Recent scientific evidence indicates that protein hydrolysates contain bioactive peptides that have potential benefits for human health. However, the bitter-tasting 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 study can focus on combining physicochemical and biological approaches to achieve high debittering efficiency and produce high-quality products.

https://onlinelibrary.wiley.com/doi/pdfdirect/10.1111/1541-4337.13050

Review on the release mechanism and debittering technology of bitter peptides from protein hydrolysates.

A novel phospholipid-based nanovesicle (PBN) was developed to encapsulate (-)-epigallocatechin gallate (EGCG), a major polyphenol in green tea, to mask its bitter taste and expand its application in food products. The PBN was formed using W/O emulsion-transfer methods and showed a multilayer membrane nanovesicle structure (around 200 nm) observed with TEM. The PBN possessed a high encapsulation efficiency (92.1%) for EGCG. The bitterness of EGCG was significantly reduced to 1/12 after encapsulation. Fourier transform infrared spectroscopy (FTIR) indicated the EGCG mainly interacted with the upper chain/glycerol/head group region of the lipid bilayerin PBN. Quartz crystal microbalance with dissipation (QCM-D) showed the addition of γ-cyclodextrin in PBN enhanced EGCG's adsorption with phospholipids and allowed for its good sustained release. Encapsulating EGCG in PBN inhibited its complexation with mucin, reducing bitterness and astringency. This provides a new method to improve EGCG's flavor, potentially expanding its application in the food industry. 

Encapsulation of (-)-epigallocatechin gallate (EGCG) within phospholipid-based nanovesicles using W/O emulsion-transfer methods: Masking bitterness and delaying release of EGCG.

Many functional food ingredients activate human bitter taste receptors (hTAS2Rs). In this study, A novel inhibitor, Trp-Trp, for hTAS2R14 was identified by searching for the agonist peptide's analogs. Trp-Trp also inhibited hTAS2R16, hTAS2R43, and hTAS2R46, which share the same agonists with hTAS2R14. The multifunctional characteristic of Trp-Trp is advantageous for use as bitterness-masking agents in functional foods.

Trp-Trp acts as a multifunctional blocker for human bitter taste receptors, hTAS2R14, hTAS2R16, hTAS2R43, and hTAS2R46.

In 2014, the Ministry of Health, Labour and Welfare reported that flavor is the most valued aspect of food for consumers. Since flavor is a perception of the combined taste and smell of food, quantifying the taste and smell of food is useful in the rational design of desirable flavors. Taste and smell are also called chemical senses as they involve the detection of chemical components. Since 2000, progress in the identification of taste and olfactory receptors has made it possible to evaluate the taste and smell of food at a molecular level by cell-based receptor assays. Recently, molecular evaluation of taste and smell focusing on the chemosensory receptors has attracted attention. This review outlines the cell-based assay methods for these chemosensory receptors. 

Evaluation and Design of Food Flavor by Cell-based Assay of Chemosensory Receptors

Food allergies are a significant health issue worldwide. In many countries, labeling of primary allergens in food products has been made mandatory to ensure consumer safety. In food manufacturing settings, the lateral flow immunoassay (LFI)—based on antigen–antibody reactions—is a rapid and accurate method for allergen testing and is widely used. Peptide arrays are tools that enable the synthesis of peptides of any sequence on a substrate and high-throughput analysis of their interactions with chemicals. This study aimed to investigate a new application of peptide arrays in the field of food technology, particularly in the development of antibodies for food allergen testing. First, monoclonal antibodies against hen egg ovalbumin, a major food allergen, were produced. Then, using a peptide array, the epitope and specificity of the antibodies were comprehensively and precisely analyzed. Finally, an LFI kit incorporating the antibodies demonstrated both high specificity and detection sensitivity for food allergen testing. These findings indicate that peptide arrays are valuable tools in the development of antibodies for food allergen testing, ensuring reliability and accuracy at the molecular level.

Comprehensive Epitope Analysis of Monoclonal Antibodies Binding to Hen Egg Ovalbumin Using a Peptide Array

Bitterness-masking peptides for epigallocatechin gallate identified through peptide array analysis

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Bitterness-masking peptides for epigallocatechin gallate identified through peptide array analysis