As a result, it is difficult to select an alternative protein to replace an animal protein in specific food products. One of the major challenges in this area is that there are no widely recognized analytical methods available to measure and compare the functional attributes of animal and alternative proteins under conditions where they may be used in real food applications. Proteins derived from animals, such as those isolated from milk (casein and whey protein), egg (ovalbumin), and meat (gelatin) are commonly used as emulsifiers in the food industry because they are amphiphilic molecules that can adsorb to oil-water interfaces, reduce the interfacial tension, and protect the oil droplets from aggregation. Consequently, it is important that any alternative proteins provide the same desirable functional and nutritional attributes as animal proteins. Moreover, they contribute to the nutritional content of foods by providing calories and essential amino acids. These proteins make important contributions to the desirable physicochemical, textural, and sensory attributes of many foods due to the diverse range of functional attributes, such as emulsification, foaming, thickening, gelling, structure forming, water holding, and oil retention. Animal proteins may be naturally present within whole foods (such as meat, fish, eggs, or milk) or they may be isolated and used as functional ingredients (such as gelatin, lysozyme, caseinate, or whey proteins). Proteins are one of the most versatile functional ingredients found in foods and so there is a strong focus on finding alternatives to animal proteins. A major thrust in this area is the replacement of animal-derived ingredients (such as those from meat, fish, eggs, or milk), with those from alternative sources (such as plants, algae, and microbes). This information should be useful to the food industry when it is trying to identify alternative proteins to replace existing emulsifiers in specific food applications.Īn important trend in the modern food industry is the creation of foods designed to reduce the negative impacts of the food supply on the environment, human health, and animal welfare. These tests include methods for characterizing the effectiveness of the proteins to promote the formation and stability of the small droplets generated during homogenization, as well as their ability to stabilize the droplets against aggregation under different conditions (e.g., pH, ionic composition, temperature, and shearing). In this article, we discuss the physicochemical principles of emulsifier functionality and then present a series of analytical tests that can be used to quantify the ability of proteins to form and stabilize emulsions. This information is required to select the most appropriate protein for each application. A major challenge in this area is the lack of standardized methods to measure and compare the functional performance of proteins under conditions they might be used in food applications. Many new kinds of plant- or microbial-derived proteins are being isolated for potential utilization as functional ingredients by the food industry. This effort is largely a result of the demand for foods that are better for the environment, human health, and animal welfare. ![]() The food industry is trying to reformulate many of its products to replace functional ingredients that are chemically synthesized or isolated from animal sources (such as meat, fish, eggs, or milk) with ingredients derived from plant or microbial sources.
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