Abstract Protein hydrolysis is a process used in the food industry to generate bioactive peptides of low molecular weight and with additional health benefits, such as antihypertensive, antidiabetic, and antioxidant properties that are often associated with their content on hydrophobic amino acids. This results in an increased bitterness of the products, making them less desirable for their use in food formulations. This review summarizes the main dietary sources of bitter bioactive peptides, including methods to determine their bitterness, such as the Q-values and electronic tongue; and the main factors and mechanisms underlying the bitterness of these compounds. The main strategies currently used to improve the taste and oral delivery of bioactive peptides are also discussed together with the main advantages and drawbacks of each technique. Debittering and masking techniques are reported in detail, including active carbon treatments, alcohol extraction, isoelectric precipitation, chromatographic methods, and additional hydrolytic processes. Other masking or blocking techniques, including the use of inhibitors, such as modified starch, taurine, glycine, and polyphosphates, as well as chemical modifications, such as amination, deamination, acetylation, or cross-linking were also discussed. The findings of this work highlight encapsulation as a highly effective method for masking the bitter taste and promoting the bioactivity of peptides compared to other traditional debittering and masking processes. In conclusion, the article suggests that advanced encapsulation technologies can serve as an effective means to mitigate the bitterness associated with bioactive peptides, while simultaneously preserving their biological activity, increasing their viability in the development of functional foods and pharmaceuticals. 

/pdf/strategies-for-oral-delivery-of-bioactive-peptides-with-3dkt0gyb.pdf

Strategies for oral delivery of bioactive peptides with focus on debittering and masking

Off-Flavors in Pulses and Grain Legumes and Processing Approaches for Controlling Flavor-Plant Protein Interaction: Application Prospects in Plant-Based Alternative Foods

Liquid Egg yolk (LEY) tend to aggregate during pasteurization and lead to pipe blockage, which has become a thorny problem in food industry. In this paper, the mechanism of two common amino acid osmolytes (betaine and proline) delaying thermal aggregation of LEY was investigated. The result showed that addition of 3% betaine or proline improved thermal denaturation temperature of LEY in rheology and also reduced its viscoelasticity. The addition of amino acid shrinked particle size distribution of LEY. Betaine LEY (BLEY) had strong surface hydrophobicity while proline LEY (PLEY) had excellent solubility, both of which maintained its emulsifying property. Scanning electron microscopy (SEM) revealed that BLEY and PLEY had more porous surfaces, and the structure was more loose compared with LEY at the same temperature. The relaxation time T2 indicated that betaine and proline can alleviate conversion of free water to immobilized and bound water during heat treatment process, thereby reducing the degree of thermal aggregation and viscosity. Fourier transform infrared spectroscopy (FT-IR) demonstrated the tendency of α-helix transformed to β-sheet as heating progress. Compared with LEY, the structure of BLEY and PLEY was more ordered, suggesting that orderliness of structure was the foundation for delaying thermal aggregation. In conclusion, this study provided a new idea and theoretical basis for production of heat-resistant LEY. 

Mechanism of amino acid delay on thermal aggregation behavior of liquid egg yolk: Thermal aggregation, water distribution, molecular structure

Soy sauce is a traditional fermented food produced from soybean and wheat under the action of microorganisms. The soy sauce brewing process mainly involves two steps, namely koji fermentation and moromi fermentation. In the koji fermentation process, enzymes from starter molds, such as protease, aminopeptidase, carboxypeptidase, l-glutaminase, amylase, and cellulase, hydrolyze the protein and starch in the raw ingredients to produce short-chain substances. However, the enzymatic reactions may be diminished after being subjected to moromi fermentation due to its high NaCl concentration. These enzymatically hydrolyzed products are further metabolized by lactic acid bacteria and yeasts during the moromi fermentation process into organic acids and aromatic compounds, giving soy sauce a unique flavor. Thus, the starter molds, such as Aspergillus oryzae, Aspergillus sojae, and Aspergillus niger, and their secreted enzymes play crucial roles in soy sauce brewing. This review comprehensively covers the characteristics of the starter molds mainly used in soy sauce brewing, the enzymes produced by starter molds, and the roles of enzymes in the degradation of raw material. We also enumerate current problems in the production of soy sauce, aiming to offer some directions for the improvement of soy sauce taste. 

Starter molds and multi-enzyme catalysis in koji fermentation of soy sauce brewing: A review

Diatom is a common single-cell microalgae with large species and huge biomass. Diatom biosilica (DB), the shell of diatom, is a natural inorganic material with a micro-nanoporous structure. Its unique hierarchical porous structure gives it great application potential in drug delivery, hemostat materials, and biosensors, etc. However, the structural diversity of DB determines its different biological functions. Screening hundreds of thousands of diatom species for structural features of DB that meet application requirements is like looking for a needle in a seaway. And the chemical modification methods lack effective means to control the micro-nanoporous structure of DB. The formation of DB is a typical biomineralization process, and its structural characteristics are affected by external environmental conditions, genes, and other factors. This allows to manipulate the micro-nanostructure of DB through biological regulation method, thereby transforming the screening mode of the structure function of DB from a needle in a seaway to biofabrication mode. This review focuses on the formation, biological modification, functional activity of DB structure, and its application in biomaterials field, providing regulatory strategies and research idea of DB from the perspective of biofabrication. It will also maximize the possibility of using DB as biological materials.

The Art of Exploring Diatom Biosilica Biomaterials: From Biofabrication Perspective.

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.

Pre-hospital control of bleeding is critical to save lives, however the development of hemostatic agents with efficient and safe performance is still a challenge. In this study, a hybrid hemostatic gauze (MG-PEG) with in-situ growth and tightly bound mesoporous silicon (MSN) was prepared by template method for hemorrhage control. This material integrated meso-porosity, blood coagulation and stability into flexible gauze fiber. The PEG in MG-PEG was not only used as template for the in-suit MSN growth, but also acted as joint connection between the gauze fibers and MSN. The MSN particles were firmly bound to the surface of gauze fibers with extremely low leakage after 3 min of sonication and displayed a comparable coagulant activity to untreated sample. The results of animal experiments confirmed that MG-PEG possessed superior hemostatic performance over silicates-based inorganic hemostasis-Combat Gauze, in terms of higher coagulant activity (in vivo clotting time <200 s), minimized loss of active components (liquids OD was only 3 % of CG), well biocompatibility (hemolysis ratio < 5 %, no cytotoxicity) and wider indications range for practical application. 

PEG-mediated hybrid hemostatic gauze with in-situ growth and tightly-bound mesoporous silicon.

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

PEG-mediated hybrid hemostatic gauze with in-situ growth and tightly-bound mesoporous silicon.