Principal Scientist Cargill Inc Plymouth, Minnesota, United States
Abstract: Plant-based proteins have attracted growing attention in food and beverage industry like never before. The advantages over animal counterparts due to fewer cultural and religious food limitations and higher sustainability and potentially fewer negative health consequences have become the main reasons for increased demand. In addition, meeting future food demand will require a protein supply chain that does not rely solely on animals. Despite the rise, consumers are looking for realistic, natural, and minimally processed alternative meat and dairy products. Plant-based proteins available today possess challenges in various categories because of poor functional and sensory properties and nutritional limitations compared to animal-based proteins. Therefore, the modification of plant-based protein (generally carried out by physical, chemical and biological methods) to improve their technological applications and consequently wide utilization is desired.
The structure of food proteins influences their function and hence their use in final applications. Researchers have employed enzymes to modify proteins under different conditions to enhance functionality and nutritional availability. The structure-function relationship of animal-based proteins is well studied over recent decades and has strengthened their extensive use in food industry. While significant progress has been made in recent years towards plant protein characterization, it still requires detailed understanding to identify plant-based alternatives that better mimic animal proteins.
In this study, with the controlled enzymatic hydrolysis, solubility of experimental corn protein isolate was enhanced at both neutral and acidic p<span style="text-transform: uppercase;">h. Upon protein hydrolysis, hydrophobic regions were more accessible, giving rise to increased surface hydrophobicity as the degree of hydrolysis was increased. Moreover, the use of attenuated total reflectance-fourier transform infrared spectroscopy analysis showed important changes occurring in the protein secondary structure as a result of enzymatic hydrolysis. In summary, with enzymatic hydrolysis, more functional experimental corn protein hydrolysate was produced which was subsequently employed in better understanding of structure-function relationship of plant-based proteins.