Determination of heterocyclic aromatic amine content of protein extracts and protein hydrolysates obtained from meat trimming wastes under different process conditions.

Development of a targeted mass spectrometry method for porcine pancreas marker peptides detection in protein hydrolysates.

Sequential ultrasound and ultra-high pressure co-treatment improves the structural and functional properties of sheep skin protein hydrolysates and their performance in low-pH beverage systems.

Kiwifruit waste valorisation: Chemical characterisation of by-products and enzymatic production of seed protein hydrolysates

Limited proteolysis of pea protein to promote aggregation/gelation: role of enzyme concentration and molecular characteristics.

AI-assisted discovery of dual antioxidant and ACE-inhibitory peptides from Hericium erinaceus.

Effect of syngas fermentation effluents containing volatile fatty acids on polyhydroxyalkanoates production.

Nanoliposomal encapsulation of chia protein hydrolysates: Physicochemical stability, in vitro release, bioaccessibility, and cytotoxicity.

A field study on a plant-based protein hydrolysate containing insecticidal protein from Metarhizium anisopliae Metchnikoff against Bactrocera oleae (Rossi) (Diptera: Tephritidae)

Antagonistic effects of sturgeon meat protein hydrolysate on alcohol-induced liver injury in mice and screening of peptides that activate alcohol dehydrogenase

Rice endosperm protein hydrolysate B (REPH-B) is produced by enzymatic degradation of rice endosperm protein. REPH-B contains the following peptides: QAFEPIRSV, pEAFEPIRSV, and TNPWHSPRQGSF. A previous study reported that REPH-B has the ability to induce plasma acylated ghrelin secretion and increase food intake in animal models. In this study, we investigated the effect of REPH-B on appetite in healthy adults aged over 40 y who had a relatively low visual analogue scale (VAS) score for hunger. Forty-six healthy subjects who were aware that their appetite had decreased were enrolled. Subjects were randomly allocated to one of two groups. The influence of REPH-B on appetite was evaluated by VAS under two conditions: repeated intake over 2 wk (Study 1) and single intake (Study 2). Though a single intake of REPH-B had no influence on any of the parameters evaluated, repeated intake of REPH-B significantly improved the VAS score for hunger. In conclusion, repeated intake of REPH-B might increase hunger in healthy adults who suffer from a lack of appetite. This study was registered with UMIN Clinical Trials Registry as UMIN000049108.

Rapeseed protein, an abundant by-product of the vegetable oil industry, is rich in essential amino acids and represents a promising source of antitumor peptides. However, the purification, characterization and mechanistic studies of antitumor peptides derived from rapeseed protein remain limited. Rapeseed protein was hydrolyzed using four proteases (alkaline protease, compound proteinase, flavourzyme and trypsin), followed by ultrafiltration and purification using gel filtration and semi-preparative HPLC. Purified peptides were identified by liquid chromatography-tandem mass spectrometry (LC-MS/MS) and antitumor activities were evaluated against HepG2, MKN-28, A549 and MCF-7 cells using the 3-(4,5-dimethyl thiazole-2-yl)-2,5-diphenyl tetrazolium bromide (i.e. MTT) assay. At 1 mg mL-1, the < 1 kDa fraction showed the strongest inhibitory effects, with inhibition rates of 55.22% ± 0.45%, 60.54% ± 0.84%, 65.33% ± 0.84% and 62.78% ± 1.57%, respectively. Five novel peptides (DHHAPQL, GVIRPPL, NDGNQPL, THPGVAQ and VTDGEAH) were identified. Among them, GVIRPPL exhibited the highest activity, with IC₅₀ values ranging from 1.14 to 1.69 mm. Mechanistic analysis showed that the reactive oxygen species (ROS) level of HepG2 cells treated with 2.0 mm rapeseed antitumor peptide GVIRPPL increased by 50.6% and reduced mitochondrial membrane potential by 53.7%, indicating that rapeseed antitumor peptides can exert antitumor effects by inducing ROS production and interfering with mitochondrial membrane potential, at the same time as having no obvious cytotoxicity to normal human hepatocytes. This study systematically isolated and identified novel antitumor peptides from rapeseed protein hydrolysates and further explored their antitumor activity and mechanisms of action, providing a scientific basis for the high-value utilization of rapeseed protein and the development of antitumor bioactive components for functional food applications. © 2026 Society of Chemical Industry.

Salmon products are excellent foods that contain indispensable nutrients including fatty acids and amino acids (AA), but during processing, salmon co-products that cannot be used for the primary purpose are also generated. Examples of such co-products include salmon protein hydrolysate concentrate (SPHC) and salmon protein hydrolysate isolate (SPHI), but there is no information about the protein quality of these co-products. Therefore, the objective of this experiment was to use the digestible indispensable amino acid score (DIAAS) method to test the hypothesis that the protein in SPHC and two sources of SPHI (SPHI1 and SPHI2) can supplement lower-quality proteins. For children from 6 months to 3 years old and individuals older than 3 years, SPHC had greater (P < 0.05) DIAAS than SPHI1 and SPHI2, and SPHI2 had greater (P < 0.05) DIAAS than SPHI1. For children from 6 months to 3 years, leucine was the first limiting AA in SPHC, and tryptophan was the first limiting AA in SPHI1 and SPHI2. For individuals older than 3 years, there was no limiting AA (DIAAS ≥ 100) for SPHC, but for SPHI1 and SPHI2 leucine was the first limiting AA. All sources of salmon protein hydrolysates had excellent AA digestibility, and SPHC can be used to compensate for lower protein quality in other ingredients to produce a balanced diet that meets requirements for all indispensable AA for individuals older than 3 years. © 2026 The Author(s). Journal of the Science of Food and Agriculture published by John Wiley & Sons Ltd on behalf of Society of Chemical Industry.

The growing global demand for protein, combined with the urgent need for effective strategies to manage conditions such as obesity and diabetes, highlights legume proteins as valuable sources of derived bioactive peptides with health-promoting properties. In this study, we employed the Caenorhabditis elegans model to investigate the effects of supplementation with hydrolysates derived from fava bean and pea protein on healthspan. Supplementation with fava bean and pea protein hydrolysates reduced fat accumulation and age-related lipofuscin pigment in the worms, without impairing their development. The fava bean protein hydrolysate significantly decreased total reactive oxygen species levels and enhanced stress tolerance to juglone exposure, suggesting the modulatory activity of the mitochondrial oxidative stress response. In contrast, pea protein hydrolysate improved the heat stress resistance of C. elegans, and gene expression and mutant analyses revealed the involvement of the endoplasmic reticulum unfolded protein response (ER-UPR) pathway in mediating its health-promoting effects. Together, our data demonstrate that fava bean and pea protein hydrolysates support healthspan in C. elegans by modulating distinct cellular stress response pathways and pave the way for further investigation in more complex animal models.

The neuraminidase protein (NA) of influenza A viruses (IAVs) plays a role in the release of viruses from infected cells. NA on viral particles hydrolyzes sialylated glycans on the cell surface for viral budding. However, the maturation and intracellular functions of NA are poorly understood. To investigate how NA functions intracellularly, glycans displayed on IAV-infected cells were profiled by lectins, and global glycome alterations, accompanied by exposed terminal galactose and glycan recapping with α1-2 fucose, were found in the virus-infected cells. Since α1-2 fucosyltransferases are localized in the Golgi, these unique structures suggest a potential NA function in the IAV-infected cells. Functional analyses using antivirals and NA-expressing cells indicate that intracellular NA function is necessary for the glycome alterations. Time-course analyses in IAV-infected cells revealed that global desialylation and α1-2 fucosylation could be observed 5 h post-inoculation, corresponding to the timeframe of viral protein expression. These observations provide a novel theory of NA functions that NA obtains its enzymatic activity intracellularly before virus assembly and serves desialylated glycans for competitive glycosyltransferases, including α1-2 fucosyltransferases, as their acceptors, resulting in glycan recapping with α1-2 fucose. Hence, intracellular NA blocks the re-sialylation of glycans, promoting efficient virus release from infected cells by inhibiting the interaction between progeny virions and sialosides. This study further demonstrated the potential NA functions of limiting secondary IAV infection. These findings provide insights into the evolutionary strategies of IAVs for shaping the strict window of superinfection by NA functions under a balance between successful replication and reassortment.IMPORTANCEInfluenza A viruses (IAVs) exploit glycans for their replication cycle. The hemagglutinin protein uses sialic acid for viral attachment, and the neuraminidase protein (NA) hydrolyzes sialosides for virus release. However, the intracellular functions of NA are not well understood. This study demonstrated that intracellular NA induces global desialylation and glycan recapping with unique structures in IAV-infected cells. This suggests a novel mode of NA function during the IAV lifecycle, where virus particles are ready to be released at the assembly, and NAs no longer need to hydrolyze the sialic acids upon egress from the cells. Therefore, the present study provides novel and significant insights into the fundamental understanding of the lifecycle of IAV. Furthermore, as NA is a primary target for anti-influenza drugs, understanding the mechanism of intracellular NA function may also support the development of antivirals.

Cancer cachexia involves progressive skeletal muscle and adipose tissue loss, which is further aggravated by cisplatin chemotherapy via increased systemic inflammation, tissue catabolism, and renal toxicity. The present study aimed to evaluate whether a combination of amaranth protein hydrolysate and Agastache rugosa extract (AKE) could attenuate cisplatin-associated cachexia and nephrotoxicity in CT26 tumor-bearing mice. Cancer cachexia was induced by subcutaneous CT26 cell inoculation in 6-week-old male BALB/c mice, followed by a 7-day tumor establishment period. Cisplatin was then administered intraperitoneally, and AKE (125 or 250 mg/kg/day) was given daily by oral gavage for 14 days. AKE administration significantly alleviated cisplatin-induced body weight loss and systemic inflammation, accompanied by preservation of skeletal muscle and adipose tissue mass, as well as increased myofiber cross-sectional area and adipocyte size. AKE markedly reduced serum inflammatory cytokines, blood urea nitrogen, and creatinine levels, indicating protection against cisplatin-induced renal injury. Mechanistically, AKE suppressed renal apoptosis through inhibition of mitogen-activated protein kinase signaling. In skeletal muscle, AKE attenuated muscle atrophy by modulating protein turnover pathways, including downregulation of muscle-specific ubiquitin ligases and restoration of Akt/mTOR and FoxO3a signaling. Furthermore, AKE mitigated adipose tissue wasting by suppressing AMP-activated protein kinase-dependent browning and restoring adipogenic signaling involved in lipid storage and differentiation. These findings demonstrate that AKE confers comprehensive protection against cisplatin-induced cachexia and nephrotoxicity by coordinately preserving muscle and adipose tissue and attenuating renal injury, suggesting its potential as a functional nutritional strategy to alleviate chemotherapy-associated tissue wasting.

Obtaining proteins and protein hydrolysate antioxidants from cold-pressed defatted rice Bran by ethanol-modified mild subcritical water extraction

Scale-up production and in vivo evaluation of fermented chicken meat protein hydrolysate for protein quality, antioxidant potential, and toxicity in male Wistar rat

Biostimulants are becoming essential and complementary tools in modern agriculture, offering an innovative and environmentally friendly approach to enhance crop production and resilience. This review explores biostimulant classification—including humic substances, seaweed extracts, protein hydrolysates, and beneficial microorganisms—and elucidates the complex mechanisms of action through which they modulate plant physiology and biochemical and molecular processes. A major focus is placed on their demonstrated ability to significantly enhance nutrient use efficiency, stimulate root growth, improve water retention, and activate plant defense systems, thereby increasing tolerance to a wide plethora of stressors like drought, salinity, and extreme temperatures. Despite their proven efficacy, the broader adoption of biostimulants faces significant hurdles, including inconsistent product formulation, fragmented regulatory frameworks, and a limited understanding of their long-term effects under diverse field conditions. By emphasizing recent scientific and technological innovations, this review proposes a framework for research and practical application. Finally, biostimulants are part of the new technologies capable of improving plant resistance to abiotic stress and adapting agricultural systems to climate change, thanks to improved productivity and efficiency in the use of production inputs and natural resources. Advances in understanding the mechanisms of action of biostimulants will enable us to modulate the concept of plant nutrition and improve crop management.

Abstract This study aimed to evaluate the potential of whey protein hydrolysate isolation (WPH) to partially replace fetal bovine serum (FBS) in Hanwoo primary muscle cell cultures, and to address issues related to cost, animal ethics, and undefined elements of FBS. WPH was prepared by enzymatic hydrolysis using bromelain. For proliferation, 10% FBS and 0.3–0.9 mg/mL WPH were used, and for differentiation, 1% FBS and 0.03–0.09 mg/mL WPH were applied. The results showed that cell proliferation increased with increasing WPH concentration, and the levels were similar to those of 20% FBS on days 4 and 5. Therefore, 0.9 mg/mL WPH was considered the most suitable concentration for proliferation. Differentiation initially increased and then decreased with increasing WPH concentration, but mRNA MyHC expression was higher than that of the 20% FBS group. Therefore, 0.06 mg/mL WPH was found to be the most suitable concentration for differentiation. These results suggest that WPH can effectively replace FBS to reduce the production costs of cultured meat and increase the value of by-product utilization, while providing a sustainable and ethical alternative source of nutrients.