Microbial transglutaminase (mTG) catalyses the formation of protein crosslinks, deamidating glutamine in a side-reaction. Gluten deamidation by human tissue transglutaminase is critical to activate celiac disease pathogenesis making the addition of mTG to wheat-based products controversial. The ability of mTG (0-2000 U.kg-1) to alter gluten’s structure, digestibility and the deamidation state of six immunogenic gluten peptides within bread was investigated. Gluten’s structure was altered when mTG exceeded 100 U.kg-1, determined by confocal microscopy, extractability and free sulfhydryl assays. The effect of mTG on six immunogenic peptides was investigated by in vitro digestion (INFOGEST) and mass spectrometry. The addition of mTG to bread (0-2000 U.kg-1) did not alter the deamidation state or digestibility of the immunogenic peptides investigated. Overall, this investigation indicated that the addition of mTG to bread does not create activated gluten peptides. This analysis provides evidence for risk assessments of mTG as a food processing aid.Cauliflowers are generally associated with healthy diets due to their positive impact on health. This research aims to evaluate the effects of cooking processes (boiling, steaming and microwaving) and different preparation times, on the content of carotenoids and provitamin A and tocopherols, in cauliflowers and to verify the effect of the cooking process on maintaining the coloring. The results revealed that the thermal processinfluencedthe antioxidant compounds releaseindependent of genotype. The highest content of zeaxanthin and lutein was found in ‘Verde di Macerata’ after boiling for 20 min. ‘Cheddar’ presented the highest content of all carotenoids and when steamed for 20 min, the highest levels ofprovitamin Awere observed.Microwaved and bolied ‘Grafitti’ for longer times showed the highest retention of tocopherol. The cooking did not negatively affect the visual aspect. ‘Verde di Macerata’ and ‘Cheddar’ may be good sources of carotenoids and tocopherols.In this work, zein/carboxymethyl dextrin nanoparticles were successfully fabricated at different zein to carboxymethyl dextrin (CMD) mass ratios. Zein/CMD nanoparticles with the negative charge and the smallest size (212 nm) were formed when the mass ratio of zein to CMD was 21, exhibiting improved encapsulation efficiency of curcumin (85.5%). Electrostatic interactions, hydrogen bonding and hydrophobic interactions were main driven forces for nanoparticles formulation and curcumin encapsulation. Fourier transform infrared spectroscopy determined curcumin might be partially embedded in CMD during encapsulation. The spherical structures of zein/CMD nanoparticles and curcumin-loaded zein/CMD nanoparticles were observed by transmission electron microscopy. The photothermal stability and antioxidant activity of curcumin were significantly enhanced after be loaded in zein/CMD nanoparticles. Furthermore, encapsulation of curcumin in zein/CMD nanoparticles significantly delayed the release of curcumin in simulated gastrointestinal fluids. These results indicated that zein/CMD nanoparticles could be effective encapsulating materials for bioactive compounds in food industry.To ensure emulsions to be continuously stable, the hydrolysates recovered from cod bones by papain acted as a natural surfactant to synthesize high-stability bilayer nano-emulsions. As assisted by Tween 20, the average diameter of synthesized nano-emulsion with enzymatic hydrolysate could exhibit stability between 300-400 nm under a broad range of pH (4-8), temperatures (30-90 °C) and salt concentration (25-250 mM). With the addition of the hydrolysates, the rate of increase of the TBARS value in the emulsion decreased. Moreover, the bilayer structure of the nano-emulsion was characterized under an atomic force microscopy and a cryo-scanning electron microscopy. Nano-LC-Q-TOF-MS was adopted to primarily identify peptides that contained hydrophobic and hydrophilic amino acids at the emulsion interface. Besides, the absorbed peptides on the interface of emulsion enhanced the stability of emulsion lipid oxidation.This study proposed a novel analytical method for the separation and determination of cobalamin and cobalt in kefir samples by high performance liquid chromatography-inductively coupled plasma-optical emission spectrometry (HPLC-ICP-OES) in addition to determination of cobalamin in HPLC system. Chromatographic parameters such as column type, buffer solution, mobile phase flow rate and sample injection volume were individually studied and optimized. In addition, cobalamin was simultaneously determined by high performance liquid chromatography with ultraviolet detection (HPLC-UV). this website LOD values of cobalt in cobalamin and cobalt for HPLC-ICP-OES system were calculated as 0.07 mg/kg (as Co) and 0.06 mg/kg, respectively. Recovery studies were conducted to evaluate the accuracy/applicability of the method. Recovery results for cobalt in cobalamin and cobalt detected by the HPLC-ICP-OES system were calculated in the range of 87.4-100.1 and 98.8-115.0%, respectively while recovery results for cobalamin were found to be between 89.2 and 98.3% for HPLC-UV system.Impact of malondialdehyde (MDA) and (-)-Epigallocatechin-3-gallate (EGCG) on gelling properties of myofibrillar proteins (MPs) was investigated. Addition of 6 mM MDA enhanced molecular interactions of proteins, thus the strength and elastic modulus (G’) of gel were improved. EGCG addition aggravated gel quality deterioration due to further modification of MPs induced by EGCG. Addition of 12 mM MDA jeopardized gel quality according to the increasing of strength and G’, but the decreasing of water-holding capacity (WHC), and the collapse of microstructure. Nevertheless, EGCG reacted with MDA forming EGCG-MDA adducts, hence improved gel quality, which was supported by the decreasing of strength, but the increasing of WHC, and the repaired microstructure of gel at 12 mM MDA. Addition of 24 mM MDA severely jeopardized gel quality, which became even worse due to EGCG addition. This work is helpful to understand the impact of MDA and polyphenols on the gel-forming capacity of MPs.