestinal conditions. These results have important implications for designing emulsion-based functional foods with improved oxidative stability and lipid digestibility.

Effect of citric acid deamidation on in vitro digestibility and antioxidant properties of wheat gluten.

The effects of citric acid deamidation on the physiochemical properties of wheat gluten were investigated. In vitro digestion was carried out to determine changes of molecular weight distribution, amino acids composition and antioxidant efficacy of wheat gluten hydrolysates. Results indicated that citric acid deamidation significantly increased gluten solubility and surface hydrophobicity, at a neutral pH. Deamidation induced molecular weight distribution change of gluten with little proteolysis. Results from FTIR indicated that the α-helix and β-turn of deamidated gluten increased accompanied by a decrease of the β-sheet structure. After deamidation, in vitro pepsin digestibility of wheat gluten decreased, while in vitro pancreatin digestibility increased. The oxygen radical absorbance capacity (ORAC) activity of the in vitro digests decreased with increase of deamidation time. The high Lys and total essential AAs amounts in the final digests suggested that the nutritional values of wheat gluten after deamidation might be enhanced.

Sequence, taste and umami-enhancing effect of the peptides separated from soy sauce

Five tasty peptides were separated from soy sauce, by sensory-guided fractionation, using macroporous resin, medium-pressure liquid chromatography and reverse phase-high performance liquid chromatography, and identified by ultra-performance liquid chromatography tandem mass-spectrometry as ALPEEV, LPEEV, AQALQAQA, EQQQQ and EAGIQ (which originated from glycinin A1bB2-445, glycinin A1bB2-445, cobyric acid synthase, leucine-tRNA ligase and glycoprotein glucosyltransferase, respectively). LPEEV, AQALQAQA and EQQQQ tasted umami with threshold values of 0.43, 1.25 and 0.76mmol/l, respectively. ALPEEV and EAGIQ had minimal umami taste, but ALPEEV, EAGIQ and LPEEV showed umami-enhancement with a threshold estimated at 1.52, 1.94 and 3.41mmol/l, respectively. In addition, the synthetic peptides showed much better sensory taste than mixtures of their constitutive amino acids. It indicated that peptides might play an important role in the umami taste of soy sauce.

Influence of glycosylation of deamidated wheat gliadin on its interaction mechanism with resveratrol

Gliadin is a main composition of wheat storage protein with unique characteristics. Polyphenol with health benefits tends to form complex with protein. In this study, glycosylation of deamidated wheat gliadin (gliadin) was carried out. Fluorescence quenching was applied to evaluate their binding mechanisms with resveratrol. Results showed that glycosylation could increase the solubility and decrease the surface hydrophobicity of gliadin. Both gliadin and glycosylated gliadin have strong affinity with resveratrol. The thermodynamic parameters of binding process indicated that complexation of resveratrol with gliadin was mainly driven by hydrophobic interaction, while by hydrogen bonds with glycosylated gliadin. The hydrosolubility of resveratrol was dramatically increased especially in the presence of glycosylated gliadin. This was consistent with the higher binding constant of glycosylated gliadin with resveratrol. Therefore, gliadin and glycosylated gliadin are both effective to carry resveratrol or other bioactive compounds, and their binding mechanisms are different due to structural difference.

Additional band broadening of peptides in the first size-exclusion chromatographic dimension of an automated stop-flow two-dimensional high performance liquid chromatography

The need to improve the peak capacity of liquid chromatography motivates the development of two-dimensional analysis systems. This paper presented a fully automated stop-flow two-dimensional liquid chromatography system with size exclusion chromatography followed by reversed phase liquid chromatography (SEC×RPLC) to efficiently separate peptides. The effects of different stop-flow operational parameters (stop-flow time, peak parking position, number of stop-flow periods and column temperature) on band broadening in the first dimension (1st D) SEC column were quantitatively evaluated by using commercial small proteins and peptides. Results showed that the effects of peak parking position and the number of stop-flow periods on band broadening were relatively small. Unlike stop-flow analysis of large molecules with a long running time, additional band broadening was evidently observed for small molecule analytes due to the relatively high effective diffusion coefficient (Deff). Therefore, shorter analysis time and lower 1st D column temperature were suggested for analyzing small molecules. The stop-flow two-dimensional liquid chromatography (2D-LC) system was further tested on peanut peptides and an evidently improved resolution was observed for both stop-flow heart-cutting and comprehensive 2D-LC analysis (in spite of additional band broadening in SEC). The stop-flow SEC×RPLC, especially heart-cutting analysis with shorter analysis time and higher 1st D resolution for selected fractions, offers a promising approach for efficient analysis of complex samples.

Effect of malondialdehyde modification on the binding of aroma compounds to soy protein isolates

The interactions of soy protein isolate (SPI) and flavor compounds (hexanal, trans-2-hexenal, 1-octen-3-ol, trans-2-octenal, nonanal, and trans-2-nonenal) were investigated. The influence of SPI structure modified by malondialdehyde (MDA) and flavor compound structure on the interactions were determined by using headspace solid-phase microextraction (SPME) and gas chromatography (GC) combined with mass spectrometry (MS). The binding of native SPI to the flavor compounds decreased in the order trans-2-nonenal>nonanal>trans-2-octenal>trans-2-hexenal>hexanal>1-octen-3-ol. It might be attributed to that aldehydes are more hydrophobic than alcohols. The former is more conducive to hydrophobic binding with the SPI. Furthermore, the aldehydes, in particular trans-s-undecenal, could also react covalently. The effect of MDA modification on protein-flavor interactions depended on the structure of the flavor compound. Upon low concentration of MDA (≤1mM), the binding of all six flavors to SPI increased. However, a further increase in the extent of MDA (≥2.5mM), more soluble and even insoluble aggregates formed, which reduced the binding of hexanal and nonanal to SPI. The other four flavors with double bond revealed little changes in binding (trans-2-octenal, and trans-2-nonenal) or even an increase in binding (trans-2-hexenal, and 1-octen-3-ol). The results suggested that hydrophobic interactions were weakened upon high extent of oxidation, whereas covalent interactions were enhanced.