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The main by‐product of the wheat germ oil extraction process is a defatted wheat germ meal, which has a relatively high protein content, making it an attractive and promising source of vegetable proteins. Four protein fractions (albumin, globulin, prolamine, and glutelin) and protein isolate from defatted wheat germ flour (DWGF) were fractionated and then characterized by amino acid analysis, SDS‐PAGE, and differential scanning calorimetry (DSC). Albumin was the major fraction (34.5%) extracted, followed by globulin (15.6%), glutelin (10.6%), and prolamine (4.6%). Protein isolate was mainly composed of albumin and globulin. These protein fractions and protein isolate showed an excellent balance of all essential amino acids, with a relatively high level of glutamic acid, arginine, leucine, and glycine, whereas cystine was lacking. All the estimated nutritional quality parameters based on amino acids composition showed that defatted wheat germ proteins had good nutritional quality. Nonreduced and reduced SDS‐PAGE analyses showed that S‐S bonds ere deficient in the structure of wheat germ proteins. The albumin fraction consisted of 19 major polypeptide bands with Mr 14,000–84,000. The globulin fraction showed four distinct polypeptides or polypeptide group bands with Mr 55,000, 37,000–43,000, 24,000, and 12,000–20,000, which may be the components of the 8S‐type and 11S‐like proteins. The prolamine fraction showed a predominant doublet‐like band at Mr 17,000–16,000, while the glutelin fraction showed five major polypeptide bands with Mr 39,000, 20,000, 18,000, 17,000, and 14,000. Protein isolate and DWGF showed very similar SDS‐PAGE patterns. Except for prolamine and glutelin fractions without detectable calorimetric response, the globulin fraction possessed the highest thermal stability (Td = 83.80°C, ΔH =1.36 J/g ), followed by protein isolate (Td = 80.05°C, ΔH = 0.76 J/g), while the albumin fraction was lowest (Td = 69.72°C, ΔH = 0.53 J/g). The findings on defatted wheat germ proteins are important for their potential application as functional food ingredients.

Pasta products and noodles have been staple foods since ancient times in many countries all over the world. These cereal products are still increasingly popular worldwide for their convenience, nutritional properties, special flavor, and taste. Pasta and noodles are essentially the same type of food but differ in their raw materials and shaping process, as well as the people and regions in the world consuming them. Many additives have been developed and are being used today in pasta and noodle products for various purposes. However, due to lack of knowledge about specific uses for some additives, they are sometimes misused by manufacturers. This can lead to opposite technological effects instead and may even cause damage to human health. Due to consumer demands, interest now focuses on natural "green" food additives with broad-spectrum functions, high effectiveness, and low toxicity. In order to provide detailed references for noodle and pasta production, as well as to provide ideas for developing new types of these products, here we summarize the types of natural additives that are being incorporated in pasta and noodle products, mainly for quality improvement and food preservation.

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The effects and mechanism of high hydrostatic pressure (HHP) on some functional and nutritional properties of soy protein isolate (SPI) for infant formula were investigated. Results indicated that solubility, water holding capacity, emulsification activity index, and foaming capacity were improved at lower pressure and time levels, whereas these properties declined at higher levels. However, the emulsification stability index dropped when the pressure increased and the foaming stability decreased with pressure and time levels rising. HHP-treated SPI gave better swallowing properties and in vitro digestibility than control. The hardness, adhesive force, and springiness of SPI gels increased with increaded pressure and elongated time, being lower than those of the control. Near UV circular dichroism spectra confirmed the alteration of tertiary and/or quaternary conformations caused by HHP. Sodiumdoecyl sulfate polyacrylamide gel electrophoresis results indicated that β-conglycinin was more pressure labile than glycinin, and high molecular weight subunits formed via disulfide linkage at higher treatment levels.