Tailoring structure and technological properties of plant proteins using high hydrostatic pressure.

The demand for proteins is rising and alternatives to meat proteins are necessary since animal husbandry is expensive and intensive to the environment. Plant proteins appear as an alternative; however, their techno-functional properties need improvement. High-pressure processing (HPP) is a non-thermal technology that has several applications including the modification of proteins. The application of pressure allows modifying proteins' structure hence allowing to change several of their properties, such as hydration, hydrophobicity, and hydrophilicity. These properties may influence the solubility of proteins and their ability to stabilize emulsions or foams, create aggregates or gels, and their general role in stability and texture of food commodities. Commonly HPP decreases the proteins' solubility yet increasing their surface hydrophobicity exposing sulfhydryl groups, which promotes aggregation or gelation or enhance their ability to stabilize emulsions/foams. However, these effects are not verifiable for all the proteins and are immensely dependent on the type and concentration of the protein, environmental conditions (pH, ionic strength, and co-solutes), and HPP conditions. This review collects and critically discusses the available information on how HPP affects the structure of plant proteins and how their techno-functional properties can be tailored using this approach.

Nutritional, Physicochemical, and Endogenous Enzyme Assessment of Raw Milk Preserved under Hyperbaric Storage at Variable Room Temperature.

Raw milk (a highly perishable food) was preserved at variable room temperature (RT) under hyperbaric storage (HS) (50-100 MPa) for 60 days and compared with refrigeration (RF) under atmospheric pressure (AP) on quality, nutritional, and endogenous enzyme activity parameters. Overall, a comparable raw milk preservation outcome was observed between storage under AP/RF and 50/RT after 14 days, with similar variations in the parameters studied indicating milk degradation. Differently, even after 60 days (the maximum period studied) under 75-100/RT, a slower milk degradation was achieved, keeping most of the parameters similar to those of milk prior to storage, including pH, titratable acidity, total solid content, density, color, viscosity, and volatile organic and fatty acid profiles, but with higher free amino acid content, signs of an overall better preservation. These results indicate an improved preservation and enhanced shelf life of raw milk by HS/RT versus RF, showing HS potential for milk and highly perishable food preservation in general.

Relevance of genipin networking on rheological, physical, and mechanical properties of starch-based formulations.

The small amount of proteins in starch-rich food industry byproducts can be an advantage to crosslink with genipin and tailor the performance of biobased films. In this work, genipin was combined with non- purified starch recovered from industrial potato washing slurries and used for films production. Starch recovered from potato washing slurries contained 0.75% protein, 2 times higher than starch directly obtained from potato and 6 times higher than the commercial one. Starch protein-genipin networks were formed with 0.05% and 0.10% genipin, gelatinized at 75 °C and 95 °C in presence of 30% glycerol. Bluish colored films were obtained in all conditions, with the higher surface roughness (Ra, 1.22 µm), stretchability (elongation, 31%), and hydrophobicity (water contact angle, 127°) for 0.10% genipin and starch gelatinized at 75 °C. Therefore, starch-rich byproducts, when combined with genipin, are promising for surpassing the starch-based films hydrophilicity and mechanical fragilities while providing light barrier properties.

Chitosan-caffeic acid-genipin films presenting enhanced antioxidant activity and stability in acidic media.

The use of chitosan films has been limited due to their high degradability in aqueous acidic media. In order to produce chitosan films with high antioxidant activity and insoluble in acid solutions caffeic acid was grafted to chitosan by a radical mechanism using ammonium cerium (IV) nitrate (60 mM). Genipin was used as cross-linker. This methodology originated films with 80% higher antioxidant activity than the pristine film. Also, these films only lost 11% of their mass upon seven days immersion into an aqueous solution at pH 3.5 under stirring. The films surface wettability (contact angle 105°), mechanical properties (68 MPa of tensile strength and 4% of elongation at break), and thermal stability for temperatures lower than 300 °C were not significantly influenced by the covalent linkage of caffeic acid and genipin to chitosan. Due to their characteristics, mainly higher antioxidant activity and lower solubility, these are promising materials to be used as active films.