Examination of the Causes of Instability of Soy Protein Isolate During Storage Through Probing of the Heat‐Induced Aggregation

This study investigated the mechanism of instability of soy protein isolate (SPI) as influenced by thermal aggregation during SPI preparation. Samples with different degrees of aggregation but similar protein solubility were prepared by heating native SPI (5 % w/v) at 80 or 90 °C for different times before spray‐drying. The samples were then stored at 37 °C for up to 12 weeks and analyzed periodically by atomic force microscopy, gel permeation chromatography, and SDS–PAGE. All SPI samples underwent remarkable protein solubility decreases during the first 8 weeks of storage. The rates of solubility loss were positively correlated with the amounts and/or sizes of soluble aggregates contained in the initial samples (time zero), suggesting their nucleation and activation effects. Solubility tests in SDS–urea solutions and disulfide analysis indicated that non‐covalent interactions were the main driving forces for protein storage instability. Conversely, disulfide bonds and protein carbonyls were abundant in soluble aggregates, and their content increased markedly during storage. This effect suggested that covalent linkages acted as blockers for hydrophobic aggregation.     

Thermal markers arising from changes in the protein component of milk

Classification of heat load applied to milk requires the detection of parameters appropriately related to the intensity of the heat treatment. Current analytical methods based on heat-induced changes in the protein component of milk have been directed either to determine the amount of protein-derived products arised from heat treatments or to evaluate the extent of thermal denaturation of milk proteins. Lately, a new analytical strategy has been developed according to the occurrence of three major whey proteins, namely bovine serum albumin (BSA), beta-lactoglobulin (βlg) and alfa-lactalbumin (αla), normally soluble at pH 4.6 in raw milk, in the pH 4.6 insoluble protein fraction recovered from heat-treated milk. The results have shown that pH 4.6 insoluble BSA, βlg and αla, as detected by ELISA in milk, can be regarded as thermal markers suited for either dairy process control or regulation purposes.     

Preparation and Characterization of Human Milk Fat Substitutes Based on Triacylglycerol Profiles

Human milk fat substitutes (HMFS) having similarity in (TAG) composition to human milk fat (HMF) were prepared by Lipozyme RM IM‐catalyzed interesterification of lard blending with selected oils in a packed bed reactor. Four oil blends with high similarity in fatty acid profiles to HMF were first obtained based on the blending model and then the blending ratios were screened based on TAG composition similarity by enzymatic interesterification in a batch reactor. The optimal ratio was determined as lard:sunflower oil:canola oil:palm kernel oil:palm oil:algal oil:microbial oil = 1.00:0.10:0.50:0.13:0.12:0.02:0.02. This blending ratio was used for a packed bed reactor and the conditions were then optimized as residence time, 1.5 h; reaction temperature, 50 °C. Under these conditions, the obtained product showed high degrees of similarity in fatty acid profile with 39.2 % palmitic acid at the sn‐2 position, 0.5 % arachidonic acid (n‐6) and 0.3 % docosahexaenoic acid (n‐3) and the scores for the degree of similarity in TAG composition was increased from 58.4 (the oil blend) to 72.3 (the final product). The packed bed reactor could be operated for 7 days without significant decrease in activity. The final product presented similar melting and crystallization profiles to those of HMF. However, due to the loss of tocopherols during deacidification process, the oxidative stability was lower than that of the oil blend. This process for the preparation of HMFS from lard with high similarity in TAG composition by physical blending and enzymatic interesterification, as optimized by mathematical models in a packed bed reactor, has a great potential for industrialization.     

Combined Urea Complexation and Argentated Silica Gel Column Chromatography for Concentration and Separation of PUFAs from Tuna Oil: Based on Improved DPA Level

Eicosapentaenoic acid (EPA, 20:5n‐3), docosapentaenoic acid (DPA) isomers (22:5n‐6 and 22:5n‐3) and docosahexaenoic acid (DHA, 22:6n‐3) derived from tuna oil were concentrated by three stages of urea fractionation at various crystallization temperatures and different fatty acid/urea ratios. Thereafter, polyunsaturated fatty acids concentrate containing comparatively enriched DPA levels was purified by argentated silica gel column chromatography. A product containing 22.2 ± 0.6 % EPA, 4.6 ± 0.0 % DPAn‐6, 5.9 ± 0.1 % DPAn‐3 and 42.3 ± 1.2 % DHA was obtained at 1:1.6 fatty acid/urea ratio (w/w) by crystallization at ?8 °C for 16 h, ?20 °C for 8 h, and ?8 °C for 16 h. A DPA isomer concentrate containing 26.1 ± 0.5 % DPAn‐6 and 22.3 ± 0.4 % DPAn‐3 was achieved by argentated silica gel chromatography in the 6 % acetone/n‐hexane solvent fraction (v/v), and the recovery of both fatty acids was 66.1 ± 3.2 and 70.7 ± 2.2 %, respectively. Furthermore, 91.9 ± 2.5 % EPA and 99.5 ± 2.1 % DHA with recoveries of 47.8 ± 2.0 and 56.7 ± 3.3 %, respectively, were obtained in various fractions.     

Composition and Structure of Single Cell Oil Produced by Schizochytrium limacinum SR31

Schizochytrium limacinum sp. was commercially utilized to produce single cell oil (SCO), but its detailed lipid profile remains unknown. In order to analyze the composition and structure of SCO produced by Schizochytrium limacinum SR31, the SCO extracted at stationary growth phase was separated into neutral lipids (NL), polar lipids and glycolipids by using silica gel column chromatography. The result of lipid classes in NL revealed that triacylglycerol (TAG) was the primary glyceride (93.81 %). Fatty acid (FA) analysis by gas chromatography–mass spectrometer (GC–MS) proved that palmitic acid (29.78 %) and docosahexaenoic acid (25.64 %) were the major FA. Quadrupole time of flight mass spectrometry in electrospray ionization mode coupled with ultra‐performance liquid chromatography was carried out to investigate TAG structures. More than 80 species were identified. Positional distribution of FA in TAG might contribute to further study of the FA shifts during the lipid turnover stage and nutritional evaluation of the SCO.     

Fabrication of effective mesoporous silica materials for emergency hemostasis application

Silicon - Uncontrolled bleeding is an important cause of traumatic death in wartime and peacetime. Despite the significant advances in hemostatic research, it is still challenging to develop safer...     

Preparation of Human Milk Fat Substitutes from Lard by Lipase‐Catalyzed Interesterification Based on Triacylglycerol profiles

Human milk fat substitutes (HMFSs) with triacylglycerol profiles highly similar to those of human milk fat (HMF) were prepared from lard by physical blending followed by enzymatic interesterification. Based on the fatty acid profiles of HMF, different vegetable and single‐cell oils were selected and added to the lard. Blend ratios were calculated based on established physical blending models. The blended oils were then enzymatically interesterified using a 1,3‐regiospecific lipase, Lipozyme RM IM (RML from Rhizomucor miehei immobilized on Duolite ES562; Novozymes A/S, Bagsværd, Denmark), to approximate HMF triacylglycerol (TAG) profiles, particularly with respect to the distribution of palmitic acid in the sn?2 position. The optimized blending ratios were determined to be: lard:sunflower oil:canola oil:palm kernel oil:palm oil:algal oil:microbial oil = 1.00:0.10:0.50:0.13:0.12:0.02:0.02. The optimized reaction conditions were determined to be: enzyme load of 11 wt%, temperature of 60 °C, water content of 3.5 wt%, and reaction time of 3 hours. The resulting product was evaluated for total and sn?2 fatty acids, polyunsaturated fatty acids, and TAG composition. A high degree of similarity was obtained, indicating the great potential of the product as a fat alternative for use in infant formulas.     

Influence of ultrasonic treatment on the structure and emulsifying properties of peanut protein isolate

Effects of ultrasonic treatment on emulsifying properties and structure of peanut protein isolate (PPI) were evaluated by analysis of particle size distribution, protein surface hydrophobicity, SDS-PAGE, circular dichroism spectra and environmental scanning electron microscopy. The emulsifying properties of the PPI were found to be improved by ultrasonic treatment. The mean particle size decreased from 474.7 nm to 255.8 nm while the molecular weight remained unaffected. The results of intrinsic fluorescence spectroscopy and surface hydrophobicity indicated that ultrasonic treatment induced tertiary structural changes of the proteins in PPI. Emulsifying activity index and emulsion stability index were found to be correlated fairly well with surface hydrophobicity (H₀) (r = 0.712 and r = 0.668, respectively).