Formation of advanced glycation end products in glucose-amino acid models of Maillard reaction under dry- and wet-heating conditions.

BACKGROUND: Advanced glycation end products (AGEs) are compounds formed by non-enzymatic processes in the Maillard reaction and can cause various chronic diseases. This study explores the AGE formation process in a glucose-amino acid system under both wet- and dry-heating conditions, and analyzes the effect of cysteine in AGE formation. RESULTS: Under wet-heating conditions, Nε-carboxymethyllysine (CML) and Nε-carboxyethyllysine (CEL) concentrations rose for the initial 90 min and subsequently declined after 120 min; after 90 min of heating, the maximum yields in the absence of cysteine were 1151.04 ± 14.01 and 3386.90 ± 26.55 ng mL-1, respectively. The concentration of pyrraline (Pyr) increased after 30 min and then decreased after 60 min with a maximum yield of 777.68 ± 23.36 ng mL-1. However, in dry-heating models, the AGE concentrations consistently increased with increasing heating time; the maximum yields for CML, CEL and Pyr were 468.66 ± 10.96, 1993.57 ± 14.81 and 1085.74 ± 58.06 ng mL-1, respectively. The addition of cysteine showed an inhibitory effect on AGE formation, especially for Pyr in the dry-heating model, with inhibition rates ranging from 17.14% to 95.60%. CONCLUSION: Although wet-heating models produced more CML and CEL, they produced less Pyr than dry-heating models. The AGE formation in wet-heating models positively correlated with the reaction rate; however, the dry-heating reaction demonstrated a more complex relationship between reaction rate and reaction protocol. Moreover, cysteine exhibited a significant inhibitory effect on AGE production, and the degree of inhibition was proportional to the cysteine concentration. This study provides important insights into the mechanisms for AGE formation under various heating conditions, such as those representing baking (dry-heating) and steaming conditions (wet-heating). © 2024 Society of Chemical Industry.

Preparation, characterization and functional evaluation of soy protein isolate-peach gum conjugates prepared by wet heating Maillard reaction.

This study was conducted to formulate a conjugate of soy protein isolate (SPI) and peach gum (PG) with improved functional properties, interacting at mass ratios of 1:1, 1:2, 1:3, 2:1, and 2:3 by Maillard reaction via wet heating method. Conjugation efficiency was confirmed by grafting degree (DG) and browning index (BI). Results indicated that DG increased with increasing concentration of PG, and decreased with increasing pH, whereas no remarkable change was observed with increasing reaction time. The conjugates were optimized at a ratio of 1:3. SDS-PAGE confirmed conjugate formation, Fourier transform infrared spectroscopy (FTIR) and circular dichroism (CD) verified conjugate secondary structural changes, and scanning electron microscopy (SEM) indicated significant overall structural changes. The functional properties, solubility, emulsifying stability, water holding, foaming, and antioxidant activity were significantly improved. This study revealed the wet heating method as an effective approach to improve the functional properties of soy protein.

Structural and functional properties of whey protein isolate-inulin conjugates prepared with ultrasound or wet heating method.

BACKGROUND: Whey protein isolate (WPI) generally represents poor functional properties such as thermal stability, emulsifying activity and antioxidant activity near its isoelectric point or high temperatures, which limit its application in the food industry. The preparation of WPI-polysaccharide covalent conjugates based on Maillard reaction is a promising method to improve the physical and chemical stability and functional properties of WPI. In this research, WPI-inulin conjugates were prepared through wet heating method and ultrasound method and their structural and functional properties were examined. RESULTS: In conjugates, the free amino acid content was reduced, the high molecular bands were emerged at sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), new C-N bonds were formed in Fourier-transform infrared (FTIR) spectroscopy, and fluorescence intensity was reduced compared with WPI. Furthermore, the result of circular dichroism (CD) spectroscopy also showed that the secondary structure of conjugates was changed. Conjugates with ultrasound treatment had better structural properties compared with those prepared by wet heating treatment. The functional properties such as thermal stability, emulsifying activity index (EAI), emulsion stability (ES) and antioxidant activity of conjugates with wet heating treatment were significantly improved compared with WPI. The EAI and ES of conjugates with ultrasound treatment were the highest, but the thermal stability and antioxidant activity were only close to that of the conjugates with wet heating treatment for 2 h. CONCLUSION: This study revealed that WPI-inulin conjugates prepared with ultrasound or wet heating method not only changed the structural characteristics of WPI but also could promote its functional properties including thermal stability, EAI, ES and antioxidant activity. © 2024 Society of Chemical Industry.

Protein interactions during dry and wet heat pre-treatment of skim milk powder (dispersions) and their effect on the heat stability of recombined filled evaporated milk.

Skim milk powder (SMP) as well as aqueous dispersions were subjected to dry and wet heat pre-treatment, respectively, to improve the heat stability of recombined filled evaporated milk (RFEM) derived therefrom. However, microrheological analysis revealed that prolonged incubation caused detrimental effects on the heat stability of RFEM, which were thought to be due to protein interactions. SDS-PAGE results indicated that protein aggregation via non-disulfide covalent bonds occurred upon long-time dry or wet heat incubation. This was probably related to some Maillard reaction products, which is sustained by the increase in lactulose and protein carbonyl content. Considerable protein aggregation via disulfide bonds in the serum was found upon wet heat incubation at temperatures of at least 80 °C. Principal component analysis (PCA) revealed that the negative effects of overprocessing on the heat stability of RFEM were predominantly related to protein cross-linking via non-disulfide covalent bonds related to protein carbonylation.

Pea protein isolate-inulin conjugates prepared by pH-shift treatment and ultrasonic-enhanced glycosylation: Structural and functional properties.

The application of pea proteins in the food industry is often limited by their poor functional properties, such as solubility, emulsification, and gelation. To address this problem, a novel method of constructing pea protein-inulin conjugates with improved functional attributes was developed, which consisted of combining a high-intensity ultrasonic treatment with a pH-shift wet heating method. This combined method promoted the Maillard reaction, leading to a grafting degree that was 2.3-times higher than that of the traditional wet heating method. SDS-PAGE confirmed the formation of pea protein-inulin conjugates. The pea protein-inulin conjugates had higher solubility than pea proteins alone, especially around the isoelectric point of the protein. Furthermore, the thermal stability, antioxidant activity, foaming and emulsifying properties of the conjugates were better than those of the protein. This study shows that the combined ultrasound/pH-shift wet heating method is highly effective at improving the functional properties of pea proteins.

Comparison of dry- and wet-heat induced changes in physicochemical properties of whey protein in absence or presence of inulin.

Changes in whey protein (10%, w/v) induced by dry-heating (60 °C for 5 days at a relative humidity of 63%), wet-heating (85 °C for 30 min) or the two-combined heating in absence or presence of inulin (8%, w/v) were studied. Mixture of whey protein and inulin showed significantly higher absorbance at 290 nm than whey protein alone in all heating conditions while only dry-heated samples showed significantly increased absorbance value at 420 nm (p < 0.05). Whey protein after heating showed significantly lower zeta potential and inulin decreased the value of all heated samples further (p < 0.05) except for samples after dry-heating. Heating decreased the free sulfhydryl group content of whey protein samples while presence of inulin decreased further (p < 0.05). Dry-heating decreased while wet-heating increased the surface hydrophobicity of whey protein. Inulin had no effect on the surface hydrophobicity of heated whey protein under dry-heating but decreased under wet-heating.

Interfacial and enhanced emulsifying behavior of phosphorylated ovalbumin.

Improvement of emulsifying properties by phosphorylation could have a wide potential application in food industry. In this study, ovalbumin (OVA) was phosphorylated under wet-heating in the presence of sodium tripolyphosphate. Phosphorylated OVA (P-OVA) with low, middle, high phosphorus content were obtained with reaction time increased. Their enhanced emulsification capacity and the mechanism were investigated. Compared with native OVA (N-OVA), the emulsifying activity and stability of P-OVA were increased by 26% and 109% (P < 0.05), respectively. The structure studies (Fourier transform infrared spectroscopy, circular dichroism spectra, scanning electron microscope) demonstrated that introduction of phosphate groups to OVA increased the molecular flexibility of P-OVA. The absolute values of surface zeta-potential and surface hydrophobicity were increased as the phosphorus content increased, which indicated that the phosphate group inhibited protein aggregation. And it caused a large amount absorption of protein on the surface of the oil droplets, which ultimately improved the emulsion stability. Both particle size and microscopic results of emulsion showed that the particle size of OVA reduced as the degree of phosphorylation increased, which improved the emulsifying ability.

Effect of glycosylation with gum Arabic by Maillard reaction in a liquid system on the emulsifying properties of canola protein isolate.

In this research, the improvement of emulsifying properties of chemically modified canola protein isolate (CPI) with gum Arabic (GA) through Maillard reaction under natural pH at 90°C was investigated. The stability, rheology and morphology of oil-in-water emulsions stabilized by conjugate of two biopolymers were evaluated by determination of droplet size, emulsifying activity (EAI), emulsifying stability (ESI) and creaming indices. The conjugate-stabilized emulsion showed smaller mean droplet size and lower creaming index values which were more effective to stabilize the emulsion compared to CPI and mixture of two biopolymers especially if pH was near the isoelectric point of CPI or when emulsions heated from 30 to 90°C. Moreover, our results demonstrated that EAI, ESI and viscosity of emulsion for CPI-GA conjugate were significantly more than those of CPI-GA mixture and CPI. These results suggested that Maillard reaction could be one of the most promising approaches to improve emulsifying properties of CPI for food applications.

Improving the emulsifying properties of ß-lactoglobulin-wild almond gum (Amygdalus scoparia Spach) exudate complexes by heat.

BACKGROUND: The present study aims to investigate the advantageous effects of wet heating, BLG (ß-lactoglobulin)/Ang (Angum gum) ratio, and pH (normal pH of mixed BLG and Ang solutions, pHc > pH > pHΦ1 ) on the emulsifying properties of wet-heated ß-lactoglobulin-wild almond gum exudate (Amygdalus scoparia Spach) mixture over those of electrostatic counterparts. RESULTS: Covalent linkage of BLG-Ang conjugates was confirmed by SDS-PAGE and FTIR analysis. Emulsion activity (EA), emulsion stability (ES), and droplet size characteristics of emulsions were significantly (P < 0.05 and P < 0.01) affected by electrostatic/wet-heating, biopolymer ratio, pH, and their interactions. The electrostatic complexes with pHc > pH > pHΦ1 exhibited higher EA and ES values for all the biopolymer ratios investigated than their electrostatic counterparts with pH after mixing. However, these values for the wet-heated samples at pH after mixing were found to be higher than those of the samples subjected to heat treatment at pHc > pH > pHΦ1 . Based on the results obtained, it was concluded that E/1:2/3.80 and W/1:2/6.69 were the two complexes with finer droplet size distributions after preparation (26.72 ± 3.71 and 15.27 ± 1.01 µm, respectively) and after one week of storage at 4 °C (30.71 ± 1.57 and 28.79 ± 0.56 µm, respectively) than others. Apparent viscosities of electrostatic and wet-heated complexes and emulsions made with the complexes were measured. CONCLUSION: Protein-polysaccharide interactions can be used as an efficient way for producing novel emulsifiers/stabilisers after heat treatment. © 2016 Society of Chemical Industry.

Effect of ultrasound treatment on the wet heating Maillard reaction between mung bean [Vigna radiate (L.)] protein isolates and glucose and on structural and physico-chemical properties of conjugates.

BACKGROUND: The objective of this study was to determine the effect of ultrasound treatment on the wet heating Maillard reaction between mung bean protein isolates (MBPIs) and glucose, and on structural and physico-chemical properties of the conjugates. RESULTS: The degree of glycosylation of MBPI-glucose conjugates treated by ultrasound treatment and wet heating (MBPI-GUH) was higher than that of MBPI-glucose conjugates only treated by wet heating (MBPI-GH). Solubility, emulsification activity, emulsification stability and surface hydrophobicity of MBPI-GUH were higher than that of MBPI-GH. Grafted MBPIs had a lower content of α-helix and unordered coil, but a higher content of ß-sheet and ß-turn structure than MBPIs. No significant structural changes were observed in ß-turn and random coil structure of MBPI-GUH, while α-helix content increased with ultrasonic time, and decreased at 300 W ultrasonic power with the increase of ß-sheet. MBPI-GUH had a less compact tertiary structure compared to MBPI-GH and MBPI. Grafting MBPIs with glucose formed conjugates of higher molecular weight, while no significant changes were observed in electrophoresis profiles of MBPI-GUH. CONCLUSION: Ultrasound-assisted wet heating Maillard reaction between MBPIs and glucose could be a promising way to improve functional properties of MBPIs.