High-intensity ultrasound treatment on casein: Pea mixed systems: Effect on gelling properties.

This study aimed to investigate the suitability of the application of high-intensity ultrasounds (HIUS) to improve the acid induced gelation of mixed protein systems formed by casein micelles (CMs) and pea. The protein suspensions were prepared in different protein ratios CMs: pea (100:0, 80:20, 50:50, 20:80, 0:100) at 8% (w/w) total protein concentration. In the suspensions, the ultrasound treatment produced an increase in solubility, surface hydrophobicity, and a decrease in the samples' viscosity, with more remarkable differences in protein blends in which pea protein was the major component. However, the replacement of 20% of CMs for pea proteins highly affected the gel elasticity. Hence, the creation of smaller and more hydrophobic building blocks before acidification due to the HIUS treatment increased the elasticity of the gels up to 10 times. Therefore, high-intensity ultrasounds are a suitable green technique to increase the gelling properties of CMs: pea systems.

Gelling properties of black soldier fly (Hermetia illucens) larvae protein after ultrasound treatment.

H. illucens, black soldier fly larvae (BSFL) is one of the sustainable sources of protein. However, the research on the functionality of BSFL proteins is limited and need to be explored to increase consumer acceptance. The aim of this study is to create a gel system from BSFL protein and evaluate the impact of ultrasound treatment at different exposure time (5, 15, 30 min) on the physicochemical properties of BSFL protein. The highest values for surface hydrophobicity, size, ζ-potential were obtained after 15 min of ultrasound treatment and the same was found for the elastic modulus. Finally, confocal laser scanning microscopy (CLSM) along with image analysis revealed the lowest pore size after 15 min of treatment. The high protein content of BSFL protein extract and its promising gel system herein created, are important features to be considered for further development of insect-based food.

Interactions between caseins and food-derived bioactive molecules: A review.

Caseins are recognized as safe for consumption, abundant, renewable and have high nutritional value. Casein molecules are found in different aggregation states and their multiple binding sites offer the potential for delivering biomolecules with nutritional and/or health benefits, such as vitamins, phytochemicals, fibers, lipids, minerals, proteins, peptides, and pharmaceutical compounds. In the present review, we highlight the interactions between caseins and food-derived bioactive molecules, with a special focus on the aggregation states of caseins and the techniques used to produce and study the particles used for delivering. Research on interactions between caseins-minerals and casein-pharmaceutical molecules are not included here. This review aims to support the development of new and innovative functional foods in which caseins can be used as designed delivery systems.

Casein-based hydrogels: A mini-review.

Casein-based hydrogels are biocompatible, biodegradable, renewable, easy to obtain, inexpensive, and non-toxic. They exist in different physicochemical states, e.g. particle hydrogels, which can be dived in suspensions or emulsions and macro hydrogels that are gel colloid type. These biomaterials have drawn increasing attention in recent years due to their abilities to form networks of different tensile strengths and to encapsulate, protect and release biomolecules. This mini-review outlines the recent advances in casein-based hydrogel research and the uses of casein-based hydrogels as drug delivery system for both hydrophobic and hydrophilic molecules. The food and biomedical potential along with possible future uses of the casein-based hydrogels are discussed throughout the document.