The aim of this study was to evaluate patatin, a major storage protein in potato tuber, as a precursor of bioactive peptides based on in silico approaches. In silico proteolysis of patatin using 16 proteases released numerous bioactive peptides exhibiting antioxidant, angiotensin-I converting enzyme (ACE) inhibitory, dipeptidyl peptidase (DPP)-IV inhibitory, glucose uptake, neuropeptide inhibitory and ion flow-regulating capacities. Chymotrypsin C released the most bioactive sequences from patatin compared with other proteases. In addition, the results of PeptideRanker demonstrated that a number of di-and tripeptides derived from patatin possessed great potential as bioactive peptides. PRACTICAL APPLICATIONSPatatin is a major protein in potato fruit juice, which is regarded as a by-product of potato starch industry. Effective conversion of patatin into high value-added ingredients will significantly improve its potential for food application and elevate its commercial value. This study provides a theoretical basis for development of patatin as a high value-added and biofunctional ingredient in the food industry.

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At present, plant-based simulated meat is attracting more and more attention as a meat substitute. This study discusses the possibility of partial substitution of rice bran (RB) for soybean protein isolate (SPI) in preparing plant-based simulated meat. RB was added to SPI at 0%, 5%, 10%, 15%, and 20% to prepare RB-SPI plant-based simulated meat by the high moisture extrusion technique. RB-SPI plant-based simulated meat revealed greater polyphenol content and preferable antioxidant capacity (DPPH radical scavenging capacity, ABTS scavenging ability, and FRAP antioxidant capacity) compared to SPI plant-based simulated meat. The aromatic amino acids (tryptophan and tyrosine) of RB-SPI plant-based simulated meats tend to be masked first, and then the hydrophobic groups are exposed as RB content increases and the polarity of the surrounding environment increases due to the change in the disulfide conformation of RB-SPI plant-based simulated meats from a stable gauche–gauche–gauche conformation to a trans–gauche–trans conformation.

The aim of this article was to study the effect of homogenisation pressure on the microstructure of soy protein isolated (SPI) particles, the size of SPI particles and the properties of SPI particle films. Particle films were prepared by homogenising SPI particles at different pressures (0, 60, 70, 80, 90 and 100 MPa), and their optical properties, water resistance and mechanical properties were investigated. With increasing homogenisation pressure, the particle size of SPI decreased from 5123 to 295.7 nm, more homogeneous and compact network structures with good integrity were gradually constructed, and α-helices and β-turns transited to βsheets and random coils. Compared to natural SPI films, the opacity value and swelling ratio of SPI particle films were reduced by 48% and 31%, respectively, and the mechanical properties increased by 47% at 90 MPa. This study offered a theoretical basis for the application of protein particle films.