Textural, Sensory and Volatile Compounds Analyses in Formulations of Sausages Analogue Elaborated with Edible Mushrooms and Soy Protein Isolate as Meat Substitute

In this study, edible mushroom and soybean protein isolate (SPI) were used to prepare a fibrous meat analogue using thermos-extrusion and the extruded mushroom-based meat analogue as meat replacer was further developed with different formulations in fabricating sausage analogues. The effect of water content (35%, 70% and 100%), three types of edible mushroom (Lentinus edodes, Pleurotus ostreatus, Coprinus comatus and a mixture of equal proportions) and their amounts (from 15% to 100%) on the physicochemical and structural profiles were studied. The results showed that the extruded mushroom-based meat analogue prepared from Coprinus comatus (15% addition) and SPI with a water content of 35% exhibited close textural profiles to real beef. Furthermore, a texture profile analysis (TPA) combined with a principal component analysis (PCA) was conducted to compare and assess the textural traits of the sausage analogues with similar commercial products. The characterization and comparison of the flavor profile of post-processing mushroom-based meat sausage analogues (MMSA) were performed using headspace-phase microextraction (HS-SPME), coupled with gas chromatography-mass spectrometry (GC-MS). A total of 64 volatile compounds were identified, and the content in dried-processing treatment was significantly higher than for steamed-processing, which indicated that the natural fermentation process contributed to the increase in aroma substances in the non-animal sourced sausage. This study developed a feasible method to fabricate a meat replacement and to create high added-value products, which offer an opportunity for developing non-animal products with satisfactory sensory properties and flavor profiles.

Role of Disulfide Bonds and Sulfhydryl Blocked by N-Ethylmaleimide on the Properties of Different Protein-Stabilized Emulsions

To investigate the role of sulfhydryl groups and disulfide bonds in different protein-stabilized emulsions, N-ethylmaleimide (NEM) was used as a sulfhydryl-blocking agent added in the emulsion. The addition of NEM to block the sulfhydryl groups resulted in a reduction in disulfide bond formation, which enabled the internal structure of the protein molecule to be destroyed, and then decreased the restriction of protein membrane on the oil droplets. Furthermore, with the NEM content increasing in the emulsion, a reduction in the protein emulsifying activity and emulsion stability also occurred. At the same time, the intermolecular interaction of the protein on the oil droplet interface membrane was destroyed, and the emulsion droplet size increased with the NEM content in the emulsion. Although NEM blocking sulfhydryl groups from forming disulfide bonds has similar effects on three types of protein emulsion, the degree of myofibrillar protein (MP), egg-white protein isolate (EPI), and soybean protein isolate (SPI) used as emulsifiers had a subtle difference.

Structural and Emulsifying Properties of Soybean Protein Isolate–Sodium Alginate Conjugates under High Hydrostatic Pressure

Soybean protein isolate (SPI) is a kind of plant derived protein with high nutritional value, but it is underutilized due to its structural limitations and poor functionalities. This study aimed to investigate the effects of high hydrostatic pressure (HHP) treatment on SPI and sodium alginate (SA) conjugates prepared through the Maillard reaction. The physicochemical properties of the conjugate synthesized under 200 MPa at 60 °C for 24 h (SPI–SA–200) were compared with those of the conjugate synthesized under atmospheric pressure (SPI–SA–0.1), SPI-SA mixture, and SPI. The HHP (200 MPa) significantly hindered the Maillard reaction. This effect was confirmed by performing SDS-PAGE. The alterations in the secondary structures, such as α-helices, were analyzed using circular dichroism spectroscopy and the fluorescence intensity was determined. Emulsifying activity and stability indices of SPI-SA-200 increased by 33.56% and 31.96% respectively in comparison with the SPI–SA–0.1 conjugate. Furthermore, reduced particle sizes (356.18 nm), enhanced zeta potential (‒40.95 mV), and homogeneous droplet sizes were observed for the SPI-SA-200 emulsion. The present study details a practical method to prepare desirable emulsifiers for food processing by controlling the Maillard reaction and improving the functionality of SPI.

Characterization of Soybean Protein Isolate-Food Polyphenol Interaction via Virtual Screening and Experimental Studies

(1) Background: Protein–polyphenol interactions have been widely studied regarding their influence on the properties of both protein and the ligands. As an important protein material in the food industry, soybean protein isolate (SPI) experiences interesting changes through polyphenols binding. (2) Methods: In this study, a molecular docking and virtual screening method was established to evaluate the SPI–polyphenol interaction. A compound library composed of 33 commonly found food source polyphenols was used in virtual screening. The binding capacity of top-ranking polyphenols (rutin, procyanidin, cyanidin chloride, quercetin) was validated and compared by fluorescence assays. (3) Results: Four out of five top-ranking polyphenols in virtual screening were flavonoids, while phenolic acids exhibit low binding capacity. Hydrogen bonding and hydrophobic interactions were found to be dominant interactions involved in soybean protein–polyphenol binding. Cyanidin chloride exhibited the highest apparent binding constant (Ka), which was followed by quercetin, procyanidin, and rutin. Unlike others, procyanidin addition perturbed a red shift of SPI fluorescence, indicating a slight conformational change of SPI. (4) Conclusions: These results suggest that the pattern of SPI–polyphenol interaction is highly dependent on the detailed structure of polyphenols, which have important implications in uncovering the binding mechanism of SPI–polyphenol interaction.

Cloning, expression and characterization of metalloproteinase HypZn from Aspergillus niger

A predicted metalloproteinase gene, HypZn, was cloned from Aspergillus niger CGMCC 3.7193 and expressed in Pichia pastoris GS115, and the physicochemical characteristics of recombinant HypZn were investigated after separation and purification. The results showed that the specific activity of the purified HypZn reached 1859.2 U/mg, and the optimum temperature and pH value of HypZn were 35°C and 7.0, respectively. HypZn remained stable both at 40°C and at pH values between 5.0 and 8.0. The preferred substrate of HypZn was soybean protein isolates, and the Km and Vmax values were 21.5 μmol/mL and 4926.6 μmol/(mL∙min), respectively. HypZn was activated by Co2+ and Zn2+ and inhibited by Cu2+ and Fe2+. The degree of soybean protein isolate hydrolysis reached 14.7%, and the hydrolysates were of uniform molecular weight. HypZn could tolerate 5000 mM NaCl and completely lost its activity after 30 min at 50°C. The enzymological characterizations indicated that HypZn has great application potential in the food industry, especially in fermented food processing.