Evaluation of pH‐treated fish sarcoplasmic proteins on rheological properties of fish myofibrillar protein mediated by microbial transglutaminase

Fish sarcoplasmic protein (SP) could be exploited in the water‐holding agent for fish protein gels, except that the gel strength is reduced. The adjustment of pH could modify protein interactions to overcome the inferior effect. Fish SP solutions were adjusted to pH 3 or 12, neutralised to pH 7 and lyophilised to be pH‐treated SPs. These SPs along with lyophilised untreated SP (Normal SP) were incorporated into fish myofibrillar protein (MP) with microbial transglutaminase (MTG). The denaturation temperature (T_d) of MP mixed with normal SP was 66 °C with the lowest shear stress value. The denaturation of MP mixed with pH‐treated SP reduced to be 57 °C, resulting in increased shear stress. The cooking loss of MP gel was reduced by adding pH‐treated SPs, while the breaking forces were similar to control. The result indicated that pH‐treated SPs could be used to reduce cooking loss of MTG‐mediated MP gels without affecting the gelling properties.     

The influence of additives on properties of heat‐induced gels from salt‐soluble proteins extracted from goose

Calcium chloride (CaCl₂) and phosphates are important additives to improve product quality during meat processing. Response surface methodology was used to study the influence of CaCl₂ and phosphates on the hardness, water‐holding capacity (WHC) and ultra‐structure of salt‐soluble goose meat protein gels. The results show that the hardness and WHC of salt‐soluble protein gels increased significantly when CaCl₂ concentration was increased and phosphates were added. Scanning electron microscopy showed that tetrasodium pyrophosphate (TSPP) and sodium tripolyphosphate (STPP) had a greater impact on the cross‐linking and pore diameter of the gel networks than sodium hexametaphosphate (SHMP). At the 0.02 m and 4:3:2 of CaCl₂ concentration and the ratio of TSPP, SHMP and STPP, hardness and WHC values were 114.55 gf and 96.65%, which corresponded to the prediction value of our model. Further results showed that the hardness and WHC of gels reached the maximum with 0.3% of phosphates levels.     

Evaluation of the peptide profile with a view to authenticating buffalo mozzarella cheese

Electrophoretic and chromatographic techniques were used to determine water‐soluble peptide profiles aiming to identify the adulteration of buffalo milk mozzarella cheese by the addition of cow's milk. Thus, cheeses were produced with contents of cow's milk varying from 0% to 100%, and the peptides extracted after production and after 20 days of refrigeration. Polyacrylamide gel electrophoresis under denaturing conditions in the presence of sodium dodecyl sulphate (SDS‐PAGE) identified a potential peptide marker of exclusively bovine origin with a size of about 21 kDa for the addition of cow's milk above 30%. Reverse‐phase high‐performance liquid chromatography (RP‐HPLC) indicated the existence of two potential peptides present in higher concentrations in buffalo milk and one exclusive for cow's milk, the latter making it possible to estimate the addition of cow's milk to buffalo milk. Six commercial brands of buffalo mozzarella cheese were evaluated, and indications of adulteration found in four of them.     

Gb3 Glycosphingolipids with Fluorescent Oligoene Fatty Acids: Synthesis and Phase Behavior in Model Membranes

Glycosphingolipids are involved in a number of physiological and pathophysiological processes, and they serve as receptors for a variety of bacterial toxins and viruses. To investigate their function in lipid membranes, fluorescently labeled glycosphingolipids are highly desirable. Herein, a synthetic route to access Gb₃ glycosphingolipids with fluorescently labeled fatty acids, consisting of pentaene and hexaene moieties either at the terminus or in the middle of the acyl chain, has been developed. The fluorescent properties of the Gb₃ derivatives were investigated in small unilamellar vesicles composed of a raft-like mixture. Phase-separated giant unilamellar vesicles (GUVs) allowed the quantification of the apparent partitioning coefficients of the Gb₃ compounds by means of confocal fluorescence laser scanning microscopy. The determined partition coefficients demonstrate that the Gb₃ derivatives are preferentially localized in the liquid-disordered (l_d) phase. To analyze whether the compounds behave like their physiological counterparts, Cy3-labeled (Cy: cyanine) Shiga toxin B subunits (STxB) were specifically bound to Gb₃-doped GUVs. However, the protein was favorably localized in the l_d phase, in contrast to results reported for STxB bound to naturally occurring Gb₃, which is discussed in terms of the packing density of the lipids in the liquid-ordered (l_o) phase.     

Antisolvent micronization of BSA using supercritical mixtures carbon dioxide + organic solvent

In this work, expanded liquid antisolvent (ELAS) process has been used to micronize bovine serum albumin (BSA) solubilized in water. Carbon dioxide mixtures with ethanol, acetone or isopropyl alcohol, at expanded liquid conditions, have been used as the antisolvent. The effect of process parameters, such as the kind of co-antisolvent and the organic co-antisolvent/water/carbon dioxide mole fraction on the morphology and dimensions of the precipitates, was studied. Changing co-antisolvent and operating conditions, we obtained nanoparticles (with a mean diameter of about 60 nm ± 10 nm), sub-microparticles (with a mean diameter of 470 nm ± 130 nm), microparticles (with a mean diameter of 0.93 μm ± 0.37 μm) and expanded microparticles with an empty core (with a mean diameter of about 9 μm ± 5 μm). Fourier transform infrared analysis on BSA powders revealed that, using acetone as co-antisolvent, no modifications of the protein secondary structure were induced by ELAS processing.     

Enzymatic modifications of pea protein and its application in protein-cassava and corn starch gels

The interactions between starch and proteins during processing influence pasting and rheological properties of starch and produce modifications on starch gel structure. Enzymatic modifications have been proposed for overcoming the limitations of using proteins as food ingredients. This work aimed to study the impact of native and enzymatically modified pea proteins on the properties of protein-starch (from cassava or corn) gels. Pea protein isolate (PPI) was incubated with endopeptidase (AL) or microbial transglutaminase (TG). Pasting profile, rheological behaviour and water retention capacity of protein-starch gels were analyzed. Protein (native and enzymatically modified) incorporation increased the viscosity of both corn and cassava starches during gel preparation. However, the hydrolyzed protein reduced drastically the increment of viscosity of protein-starch gels. The addition of PPI led to corn starch network that shifted from an elastic-like nature to a more viscous-like, whereas the opposite effect was observed in cassava gel network. TG- and AL-treated proteins led to a decrease of both G′ and G″ moduli of protein-starch gels, and AL-treated proteins showed the highest decrease on these parameters. Hydrolyzed proteins also favoured the syneresis of the protein-corn starch gel, whereas crosslinked proteins tended to reduce it. Enzymatic modifications of pea proteins affected significantly pasting and rheological properties of protein-starch gels.     

Composition and Structure of the Bovine Milk Fat Globule Membrane—Some Nutritional and Technological Implications

Milk fat is dispersed in milk as small, spherical globules, stabilized in the form of emulsion by its surrounding membrane. This membrane, called the milk fat globule membrane (MFGM), is created in the secretory cells of the mammary gland, and represents an ordered and unique biophysical system. This review characterizes the main milk fat globule components, their structure, and intracellular origin. The milk fat globule membrane has many potentially bioactive components. These are discussed in terms of their health effects for the native and processed globules. Because of their functional and nutritional properties, MFGM components can be used as valuable ingredients in the manufacture of new functional foods.     

Design of whey protein nanostructures for incorporation and release of nutraceutical compounds in food

Whey proteins are widely used as nutritional and functional ingredients in formulated foods because they are relatively inexpensive, generally recognized as safe (GRAS) ingredient, and possess important biological, physical, and chemical functionalities. Denaturation and aggregation behavior of these proteins is of particular relevance toward manufacture of novel nanostructures with a number of potential uses. When these processes are properly engineered and controlled, whey proteins may be formed into nanohydrogels, nanofibrils, or nanotubes and be used as carrier of bioactive compounds. This review intends to discuss the latest understandings of nanoscale phenomena of whey protein denaturation and aggregation that may contribute for the design of protein nanostructures. Whey protein aggregation and gelation pathways under different processing and environmental conditions such as microwave heating, high voltage, and moderate electrical fields, high pressure, temperature, pH, and ionic strength were critically assessed. Moreover, several potential applications of nanohydrogels, nanofibrils, and nanotubes for controlled release of nutraceutical compounds (e.g. probiotics, vitamins, antioxidants, and peptides) were also included. Controlling the size of protein networks at nanoscale through application of different processing and environmental conditions can open perspectives for development of nanostructures with new or improved functionalities for incorporation and release of nutraceuticals in food matrices.