Due to the recent increase in the human population and the associated shortage of protein resources, it is necessary to find new, sustainable, and natural protein resources from invertebrates (such as insects) and underutilized plants. In most cases, compared to plants (e.g., grains and legumes) and animals (e.g., fish, beef, chicken, lamb, and pork), insect proteins are high in quality in terms of their nutritional value, total protein content, and essential amino acid composition. This review evaluates the recent state of insects as an alternative protein source from production to application; more specifically, it introduces in detail the latest advances in the protein extraction process. As an alternative source of protein in food formulations, the functional characteristics of edible insect protein are comprehensively presented, and the risk of allergy associated with insect protein is also discussed. The biological activity of protein hydrolyzates from different species of insects (Bombyx mori, Hermetia illucens, Acheta domesticus, Tenebrio molitor) are also reviewed, and the hydrolysates (bioactive peptides) are found to have either antihypertensive, antioxidant, antidiabetic, and antimicrobial activity. Finally, the use of edible insect protein in various food applications is presented.

The increasing demand for sustainable protein sources has intensified interest in improving the processing efficiency of traditional proteins and developing novel alternatives, particularly those derived from plants and algae. Among various processing technologies, pH shifting has attracted attention due to its simplicity, low cost, and capacity to effectively alter protein structure and functionality. However, employing pH shifting alone requires extremely acidic or alkaline conditions, which can lead to protein denaturation and the generation of undesirable by-products. To address these limitations, this review explores the integration of pH shifting with physical processing techniques such as ultrasound, high-pressure processing, pulsed electric fields, and thermal treatments. Moreover, this review highlights the effects of these combined treatments on protein conformational transitions and the resulting improvements in functional properties such as solubility, emulsification, foaming capacity, and thermal stability. Importantly, they reduce reliance on extreme chemical conditions, providing greater sustainability in industrial applications, particularly in food product development where milder processing conditions help preserve nutritional quality and functional properties. In that sense, this combined treatment approach provides a promising and eco-efficient protein modification strategy, and bridges technological innovation with sustainable resource utilization.