Recent scientific evidence indicates that protein hydrolysates contain bioactive peptides that have potential benefits for human health. However, the bittertasting hydrophobic peptides in protein hydrolysates negatively affect the sensory quality of resulting products and limit their utilization in food and pharmaceutical industries. The approaches to reduce, mask, and remove bitter taste from protein hydrolysates have been extensively reported. This review paper focuses on the advances in the knowledge regarding the structure-bitterness relationship of peptides, the release mechanism of bitter peptides, and the debittering methods for protein hydrolysates. Bitter tastes generating with enzymatic hydrolysis of protein is influenced by the type, concentration, and bitter taste threshold of bitterness peptides. A "bell-shaped curve" is used to describe the relationship between the bitterness intensity of the hydrolysates and the degree of hydrolysis. The bitter receptor perceives bitter potencies of bitter peptides by the hydrophobicity recognition zone. The intensity of bitterness is influenced by hydrophobic and electronic properties of amino acids and the critical spatial structure of peptides. Compared to physicochemical debittering (i.e., selective separation, masking of bitter taste, encapsulation, Maillard reaction, and encapsulation) and other biological debittering (i.e., enzymatic hydrolysis, enzymatic deamidation, plastein reaction), enzymatic hydrolysis is a promising debittering approach as it combines protein hydrolyzation and debittering into a one-step process, but more work should be done to advance the knowledge on debittering mechanism of enzymatic hydrolysis and screening of suitable proteases. Further
Peanut oil body (POB), which is rich in unsaturated fatty acids and bioactive substances, is widely used in cosmetics, food, and medicine. Compared with synthetic emulsifiers, peanut oil bodies have health advantages as natural emulsions. The physicochemical properties of oil bodies affect their food processing applications. To improve peanut oil body yield, cell-wall-breaking enzymes were screened for aqueous enzymatic extraction. The optimum conditions were as follows: enzymatic hydrolysis time, 2 h; material-to-liquid ratio, 1 : 5 (
m
/
v
); enzyme concentration, 2% (
v
/
m
); and temperature, 50°C. Oil body stability was closely related to pH. With increasing pH, the average particle size and zeta-potential of the oil bodies increased, indicating aggregation, as confirmed by microstructure analysis. At pH 11, exogenous proteins at the oil body interface were eluted, leaving endogenous proteins, which led to a decreased interfacial protein content and oil body aggregation. Therefore, oil body stability decreased under alkaline pH conditions, but no demulsification occurred.
Background and Objective: The high cost of enzyme preparation and the stable emulsion produced in the process limit the large-scale application of aqueous enzymatic method. In this study, a new aqueous enzymatic method for efficient peanut oil and protein extraction was optimized. And the composition, structure, and stability of the produced emulsions were characterized.
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