Maillard Reaction Process and Characteristic Volatile Compounds Formed During Secondary Thermal Degradation Monitored via the Change of Fluorescent Compounds in the Reaction of Xylose-Corn Protein Hydrolysate.

Until now, no effective method has been found to monitor the Maillard reaction process for complex protein hydrolysates. Dynamic changes in the concentration of α-dicarbonyl compounds, fluorescence intensity, and browning degree were investigated during the Maillard reaction of corn protein hydrolysates. When the fluorescence intensity reached the peak, deoxyosones would continue to be increased by ARP's degradation. However, the reaction node with the highest fluorescence intensity coincided with the turning point of the browning reaction, and the subsequent browning rate remarkably increased. Therefore, the change in fluorescence intensity could be used to monitor the degradation of ARP and the formation of browning melanoidin at different stages of the Maillard reaction of complex systems, thus effectively indicating the process of the Maillard reaction. When Maillard reaction intermediates (MRIs) with maximum fluorescent compounds were heated, the most abundant pyrazines were subsequently achieved. However, furan compounds would be progressively increased during the thermal process of MRIs with continuously enhanced browning.

Light-Colored Maillard Peptides: Formation from Reduced Fluorescent Precursors of Browning and Enhancement of Saltiness Perception.

The browning formation and taste enhancement of peptides derived from soybean, peanut, and corn were studied in the light-colored Maillard reaction compared with the deep-colored reaction. The fluorescent compounds, as the browning precursors, were accumulated during the early Maillard reaction of peptides and subsequently degraded into dark substances, which resulted in a higher browning degree of deep-colored Maillard peptides (MPs), especially for the MPs derived from corn peptide. However, the addition of l-cysteine in light-colored Maillard reaction reduced the formation of deoxyosones and short-chain reactive α-dicarbonyls, thereby weakening the generation of fluorescent compounds and inhibited the browning of MPs. Synchronously, the peptides were thermally degraded into small peptides and amino acids, which were consumed less during light-colored thermal reaction due to its shorter reaction time at high temperature compared with deep-colored ones, thus contributing to a stronger saltiness perception of light-colored MPs than deep-colored MPs. Besides, the Maillard reaction products derived from soybean and peanut peptides possessed an obvious "kokumi" taste, making them suitable for enhancing the soup flavors.

Formation of Fluorescent Maillard Reaction Intermediates of Peptide and Glucose during Thermal Reaction and Its Mechanism.

The dynamic changes in fluorescence intensity of the Maillard reactions of l-alanyl-l-glutamine (Ala-Gln)/Diglycine (Gly-Gly)/glycyl-l-glutamine (Gly-Gln) and glucose were investigated. It was found that the fluorescence intensity would increase with the reaction time; however, it would decrease after longer heating at higher temperatures, which was accompanied by rapid browning. The strongest intensity occurred at 45, 35, and 35 min at 130 °C for Ala-Gln, Gly-Gly, and Gly-Gln systems, respectively. The simple model reactions of Ala-Gln/Gly-Gly and dicarbonyl compounds were selected to reveal the formation and mechanism of fluorescent Maillard compounds. It was confirmed that both GO and MGO could react with peptides to form fluorescent compounds, especially GO, and this reaction was sensitive to temperature. The mechanism was also verified in the complex Maillard reaction of pea protein enzymatic hydrolysates.

Preparation of Saltiness-Enhancing Enzymatic Hydrolyzed Pea Protein and Identification of the Functional Small Peptides of Salt Reduction.

According to the correlation of saltiness determined by electronic tongue and perceived NaCl concentration, favorable enzymatic hydrolysis parameters were achieved to prepare the saltiness enhancing mixture peptides from pea protein. Six peptide fractions (F1, F2, F3, F4, F5, and F6) were isolated using Sephadex G-10 gel filtration. Among them, fraction F4 (0.1%) exhibited the highest saltiness (5.90 ± 0.03). The amino acid sequences of five main peptides identified by time-of-flight mass spectrometry were Tyr-Trp (367.40 Da), Gly-Glu-His-Glu (470.43 Da), Glu-Arg-Phe-Gly-Pro (604.65 Da), Gly-Ala-Gly-Lys (331.37 Da), and Pro-Gly-Ala-Gly-Asn (414.41 Da). Tyr-Trp (0.01%) in 0.4% NaCl solution had a 20% saltiness-enhancement compared with 0.4% NaCl solution. More salivary aldosterone was secreted after tasting hydrolysate or Tyr-Trp solutions via enzyme-linked immunosorbent assay, reflecting the improvement of human sensitivity to saltiness. Thereby, the saltiness-enhancing effect was confirmed for the small peptides from hydrolyzed pea protein and the main contributor was further identified.

Simultaneously Enhanced Formation of Pyrazines and Furans during Thermal Degradation of the Glycyl-l-glutamine Amadori Compound by Selected Exogenous Amino Acids and Appropriate Elevated Temperatures.

The Amadori compound of glucose and glycyl-l-glutamine (Gly-Gln-ARP) was prepared and characterized by UPLC-MS/MS and NMR. Gly-Gln-ARP could be thermally degraded into Gly-Gln and other secondary reaction products like glycyl-l-glutamic acid and its ARP via deamidation. The thermal processing temperature exerted a tremendous influence on the flavor formation of ARP. Furans were mainly formed at 100 °C, while an elevated temperature of 120 °C facilitated the massive accumulation of α-dicarbonyl compounds through the retro-aldolization of deoxyglucosone, and then increased the formation of pyrazines. The extra-added amino acids further promoted the formation of pyrazines at 120 °C, especially Glu, Lys, and His, further increasing the total concentration of pyrazines to 457 ± 6.26, 563 ± 65.5, and 411 ± 59.2 µg/L, respectively, exceeding the pure heated control at 140 °C (296 ± 6.67 µg/L). The total concentration of furans was enhanced to (20.7 × 103) ± 8.17 µg/L by extra-added Gln. Different increasing effects were observed on the type and flavor intensity of formed pyrazines and furans from different extra-added amino acids.

Controlled Selective Formation of Amadori Compounds from α/ε Mono- or Di-glycation of Lysine with Xylose.

Three Amadori rearrangement products (Xyl-α-Lys-ARP, Xyl-ε-Lys-ARP, and diXyl-α,ε-Lys-ARP) were observed in the xylose-lysine (Xyl-Lys) Maillard reaction model. They were separated and characterized by liquid chromatography with tandem mass spectrometry and NMR. The crucial roles of reaction temperature, pH, molar ratio of Xyl to Lys, and reaction time in the formation of different Xyl-Lys-ARPs were investigated. The proportion of Xyl-α-Lys-ARP among all Xyl-Lys-ARPs was increased to 48.41% (its concentration was 25.31 µmol/mL) after the reaction at pH = 5.5 and a molar ratio of 3:1 (Xyl: Lys) for 9 min, while only Xyl-ε-Lys-ARP was generated at a higher pH (7.5) and a lower molar ratio of 1:5. Moreover, the much higher activation energy (84.08 kJ/mol) of diXyl-α,ε-Lys-ARP than Xyl-α-Lys-ARP (34.19 kJ/mol) and Xyl-ε-Lys-ARP (32.32 kJ/mol) indicated a pronounced promoting effect on diXyl-α,ε-Lys-ARP formation by high temperatures. A complete conversion from Xyl-α-Lys-ARP and Xyl-ε-Lys-ARP to diXyl-α,ε-Lys-ARP was achieved through the reaction time prolongation and Xyl concentration increase at a higher temperature; the concentration of diXyl-α,ε-Lys-ARP was 39.05 µmol/mL at a molar ratio of 5:1 for 40 min. Accordingly, the selective preparation of Xyl-α-Lys-ARP, Xyl-ε-Lys-ARP, and diXyl-α,ε-Lys-ARP could be achieved through adjusting the Xyl-Lys ratio, pH, and reaction time.

Cysteine-Induced pH-Dependent Formation of Thiols and Sulfides or 2-Acetylthiazole and Pyrazines during Thermal Treatment of N-(1-Deoxy-d-xylulos-1-yl)-alanine.

The influence of pH was studied on volatile flavor formation during thermal treatment of an Amadori rearrangement product (ARP) with or without the addition of cysteine (Cys). The formation of thiols and sulfides or 2-acetylthiazole and pyrazines induced by Cys during thermal degradation of ARP was pH-dependent. At low pH levels, the hydrolysis of Cys to hydrogen sulfide (H2S) was promoted, giving rise to the increase of thiols and sulfides with an obvious meaty aroma. However, alkaline conditions were beneficial for enhancing the cyclization or transformation of imine to the enol structure, which strengthened the formation of 2-acetylthiazole and pyrazines with a roasted and nutty aroma. The imine was derived from the nucleophilic addition of Cys and methylglyoxal (MGO) and subsequent decarboxylation. At pH 8, Cys-induced variation of the flavor profile was weakened during thermal degradation of ARP. Accordingly, the combinational effect of pH and added Cys could be beneficial for achieving the desirable flavors during thermal processing of ARP.