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Soybean protein pastes were preheated for different times (20, 25 and 30 min) with l-cysteine to improve the printability and self-gelation properties and to explore the relationship between the degree of denaturation and the feasibility of microwave 3D printing. As the pre-denaturation degree increased, ordered secondary structures in proteins gradually decreased, and tertiary structures unfolded. Soybean protein printability, moulding quality increased, and soybean protein, which is not suitable for printing in its natural state, achieved self-gelling after 3D printing. Soybean protein pastes preheated for 25 min with l-cysteine achieved a complete hollow sphere structure compared to other formulations, while pastes preheated for 30 min formed a coarser structure, and blockage occurred during printing. The covalent bond of ε- (γ-glutamine) formed by the synergistic effect of transglutaminase (TGase) and microwaves was the main force driving the gel network structure formation. The most suitable pre-denaturation degree of soybean protein was quantitatively characterized as 57 %.

Chilled surimi has become increasingly popular owing to its superior texture and freshness. In this study, changes in the microbiota and gel properties during chilled surimi storage, and the contributions of dominant bacteria to the physicochemical properties of chilled surimi were investigated. The results showed that Pseudomonas gessardii, Aeromonas media, and Acinetobacter johnsonii were the dominant bacteria during chilled surimi storage. P. gessardii was the key bacteria that degraded protein in the process of surimi spoilage, which led to high total volatile base nitrogen (TVB-N), trichloroacetic acid (TCA)-soluble peptides as well as poor gel properties. Both P. gessardii and A. media were high putrescine producers, whereas only A. media produced cadaverine. In this study, spoilage microorganisms in chilled surimi were investigated for the first time, and it was found that P. gessardii had the greatest influence on surimi quality, which provides a research basis for in-depth study on the mechanism of microbial spoilage and the preservation of chilled surimi.

The existence of microwave non-thermal effects in food processing is still debated. In this study, molecular dynamics (MD) simulations were performed to investigate the conformation, electrostatic profiles, and intramolecular hydrogen bonds (intra-HB) of glucose in aqueous solution under alternating electric fields of microwaves ranging from 0 to 109 V/m at 2.45 GHz. The results showed a field-induced threshold of 109 V/m. At the threshold, alternating microwaves reoriented the flexible moieties and thus enhanced the intra-HB. The conformational transition among gg, gt, and tg conformers at 109 V/m possibly resulted from the uneven electrostatic potential and the increased intra-HB. In practice, the maximum electric field of microwaves is several times weaker than the threshold, verifying the absence of microwave non-thermal effects for glucose molecules in food processing. This study provides a novel strategy to evaluate the potential non-thermal effects of microwaves in food processing and the related underlying food safety issues.

Contamination of rice by cadmium (Cd) is threatening a large population in China. In this study, we report that soaking rice grains in a hydrochloric acid (HCl) solution can remove Cd to a desirable extent. The results indicated that the degree of Cd removal was up to 45%∼85% at different soaking times and concentrations of HCl (0.06 M ∼ 0.18 M), which was found to be logarithmically correlated with the reaction time at the optimized liquid–solid ratio of 1:2. Three HCl concentration-dependent mathematical models were established, which revealed various optimal soaking conditions depending on the initial Cd contamination. Four Cd-contaminated rice grain samples with different degrees of contamination were then tested based on the mathematical models, and the final Cd content was reduced to an acceptable extent. Moreover, the physicochemical and food properties of rice flours and rice grains after Cd removal were evaluated to highlight their potential applications.

This work was aimed to compare the effect of microwave (MW) heating on the cathepsin L (Cat L)-induced degradation of myofibrillar protein (MP) gels with that of water bath (WB) heating. First, Cat L from silver carp was purified and determined to be 45 kDa. The gel strength of the MW-heated MP gels were significantly higher than those of the WB-heated when Cat L was added (P 0.05). The gel electrophoresis pattern and scanning electron microscopy analysis indicated that MW heating inhibited the Cat l-induced hydrolysis of MP gels. In addition, the number of sulfhydryl groups and surface hydrophobicity of MW-heated gels were lower than those of WB-heated gels when Cat L was added. These results indicated that MW heating could effectively weaken the degradation of Cat L on MP gels by manipulating disulfide bonds and hydrophobic amino acids, resulting in good gel properties and a compact protein network.

The inhibitory effects of seven polyphenols on 3-chloropropane-1,2-diol fatty acid esters (3-MCPDE) formation were investigated in palm oil models. Results showed that there was not a positive significant correlation between the free-radical scavenging activities of the tested compounds and their 3-MCPDE-formation inhibitory activities; puerarin, with weak antioxidant activity, showed the highest inhibitory capacity. Moreover, puerarin reduced the content of glycidol and glycidyl esters (GEs), two key intermediates of 3-MCPDE formation in the oil models; and a puerarin-adduct was discovered in the oil fortified with glycidol or GEs, with its structure elucidated by LC-MS/MS and comparison with newly synthesized ones. Based on its chemical structure, we proposed that puerarin, at least in part, reacted with glycidol and GEs to inhibit 3-MCPDE formation. In addition, the formed compound, puerarin-7-O-propanediol was identified in the potato chips frying system, further confirming reacting with glycidol/GEs as a key mechanism of puerarin to inhibit 3-MCPDE formation.

Radical generation in rice starch under microwave treatment as well as the related chemical bond changes were investigated by electron paramagnetic resonance (EPR) and Raman spectroscopy. Samples with water activity of 0.4 and 0.7 have been treated and analyzed. It was found that microwave power level and water content could influence the amount of radicals along with the radical components and their contribution. Raman spectra showed corresponding changes in vibrational features of chemical bonds. During storage the signal intensity started to drop after a short period of increase. Rice starch radicals were relatively stable and could exist a long time in room temperature. Through signal simulation, 3 main components were separated from the original spectra and the evolving process was investigated. The main component was the radical located on C1 position in the glucose ring.

The inhibitory effect of caffeic acid on the formation of 2-amino-1-methyl-6-phenylimidazo[4,5-b] pyridine (PhIP) was investigated in chemical model systems under microwave heating (MW). A mechanistic study was subsequently carried out to identify the inhibitory mechanism. The results showed that both for conductive heating (CV) and MW, the inhibition of PhIP increased with the concentration of caffeic acid but decreased with the prolongation of heating time. The inhibition on PhIP under MW was always higher than under CV, which were dominated by the difference in dielectric loss (e″). UPLC-MS analysis showed that caffeic acid releases a CO2 molecule to produce 4-vinylcatechol which can form adducts with phenylacetaldehyde, thus reducing its availability for PhIP formation. The structure of adduct was characterized as 3-(3,4-dihydroxyphenyl)-2-phenylbutanal with a molecular weight of 256. The findings indicate that trapping of phenylacetaldehyde by 4-vinylcatechol is a key mechanism of caffeic acid in inhibiting PhIP formation.

Microwave (MW) heating improved the activity of transglutaminase (TGase) by inducing conformational changes due to structural modification. However, when TGase and myofibrillar protein were heated, the solubility and degree of crosslinking were similar. Further, the gel properties of the mixed solution pre-gelled by MW heating were lower than that obtained with water bath (WB) pre-gelling. We compared the effects on myofibrillar proteins at the same heating rate, our results showed that MW promoted aggregation, as the particle distribution tended toward larger molecular size. The increase of random coil as investigated by circular dichroism (CD) indicated that WB induced the unfolding of myofibrillar protein. MW enhanced intermolecular forces by engendering more disulfide bonds, which hindered the catalysis by TGase. Finally, SDS-PAGE indicated that the myosin molecules had more head crosslinking during MW treatment. MW and WB cause different response behaviors of myofibrillar protein, thereby affecting the catalytic effect of TGase.

Transglutaminase (TGase) was selected as model enzyme to investigate the effects of microwave (MW) heating on its activity and structure compared to water bath (WB) heating. MW heating can enhance the activity of TGase and reach the maximum at 20 min, whereas conduction heating has little effect on the activity of TGase. The difference of dielectric properties between MW heating and WB heating were not obvious, but MW heating had higher conductivity than WB heating. The results of ultraviolet and fluorescence spectra show that MW heating can change the enzyme activity by changing the conformation of TGase. The decrease of α-helix and an increase of β-sheet and β-turn investigated by circular dichroism (CD) indicated the secondary structures of TGase were changed when treated by MW heating. Further gel properties test confirmed that TGase treated by MW could improve the functional and mechanical properties of surimi gel.