{"id":7354,"date":"2024-09-26T07:58:48","date_gmt":"2024-09-26T07:58:48","guid":{"rendered":"https:\/\/longchangchemical.com\/?p=7354"},"modified":"2026-04-28T10:42:36","modified_gmt":"2026-04-28T10:42:36","slug":"how-to-effectively-weaken-the-bitter-taste-of-protein-hydrolysate","status":"publish","type":"post","link":"https:\/\/longchangchemical.com\/it\/how-to-effectively-weaken-the-bitter-taste-of-protein-hydrolysate\/","title":{"rendered":"Come attenuare efficacemente il sapore amaro dell'idrolizzato proteico?"},"content":{"rendered":"

How to effectively weaken the bitter taste of protein hydrolysate?<\/p>\n

In modern food industry, protein hydrolysis is generally based on enzymatic hydrolysis, protein hydrolysates have better physiological activity than intact proteins, and small molecule peptides are easy to be absorbed by the human body effectively and quickly. Recent studies have shown that hydrolysates such as soybean peptides also have low antigenicity, antihypertensive, cholesterol inhibition and other health functions. However, proteins produce different degrees of bitterness during enzymatic hydrolysis, which limits the application of protein hydrolysates in modern food. Therefore how to reduce the bitter taste of protein hydrolysate becomes the main technical bottleneck in the development of protein hydrolysate as food. In this paper, the factors affecting the formation of bitter flavor and the methods for removing the bitterness are reviewed.<\/p>\n

Generation of bitter flavor<\/p>\n

The bitter taste of protein hydrolysate mainly comes from the hydrophobic polypeptide in the hydrolysate, the natural protein itself does not have bitter taste, most of the hydrophobic side chain is wrapped inside the protein molecule, which can’t be contacted with the taste cells; on the other hand, the intact proteins have a large molecular weight and complex molecular configuration, and there is a spatial distance between the hydrophobic residues and the taste receivers on the taste buds, so that no bitterness will be produced. After enzymatic hydrolysis of proteins to produce polypeptides of lower molecular weight, the hydrophobic side chains are exposed and the polypeptides come into contact with the taste cells and produce a bitter taste. In addition, the presence of hydrophilic groups and basic amino acid residues in the peptide also has an effect on the peptide bitter taste.<\/p>\n

Factors in the formation of bitter taste<\/p>\n

Hydrophobicity of bitter peptides
\nAmino acid sequence (primary structure) of the peptide
\nSpatial structure of the peptide (secondary structure)
\nMolecular weight size of the peptide, source of protein raw material
\nChoice of protease type
\nDegree of protein hydrolysis<\/p>\n

With the enzymatic reaction of protease, large molecules of protein are sheared apart by protease from different sites to become small molecules of polypeptide. If the end of the polypeptide is hydrophobic amino acid residues or the polypeptide contains more hydrophobic amino acids, it is easy to be combined with the bitter receptor to produce a high-intensity bitter taste; and it has been found that hydrophobic amino acids existing in the form of a single unit are much weaker in their bitter taste. Common hydrophobic amino acids are tyrosine, tryptophan, phenylalanine, valine, leucine, isoleucine, alanine and methionine [6], reducing the proportion of these amino acids in the middle and ends of the polypeptide can substantially reduce the bitterness of proteolytic products.<\/p>\n

After years of intensive research, we have developed the FF series (including two products: FF104 and FF106), a complex enzyme preparation that can substantially reduce the bitter flavor of proteolytic digests. The enzymes are prepared by mixing selected endonucleases and exonucleases. The endonuclease can efficiently hydrolyze the internal peptide chain of proteins and hydrolyze large proteins into polypeptides; the exonuclease can quickly cut down the hydrophobic amino acids at the N-terminal end of the polypeptide chain and turn it into polypeptides with hydrophilic amino acids at the N-terminal end. By reducing the proportion of peptides with hydrophobic amino acids at the N-terminal end, the bitter flavor of the proteolytic solution can be reduced.<\/p>\n

Application process<\/p>\n

Proteolytic solution —-pH6.0-6.5, T 50-55\u2103—- Add 0.1-0.3% of FF104\/FF106—- React for 5-6h—- Elevate the temperature to 75\u2103, keep warm for 30min—- Add other substances, Melad reaction —– Concentration and drying —- Finished product<\/p>\n

Application examples<\/p>\n

Application of FF104 and FF106 in yeast extracts<\/p>\n

Both enzyme preparations can substantially improve the bitterness of the product, have a certain enhancement effect on freshness, fullness and thickness, and can substantially improve the overall taste of the applied product.<\/p>\n

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A practical sourcing checklist for enzyme, biotech, and food-ingredient topics<\/h2>\n

In enzyme and food-processing projects, the most useful decision frame is usually application fit plus process stability: which ingredient performs under the intended pH, temperature, time, and substrate conditions without creating a downstream quality or compliance problem.<\/p>\n