Water‐soluble myofibrillar proteins prepared by high‐pressure homogenisation: a comparison study on the composition and functionality

To expand utilisation of meat in various products, the characterisation and functionalities of water‐soluble myofibrillar proteins (WSMP) induced by high‐pressure homogenisation (HPH) were determined by comparison with those of soy protein isolate (SPI) and whey protein isolate (WPI). WSMP had high contents of protein (87.40%), which was mainly composed of myosin, actin and tropomyosin. The essential amino acids of WSMP achieved the FAO/WHO/UNO (2007) standards for preschool children, and the contents of lysine and sulphur‐containing amino acids of WSMP were higher than those of SPI, making it desirable for children formulations. WSMP showed higher surface hydrophobicity while its water solubility was similar to that of SPI, but lower than that of WPI. WSMP demonstrated superior water/oil absorption capacities and emulsifying properties. The fibrous structure and high hydrophobic activity characteristics of WSMP were able to stabilise oil droplets with submicron droplet size, consequently responsible for its excellent emulsifying properties.     

R‐Index Measure of Microencapsulated Tributyrin in Gamma‐Cyclodextrin Influenced by Drying Method

Microencapsulation is commonly used in the food industry for a variety of purposes including added ingredient functionally and taste‐masking for those ingredients with negative sensory qualities. Tributyrin (TB), a source intestinally‐essential butyric acid, possesses negative aroma (cheesy, fecal) and taste (bitter) qualities. This has significantly limited its use in food applications for the potential improvement of intestinal health. Utilizing spray drying and low‐temperature oven drying, microcapsules containing TB were produced using whey (WPI), WPI and inulin, and gamma‐cyclodextrin (GCD). To determine how microcapsule formulation and drying method affected the perception of TB relative to a control, microencapsulated and free TB were added to an infant formula system and evaluated using the rating method to determine R‐index measures. Pooled R‐index measures (α = 0.01, 2‐tailed, and n = 170) indicated that the only microcapsule not significantly different from the control (R‐index below 57.95%) was the GCD and TB oven dried (GCT OD) microcapsule. All other WPI, WPI–inulin, and GCD and TB spray‐dried (GCT SD) microcapsules were all significantly different from the control. Average individual R‐index results indicated that all microcapsules in infant formula, except for GCT OD, were significantly different (P < 0.01) from the control formula but not from free TB. Spray drying may create microcapsules with surface TB and disturb the GCD–TB complex, allowing free, and surface TB to be perceived by the panelists. The GCT OD microcapsule has the potential to be used for the potential oral treatment of intestinal disorders in functional food applications without the negative sensory qualities of TB.     

Microencapsulation of Bifidobacterium bifidum F‐35 in Whey Protein‐Based Microcapsules by Transglutaminase‐Induced Gelation

Abstract: Bifidobacterium bifidum F‐35 was microencapsulated into whey protein microcapsules (WPMs) by a transglutaminase (TGase)‐induced method after optimization of gelation conditions. The performance of these WPMs was compared with that produced by a spray drying method (WPMs‐A). WPMs produced by the TGase‐induced gelation method (WPMs‐B) had larger and denser structures in morphological examinations. Native gel and SDS‐PAGE analyses showed that most of the polymerization observed in WPMs‐B was due to stable covalent crosslinks catalyzed by TGase. The degradation properties of these WPMs were investigated in simulated gastric juice (SGJ) with or without pepsin. In the presence of pepsin, WPMs‐A degraded more quickly than did WPMs‐B. Finally, survival rates of the microencapsulated cells in both WPMs were significantly better than that of free cells and varied with the microencapsulation method. However, WPMs‐B produced by TGase‐induced gelation could provide better protection for microencapsulated cells in low pH conditions and during 1 mo of storage at 4 °C or at ambient temperature.     

Gelation enhancement of soy protein isolate by sequential low‐ and ultrahigh‐temperature two‐stage preheating treatments

The effects of combined two heating steps with low (LT, 60 °C for 1 h) and ultrahigh (UHT, 130 or 140 °C for 4 s) temperatures on the thermal gelation of soy protein isolate (SPI) were studied. UHT pretreatments significantly increased protein solubility and enhanced the gelling potential of SPI. Yet, the two‐stage preheating treatment with LT and then UHT‐130 °C had a most remarkable effect: the gel strength of the SPI₆₀₊₁₃₀ sample was, respectively, 1.45‐, 1.64‐ and 3.19‐fold as strong as those of SPI₆₀, SPI₂₅₊₁₃₀, and SPI₂₅. In comparison with single LT or UHT treatments, this two‐stage heating also produced greater amounts of soluble protein aggregates stabilised predominantly by disulphide bonds and hydrophobic forces, contributing to the improved gel network structure.     

Effect of limited enzymatic hydrolysis on physico‐chemical properties of soybean protein isolate‐maltodextrin conjugates

The effect of limited hydrolysis was investigated on the physico‐chemical properties of soy protein isolate–maltodextrin (SPI‐Md) conjugate. The hydrolysates at a degree of hydrolysis (DH) of 1.8% showed much higher surface hydrophobicity (H₀; 71.39 ± 3.60) than that of the SPI control (42.09 ± 2.17) and SPI‐Md conjugates (53.46 ± 2.74). Intrinsic fluorescence analysis demonstrated the unfolding of protein molecule and exposure of hydrophobic groups of SPI‐Md conjugate hydrolysates. As evidenced by far‐UV circular dichroism (CD) spectroscopy, the limited hydrolysis increased the unordered secondary structures of SPI‐Md conjugates. The denaturation temperature (T_d) of SPI‐Md conjugate was significantly increased by subsequent limited hydrolysis from 102.53 ± 0.60 °C to 108.11 ± 0.61 °C at DH 1.8%. In particular, the emulsifying activity index (EAI) was improved notably after limited hydrolysis of DH 1.8% (147.76 ± 4.39 m² g^?1) compared with that of native SPI (88.90 ± 1.44 m² g^?1) and SPI‐Md conjugate (108.97 ± 1.45 m² g^?1).     

Encapsulation of Beta‐carotene in Lipid Microparticles Stabilized with Hydrolyzed Soy Protein Isolate: Production Parameters,Alpha‐tocopherol Coencapsulation and Stability Under Stress Conditions

The objectives of this research were to study the encapsulation of beta‐carotene (BC) in solid lipid microparticles (SLM) of palm stearin (PS) and stabilized with hydrolyzed soy protein isolate (HSPI), and also to investigate the effect of alpha‐tocopherol (TOC) addition to the systems. Through the characterizations of SLM produced with different formulations, it was verified that systems with 5% (w/v) PS, 1.0% (w/v) HSPI, and 0.3% (w/v) xanthan gum (XG) presented the highest stability, with average diameters of approximately 1.2 μm. This formulation was applied for the production of BC‐loaded SLM, with different concentrations of TOC. In SLM containing TOC, nearly 75% of encapsulated BC was preserved after 45 d of storage. The kinetic profiles for degradation of encapsulated BC were fitted to a pseudo‐1st‐order model, and the results showed that the main difference among the systems with different BC:TOC ratios was the residual concentration of BC. The stability of the BC‐loaded SLMs was also studied after stress conditions, and the results showed that the SLMs were able to support thermal treatments over 60 °C but presented low stability after different ionic strength stresses.     

Influence of Xanthan–Curdlan Hydrogel Complex on Freeze‐Thaw Stability and Rheological Properties of Whey Protein Isolate Gel over Multiple Freeze‐Thaw Cycle

The effect of adding xanthan–curdlan hydrogel complex (XCHC) at 2 concentrations (0.25 and 0.5% w/w) on the freeze‐thaw stability of heat‐induced whey protein isolate (WPI) gel was investigated. Samples were stored at 4 °C for 24 h before subjected to 5 freeze‐thaw cycles alternating between ?16 °C (18 h) and 25 °C (6 h). Adding XCHC to the WPI solution resulted in the reduction of a significant amount of syneresis up to 5 repeated freeze‐thaw cycles. Addition of XCHC decreased the amount of syneresis from 45% in the control sample (pure WPI gel) to 31.82% and 5.44% in the samples containing 0.25% and 0.5% gum, respectively, after the 5th freeze‐thaw cycle. XCHC increased the storage modulus (G′) of the gels and minimized the changes of the G′ values over the 5 freeze‐thaw cycles, indicating improvement of the stability of the system. Furthermore, the minimum protein concentration for gel formation decreased in the presence of the XCHC. Scanning electron microscopy (SEM) images showed that addition of XCHC resulted in the formation of a well‐structured gel with numerous small pores in the network, which consequently improved the water retention ability during the temperature abuses up to 5 freeze‐thaw cycles. These results have important implications for using XCHC in the formulation of the frozen WPI‐based products with improved freeze‐thaw stability and rheological properties.     

Initial Droplet Size Impacts pH‐Induced Structural Changes in Phase‐Separated Polymer Dispersions

The effect of pH change on the morphology of whey protein isolate (WPI)–pectin dispersions obtained from phase‐separated systems after mild shear was studied. The purpose of this study was to examine the impact of mixing speed on the initial particle size of biopolymer complexes and their structure morphology after sequentially changing the pH. Therefore, solutions of WPI and pectin were combined at pH 6.1, allowed to phase separate and were then mildly homogenized at 50, 100, and 150 rpm, respectively, to form a dispersion containing differently sized WPI droplets in a surrounding pectin‐rich phase. Each dispersion was then subjected to a pH change, such as 6.1 to 5.2 and 3.2, by slowly adding hydrochloric acid. The systems morphology, size, appearance, rheology, and storage stability was then characterized by optical microscopy, static light scattering, visual inspections, and steady shear rheometry to gain insights into the structural rearrangements. Results indicated substantial changes in the structure of the dispersion when the pH was changed. Formation of core‐shell structures from the WPI droplets was observed at an intermediate pH. There, initial droplet size was found to affect structures formed, that is, core‐shell type particles would only form if droplets were large (>1.5 μm) prior to pH change. Insights gained may be of importance to food manufacturers intending to create new structures from mixtures of proteins and carbohydrates.     

Calcium sulphate‐induced soya bean protein tofu‐type gels: influence of denaturation and particle size

Soya bean protein isolate (SPI) dispersions (7.25%, w/v) were heated at 65, 75, 85 or 90 °C for different time periods to produce SPI aggregates with diverse degrees of denaturation and particle size to investigate the effects on calcium sulphate (CaSO₄)‐induced tofu‐type gel. The results revealed that gel hardness and water‐holding capacity correlated positively with the degree of denaturation of glycinin (11S) and the particle size of the SPI aggregates. The formed gels showed more uniform and denser network structures with increasing degrees of denaturation and particle size of SPI. Hydrophobic interaction was speculated to be the crucial factor for the retention of gels prepared by SPI whose degree of denaturation by 11S was lower than 4.35%. However, disulphide bonds probably played a more important role in the retention of gels generated by SPI with the 11S denaturation degree of >84.47%. Moreover, the bulk density of the protein aggregates might determine the gel structures to a certain extent.     

Iron‐encapsulated cold‐set whey protein isolate gel powder – Part 1: Optimisation of preparation conditions and in vitro evaluation

A central composite design with a quadratic model was used to investigate the effects of three independent variables involved in the synthesis of iron‐encapsulated cold‐set whey protein isolate gel (WPI) on encapsulation efficiency (EE) and L*, a*, b* colour characteristics. The optimal conditions for maximum EE with minimum colour alteration were determined as 6.8% WPI, 18.8 mM iron and pH 7. In an in vitro gastrointestinal assay, only about 28% of the encapsulated iron was released in the gastric condition (with pepsin at pH 1.2), compared to 95% in the intestinal condition (with pancreatin at pH 7.5).     

Improvement in emulsifying properties of soy protein isolate by conjugation with maltodextrin using high‐temperature,short‐time dry‐heating Maillard reaction

Soy protein isolate (SPI)–maltodextrin (MD) conjugates were synthesised using Maillard reaction under high‐temperature (90, 115 and 140 °C), short‐time (2 h) dry‐heating conditions. The loss of free amino groups in proteins and sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS‐PAGE) profile confirmed that SPI‐MD conjugates were formed and higher dry‐heated temperatures could increase the glycosylation degree. The emulsifying properties of SPI and SPI‐MD conjugates were evaluated in oil‐in‐water emulsions. The emulsions stabilised with SPI‐MD conjugates synthesised at 140 °C exhibited higher emulsifying stability and excellent storage stability against pH, ionic strength and thermal treatment compared with those synthesised at 90 °C, 115 °C and SPI stabilised emulsions. This might be due to a greater proportion of conjugated MD in SPI‐MD conjugates synthesised at 140 °C because of the higher glycosylation degree, and more conjugated MD on the droplet surface could provide steric effect and enhance the stability of the droplets in the emulsions.