Weizheng Sun

Effect of maillard reaction products derived from the hydrolysate of mechanically deboned chicken residue on the antioxidant, textural and sensory properties of Cantonese sausages.

Protein hydrolysates as precursors of Maillard reaction were obtained via enzymatic hydrolysis of mechanically deboned chicken residue (MDCR). The Maillard reaction products (MRPs) were prepared at 90 (M1), 100 (M2), 110 (M3) and 120 degrees C (M4), respectively. MRPs possessed a strong reducing power and 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging activity. According to the evolution of total free fatty acids and peroxide value of Cantonese sausage with MRPs during storage, M1 and M3 had a potent antioxidant activity (P<0.05) due to their antioxidant abilities and inhibitory action against lipolytic enzymes. Cantonese sausages treated with M1 and M2 showed good textural and sensory properties. However, M3 and M4 had a negative (P<0.05) effect on the flavour and texture of Cantonese sausages compared to control. The results suggested that M1 was very potential to be used to improve their antioxidant, textural and sensory quality.

Effect of Oxidation on the Emulsifying Properties of Myofibrillar Proteins

The aim of this work was to investigate the effect of chemical oxidation on the emulsifying properties of myofibrillar proteins. Myofibrillar proteins were oxidized by a hydroxyl radical generating system (Fenton reaction). Structural changes of oxidized or non-oxidized myofibrillar proteins were determined using surface hydrophobicity (H0) and Fourier transform infrared (FTIR) spectroscopy. The results suggested that H0 increased (p < 0.05) after treatment with oxidizing agent. Result from FTIR suggested that protein aggregation occurred and there was an increase in β-sheet structure accompanied by a decrease in turns, alpha helix, and random structures with the increase of oxidizing agent. Changes in zeta potential of the test emulsions suggested that protein oxidation could alter the electric charge of myofibrillar proteins. The analysis of the emulsions showed that protein oxidation had a negative effect on the emulsifying properties of myofibrillar proteins due to changes in electric charge, surface active properties, and protein molecular flexibility.

Effects of Microfluidization Treatment and Transglutaminase Cross-Linking on Physicochemical, Functional, and Conformational Properties of Peanut Protein Isolate

Peanut protein isolate (PPI) was treated by high-pressure microfluidization (40, 80, 120, and 160 MPa) and/or transglutaminase (TGase) cross-linking. It was found that individual microfluidization at 120 MPa was more effective in improving the solubility, emulsifying properties, and surface hydrophobicity of PPI than at other pressures (e.g., 40, 80, or 160 MPa). Individual TGase cross-linking also effectively changed the physicochemical and functional properties of PPI. Microfluidization (120 MPa) or TGase cross-linking caused the unfolding of PPI structure, resulting in the decrease of α-helix and β-turns levels and the increase of β-sheet and random coil levels, as proved by Fourier transform infrared (FTIR) and circular dichroism (CD) spectra. Compared with individual treatments, microfluidization followed by TGase cross-linking significantly (p < 0.05) improved the emulsion stability during long-term storage (20 days). Moreover, the combined treatments led to looser structure of PPI and resulted in more obvious changes in physicochemical properties.

Physicochemical changes of myofibrillar proteins during processing of Cantonese sausage in relation to their aggregation behaviour and in vitro digestibility

The physicochemical changes of myofibrillar proteins, especially oxidation behaviour, were measured to determine their mechanism of action on in vitro protein digestibility during Cantonese sausage processing. The results indicated that the carbonyl level significantly increased (p<0.05) during the process. The SH group level decreased, while S-S group level increased gradually. Protein aggregation was induced by oxidation and heat treatment. Result from Fourier transform infrared (FTIR) spectroscopy confirmed protein aggregation occurred. The analysis of in vitro digestibility showed a highly significant (p<0.05) correlation between pepsin activity and carbonyl group formation, S-S group level, protein surface hydrophobicity, D4,3. A negative and highly significant correlation between trypsin, α-chymotrypsin activity and carbonyl group formation was measured, while no significant correlation with S-S groups, protein surface hydrophobicity, D4,3 was observed. It indicated that not only protein oxidation and aggregation but also degradation by pepsin would influence proteolysis with trypsin and α-chymotrypsin.

Oxidation of sarcoplasmic proteins during processing of Cantonese sausage in relation to their aggregation behaviour and in vitro digestibility.

The physicochemical changes of sarcoplasmic proteins, especially oxidation behaviour, were measured to determine their mechanism of action on in vitro protein digestibility during Cantonese sausage processing. The results indicated that carbonyl level increased (p<0.05) during the process. The fluorescence loss of tryptophan residues was a direct consequence of the oxidative degradation. All the parameters of protein aggregation were highly (p<0.05) correlated with carbonyl level and protein surface hydrophobicity (H(0)), indicating that protein oxidation and thermal denaturation could induce protein aggregation, leading to secondary structural changes. The analysis of in vitro digestibility showed no correlation between pepsin activity and protein oxidation, due to the biphasic response of sarcoplasmic proteins toward proteolysis. However, a highly significant (p<0.05) correlation was observed with trypsin and α-chymotrypsin activity, indicating that protein oxidation induced the changes in H(0), protein aggregation and secondary structure, which further influenced in vitro digestibility.

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.

Structural Evaluation of Myofibrillar Proteins during Processing of Cantonese Sausage by Raman Spectroscopy

Structural changes of myofibrillar proteins from raw pork muscle and Cantonese sausage at different processing periods were elucidated using Raman spectroscopy. Fourier deconvolution combined with iterative curve fitting were used to analyze the amide I Raman band. Results from amide I, amide III, and C-C stretching vibrations in 890-1060 cm(-1) showed that α-helix decreased accompanied by an increase in β-sheet structure during the first 18 h, and a rebuilding process of secondary structures was observed at the rest stage due to proteolysis. The hierarchical cluster analysis results of amide I and amide III confirmed this rebuilding process. Changes in a doublet near 850 and 830 cm(-1) suggested that some tyrosine residues became buried in a more hydrophobic environment due to intermolecular interactions. Raman spectra in the 2855-2940 cm(-1) region suggested that the environment of aliphatic side chains might have been changed during the final stage and further confirmed above rebuilding process.

Binding of Aroma Compounds with Myofibrillar Proteins Modified by a Hydroxyl-Radical-Induced Oxidative System

The objective of this study was to investigate the influence of oxidation-induced structural modifications of myofibrillar protein on its binding ability with aroma compounds such as 2-methyl-butanal, methional, 2-pentanone, 2-heptanone, and nonanal. A method using solid-phase microextraction (SPME) combined with gas chromatography/mass spectrometry (GC/MS) was used to determine the corresponding binding ability. The binding with aroma compounds was found to be strongly affected by the oxidation levels of proteins, probably due to the varying modifications in protein structure and surface. Incubation with oxidants around or below 1 mM mainly caused the refolding of protein structure and accelerated the protein aggregation, which reduced the affinity of the aroma compounds, thus decreasing the binding ability. Nevertheless, treatment with oxidants over 2.5 mM would cause protein reaggregation and partial degradation, and thus, the subsequent modification of protein surface properties. The aggregated protein with wrinkled surfaces favored the hydrophobic interactions with aroma compounds, forming the protein-aroma compound complex, thus enhancing the resultant binding ability as evidenced by fluorescence quenching and SPME-GC/MS analysis.

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.

Effect of Protein Oxidation on the Conformational Properties of Peanut Protein Isolate

Peanut protein isolate (PPI) was oxidized by peroxyl radicals derived from 2,2′-azobis (2-amidinopropane) dihydrochloride (AAPH), and the conformational properties of oxidized PPI were investigated. Oxidation of PPI resulted in gradual carbonyl generation and free sulfydryl group degradation. The analysis of the maximum emission wavelength indicated change in the tertiary conformation of PPI after oxidation. Lower level oxidation could generate soluble protein aggregates with more flexible structure, while higher level oxidation would induce the formation of insoluble aggregates. Result from dynamic light scattering (DLS) and protein solubility showed that protein aggregation was correlated with protein surface hydrophobicity, indicating that protein oxidation and heat treatment could induce protein aggregation, leading to PPI conformational changes.