Effects of combined high pressure and temperature on solubility, foaming, and rheological properties of soy 11S globulin

Abstract

This study examines the effects of combined high pressure (0.1, 200, and 400 MPa) and temperature (25 and 50 C) on the solubility, aggregation, conformation, foaming, emulsifying capacity, and rheological properties of soy 11S globulin. The foaming stability, particle size, free sulfhydryl groups content, emulsifying activity, emulsifying stability, and shear stress of soy 11S globulin were decreased significantly (p ≤ .05) compared with that of 0.1 MPa-treated sample, but the solubility, surface hydrophobicity, foaming capacity, and apparent viscosity were increased significantly (p ≤ .05), except the sample treated at 400 MPa and 50 ± 2 C. The solubility, surface hydrophobicity and free sulfhydryl groups content of soy 11S globulin decreased significantly (p ≤ .05) with increasing pressure and temperature, which caused the decrease of the foaming capacity, emulsifying activity, emulsifying stability, shear stress, and apparent viscosity. Overall, the use of high-pressure and thermal treatments combined could change the foaming, emulsifying, and rheological properties of soy 11S globulin through the increase/decrease of protein solubility, aggregation, surface hydrophobicity, and free sulfhydryl groups content. Practical applicationsThis study provides a method of high-pressure and thermal treatments combined, which can change the solubility, foaming, and rheological properties soy 11S globulin, and its use should be expanded in food processing. | INTRODUCTIONDue to its high nutritional value and cost performance, soybean and its products have been widely used in food all over the world (Yue, Li, Liu, Zhang, & Zheng, 2021). The soy 11S globulin is the main component of soy protein, comprising over 35% of the total protein content, and it is composed of disulfide-bonded acidic subunit A and basic subunit B, connected via a disulfide bond (Nishinari, Fang, Guo, &

Effects of low‐frequency magnetic field on solubility, structural and functional properties of soy 11S globulin

“…Surface hydrophobicity and intrinsic fluorescence Soy 11S globulin solution was diluted to 1 mg mL −1 with 0.1 mol L −1 phosphate buffer (pH 7.0), and 1 mg mL −1 bromophenol blue (BPB) solution was prepared with distilled water. Surface hydrophobicity was measured according to the method described by Xie et al 22 Briefly, 5 mL diluted protein solution was mixed with 1 mL BPB solution, then centrifuged at 4000 × g for 15 min, the supernatant was diluted 15 times with phosphate buffer. The absorbance was measured at 595 nm.…”