Food allergens are a significant concern for global public health. Enzymolysis, which includes enzymatic hydrolysis and enzymatic cross-linking, is known for its mild conditions, as well as its high efficiency and stability, making it a widely employed method to reduce the allergenicity of food proteins. A small group of eight foods-four of animal origin (milk, eggs, fish, and crustacean shellfish) and four of plant origin (tree nuts, peanuts, wheat, and soybeans) accounts for approximately 90% of all food allergies. However, there has been no comprehensive summary of how enzymolysis impacts the digestibility and allergenicity of these eight key foods, based on both in vitro and in vivo studies. This paper seeks to provide a systematic review of the influence of enzymolysis on food allergenicity, with a focus on molecular characteristics, epitopes, immunoglobulin (Ig) E/IgG binding capacity, and digestive stability during in vitro digestion. The potential immune regulation effects of enzymolysis products in cell and animal allergy models are also highlighted.