Plant-derived Proteins Research Articles

Relationship between rheological parameters and structure formation in high moisture extrusion of plant protein biopolymers

High moisture extrusion (HME) is widely employed to texturize plant-derived protein ingredients, but its development is still much based on trial and error. In this project, it was hypothesized that the rheological properties of plant-based mixtures analyzed when in the molten state and during their cooling can aid in understanding their structure formation. To test this hypothesis, biopolymer formulations containing pea protein isolate (PPI) were examined at different moisture and starch contents, and their rheological properties were analyzed using a closed cavity rheometer (CCR) at temperatures relevant to those applied during HME processing. The results obtained with the CCR were then contrasted with the mechanical properties of HME obtained using a lab scale extruder, measured using oscillatory rheology, large deformation, and dynamic mechanical analysis. Low moisture (55 %) HMEs were stiff and brittle, while high moisture (65 %) HMEs formed more flexible and anisotropic structures. Addition of starch created softer structures. The viscoelastic properties of the biopolymer mixes measured with the CCR were correlated with the mechanical parameters of the final extrudates. Strong correlations were found between small deformation rheological parameters measured in the CCR and the hardness values, while non-linear viscoelastic parameters were correlated with anisotropy indexes. Results demonstrated that the material properties measured at the early cooling stages strongly influence the structural heterogeneity in HMEs. This study highlights the potential to use the viscoelastic properties of the biopolymer mix measured with the CCR to predict their structural features when processed by extrusion.

Biomimetic non-collagenous proteins-calcium phosphate complex with superior osteogenesis via regulating macrophage IL-27 secretion

Traumatic defects or non-union fractures presents a substantial challenge in the fields of tissue engineering and regenerative medicine. Although synthetic calcium phosphate-based biomaterials (CaPs) such as dibasic calcium phosphate anhydrate (DCPA) are commonly employed for bone repair, their inadequate cellular immune responses significantly impede sustained degradation and optimal osteogenesis. In this study, drawing inspiration from the key structure of an acidic non-collagenous protein-CaP complex (ANCPs-CaP) essential for natural bone formation, we prepared biomimetic mineralized dibasic calcium phosphate (MDCPA). This preparation utilized plant-derived non-collagenous protein Zein as the organic template and acidic artificial saliva as the mineralization medium. Physicochemical property analysis revealed that MDCPA is a complex of Zein and DCPA, which mimics the composite of the natural ANCP-CaP. Moreover, MDCPA exhibited enhanced biodegradability and osteogenic potential. Mechanistic insight revealed that MDCPA can be phagocytized and degraded by macrophages via the FCγRIII receptor, leading to the release of interleukin 27 (IL-27), which promotes osteogenic differentiation by osteoimmunomodulation. The critical role of IL-27 in osteogenesis is further confirmed using IL-27 gene knockout mice. Additionally, MDCPA demonstrates effective healing of critical-sized defects in rat cranial bones within only 4 w, providing a promising basis and valuable insights for critical-sized bone defects regeneration.

Aqueous-based assembly of plant-derived proteins yields a crosslinker-free biodegradable bioplastic consistent with green chemistry principles.

Plastics are an indispensable part of modern life. Due to the harmful environmental consequences of petroleum-based plastic usage, there is an urgent need to replace them with biodegradable bioplastics that meet the sustainability standards required for a low environmental footprint. Here, we use plant-derived proteins to produce bioplastics. Since most plant-derived proteins are not water-soluble, there has always been a need to use acidic or basic solutions or organic solvents with plasticizers and crosslinkers to produce bioplastic. Here, we present a counterintuitive approach for using water-insoluble plant-derived soy and pea proteins to manufacture large-scale bioplastics using only water as a solvent without common plasticizers or crosslinkers. We show that bioplastics can form via a self-assembly process initiated by a small molecular initiator while maintaining favourable mechanical properties. The lack of crosslinking and the protein nature of the bioplastic leads to a rapid biodegradation process under various conditions. Overall, the approach we present is highly attractive in terms of cost and time, and most importantly, it obeys all the relevant principles of green chemistry in bioplastics production.

Postprandial plasma aminoacidemia and indices of appetite regulation following pea-rice blend, pea isolate and whey protein ingestion in healthy young adults.

Plant-derived proteins are often deficient in essential amino acids and have lower rates of digestibility than animal-derived proteins. Blending different plant-derived proteins could compensate for these deficiencies and may augment postprandial aminoacidemia over single-source plant proteins. This study assessed plasma amino acids and appetite hormones, appetite sensations and ad libitum energy intake following ingestion of a pea-rice protein blend (BLEND), compared with pea-only (PEA) and whey (WHEY) protein. In a randomised, double-blind, crossover design, ten healthy adults (M n 4, F n 6; mean (sd) age 22 (sd 3) years; BMI 24 (sd 3) kg·m2) ingested 0·3 g·kg·body mass-1 of BLEND, PEA or WHEY. Arterialised venous blood samples and appetite ratings were obtained in the fasted state and over 240 min postprandially. Energy intake was measured via an ad libitum buffet-style test meal. Mean plasma essential amino acid incremental AUC was higher in WHEY, compared with PEA (P < 0·01; mean diff (95 % CI): 44218 (15806, 72631) μmol·240 min·l-1) and BLEND (P < 0·01; 14358 (16031, 101121) μmol·240 min·l-1), with no differences between PEA and BLEND (P = 0·67). Plasma ghrelin and glucagon-like peptide-1, appetite ratings and ad libitum energy intake responses did not differ between treatments (P > 0·05 for all). Ingestion of a pea-rice protein blend did not augment postprandial aminoacidemia above pea protein, perhaps attributable to marginal differences in essential amino acid composition. No between-treatment differences in appetite or energy intake responses were apparent, suggesting that the influence of protein ingestion on perceived appetite ratings and orexigenic hormonal responses may not be solely determined by postprandial plasma aminoacidemia.

Natural Plant Materials as a Source of Neuroprotective Peptides.

In many circumstances, some crucial elements of the neuronal defense system fail, slowly leading to neurodegenerative diseases. Activating this natural process by administering exogenous agents to counteract unfavourable changes seems promising. Therefore, looking for neuroprotective therapeutics, we have to focus on compounds that inhibit the primary mechanisms leading to neuronal injuries, e.g., apoptosis, excitotoxicity, oxidative stress, and inflammation. Among many compounds considered neuroprotective agents, protein hydrolysates and peptides derived from natural materials or their synthetic analogues are good candidates. They have several advantages, such as high selectivity and biological activity, a broad range of targets, and high safety profile. This review aims to provide biological activities, the mechanism of action and the functional properties of plant-derived protein hydrolysates and peptides. We focused on their significant role in human health by affecting the nervous system and having neuroprotective and brain-boosting properties, leading to memory and cognitive improving activities. We hope our observation may guide the evaluation of novel peptides with potential neuroprotective effects. Research into neuroprotective peptides may find application in different sectors as ingredients in functional foods or pharmaceuticals to improve human health and prevent diseases.

Simple and eco-friendly fabrication of hempseed protein by one-step low-temperature-induced phase separation and centrifugal removal of oil

Hempseed protein is an emerging plant-derived alternative protein with unmatched nutritional and health benefits. However, the currently available industrial hempseed protein production relies on a defatting step using an organic solvent, hexane with health and environmental risks, which also damages the proteins’ structural and functional properties. In this study, we describe a successful method for the simple and eco-friendly simultaneous extraction of proteins and removal of oil based on the “hydrophilic” properties of hempseed oil. Both hempseed protein isolates (HPIs) extracted from hexane-defatted hempseed flour (HHPI) and non-defatted hempseed flour (NHHPI) exhibited great similarities in protein contents (both >90%), amino acid composition, protein subunits and functional properties (solubility, water retention and foaming). However, NHHPI significantly outperformed HHPI in keeping native structural and some processing properties. NHHPI exhibited a higher percentage of α-helix (44.29%) with lower amount of random coil (15.33%) than HHPI (α-helix 41.71%, random coil 19.07%), higher fluorescence intensity with lower incident wavelength (λmax = 326) than HHPI (incident wavelength λmax = 329). Meanwhile, NHHPI displayed higher surface hydrophobicity (807.01), fat absorption (1.35 g/g) and emulsion activity (2.36 m2/g) as compared to HHPI (743.48, 1.14 g/g, 1.78 m2/g, respectively). These findings highlight the importance of a new defatting method for HPI extraction, which may also be applicable to other oilseed proteins.

Modification of rice protein and its components: Enhanced fibrils formation and improved foaming properties

Plant-derived proteins like rice protein are considered an ideal source for yielding amyloid fibrils due to sustainability and affordability. However, the inherent low solubility of rice protein often restricts its self-assembly capability under common fibrillization protocols. Hence, this study comprehensively investigated the effect of modification on the self-assembly behavior, protein structure and foaming properties of rice protein and its components. The modification facilitated the transformation of α-helix to β-sheet, promoting fibrils formation. All modified proteins, except rice protein, exhibited significantly increased zeta potential values. AFM results revealed that the modified rice protein and globulin fibrils exhibited entangled aggregation behavior, while the glutelin fibril was notably extended, with several micrometers in length. Additionally, modification promoted the aggregation of albumin and prolamin particles to form short and straight fibrils. Amino acid analysis indicated that the content difference of amino acids with different characteristics and the change of aromatic amino acid interaction caused by modification may lead to different self-assembly behavior of the same protein. Furthermore, the foaming capability and stability of most protein fibrils were significantly improved by the modification. These findings provide valuable insights into the regulation of plant-derived protein fibrillation through modification.

Evaluating stability and bioactivity of Rehmannia-derived nanovesicles during storage

Plant-derived nanovesicles (PDNVs) have garnered growing attention in the biomedical field owing to their abundance in plant-derived ribonucleic acids (RNA), proteins, lipids and metabolites. The question about the preservation of PDNVs is a crucial and unavoidable concern in both experiments’ settings and their potential clinical application. The objective of this research was to examine the impact of varying storage temperatures on the stability and bioactivity of Rehmannia-derived nanovesicles (RDNVs). The results showed that RDNVs aggregated after 2 weeks of storage period at 4 °C, and the particle size of some RDNVs gradually increased with time, along with the increase of solution potential. After 2 months of storage, all RDNVs exhibited varying levels of aggregation irrespective of storage temperature. The bioactivities of nanovesicles under different temperature storage conditions revealed a gradual decline in cell proliferation inhibition bioactivity over time, significantly lower than that of freshly prepared RDNVs. In contrast, the preservation of anti-migratory activity in RDNVs was found to be more effective when subjected to rapid freezing in liquid nitrogen followed by storage at − 80 °C, as opposed to direct storage at − 80 °C. These findings suggest that temperature alone may not be sufficient in safeguarding the activity and stability of RDNVs, highlighting the necessity for the development of novel protective agents for PDNVs.

Curcumin-loaded microcapsules with soy and whey protein as wall material: In vitro release, and ex vivo absorption based on the rat small intestine

Plant proteins, serving as an environmentally friendly and cost-effective alternative to animal proteins, have gained widespread usage in encapsulating various bioactive compounds like curcumin. However, understanding how plant protein-based microcapsules compare to those made with animal proteins in terms of disintegration, release, and absorption in the gastrointestinal tract (GIT) remains limited. This study aims to investigate the impact of soy protein isolate (SPI) and whey protein isolate (WPI) as wall materials on the release, stability, and absorption of curcumin. Spray-dried SPI-based microcapsules (SPI–C) exhibited significantly lower encapsulation efficiency (77.1%) and loading efficiency (3.6%) compared to WPI-based microcapsules (WPI–C) (97.6% and 9.6%, respectively). Structural analysis revealed pleated hollow spherical structures for SPI-C and a concave surface with a single-chamber structure for WPI-C. SPI-C demonstrated higher proteolysis (55.8% vs. 44.1%) during in vitro digestion, leading to greater curcumin release ratio (67.9% vs. 59.2%) and digestive stability (97.9% vs. 93.7%) compared to WPI-C. Notably, SPI-C exhibited higher apparent permeability (0.97 × 10−6 cm/s) to the ex vivo rat small intestine than WPI-C (0.44 × 10−6 cm/s). These findings suggest improved gastrointestinal stability and absorption of curcumin encapsulated by SPI, indicating the potential for enhanced utilization of plant-derived proteins in encapsulating bioactive compounds.

Ultrafiltration of Rapeseed Protein Concentrate: Effect of Pectinase Treatment on Membrane Fouling.

Membrane filtration technologies have shown great potential as a gentle and effective method for concentrating and fractionating proteins for food applications. However, the application of this technology to plant-derived protein streams is in its infancy. In this study, an aqueous rapeseed protein concentrate was obtained with wet milling, and its performance during ultrafiltration with two distinct molecular weight cut-offs (10 and 100 kDa) was tested. All rapeseed proteins were retained during filtration. The addition of pectinase during extraction prior to filtration caused important structural modifications to the extract, resulting in increased permeate fluxes, increased carbohydrate permeation and a reduction in irreversible fouling. Lager pore sizes led to more pronounced fouling. FTIR analysis of the spent membranes showed that proteins and lipids are causing irreversible fouling.

AlphaFold-guided redesign of a plant pectin methylesterase inhibitor for broad-spectrum disease resistance

Plant cell walls are a critical site where plants and pathogens continuously struggle for physiological dominance. Here we show that dynamic remodeling of pectin methylesterification of plant cell walls is a component of the physiological and co-evolutionary struggles between hosts and pathogens. A pectin methylesterase (PsPME1) secreted by Phytophthora sojae decreases the degree of pectin methylesterification, thus synergizing with an endo-polygalacturonase (PsPG1) to weaken plant cell walls. To counter PsPME1-mediated susceptibility, a plant-derived pectin methylesterase inhibitor protein, GmPMI1, protects pectin to maintain a high methylesterification status. GmPMI1 protects plant cell walls from enzymatic degradation by inhibiting both soybean and P. sojae pectin methylesterases during infection. However, constitutive expression of GmPMI1 disrupted the trade-off between host growth and defense responses. We therefore used AlphaFold structure tools to design a modified form of GmPMI1 (GmPMI1R) that specifically targets and inhibits pectin methylesterases secreted from pathogens but not from plants. Transient expression of GmPMI1R enhanced plant resistance to oomycete and fungal pathogens. In summary, our work highlights the biochemical modification of the cell wall as an important focal point in the physiological and co-evolutionary conflict between hosts and microbes, providing an important proof of concept that AI-driven structure-based tools can accelerate the development of new strategies for plant protection.

Evaluation of plant-derived biomaterials for the development of tissue-engineered corneal substitutes.

Corneal blindness affects over 10 million patients worldwide. Due to the limited supply of donor corneas and frequent graft failure, bioengineered alternatives are crucial. To overcome drawbacks associated with corneal substitutes from synthetic biomaterials, fabrication from plant-derived biomaterials is a potential alternative. Herein, soy protein and glutenin in combination with different crosslinkers were evaluated for fabrication of corneal substitutes. Optical, mechanical, and biochemical properties of fabricated constructs and control rabbit corneas were evaluated in vitro. Soy protein crosslinked with peroxidase/H202 possessed transparency and mechanical properties comparable to controls, although their water content and biocompatibility were inferior. In contrast, soy protein crosslinked with tannic acid showed similar water content, tensile strength, and biocompatibility as rabbit corneas; however, these constructs displayed significantly lower transparency and higher strain to failure. Finally, glutenin cross-linked using formaldehyde showed excellent transparency, strain to failure, and biocompatibility, however; they exhibited significantly lower water content and tensile strength than controls. This study is the first to establish CIELAB color values for the rabbit cornea, allowing quantitative optical evaluation of tissue-engineered substitutes. Thus, a crosslinking strategy utilizing plant-derived proteins for fabrication of constructs with properties comparable to rabbit corneas is a promising direction for development of tissue-engineered corneal substitutes.

Enhanced enzymatic hydrolysis of lignocellulosic substrate with less-expensive formulation of homemade cellulase cocktails

This study focused on the efficient production of fermentable sugars from high-solids enzymatic hydrolysis of the lignocellulosic substrate, using homemade cellulase preparation (from China company) combined with surfactants, plant-derived proteins, and accessory enzymes. Results show that various non-ionic and ionic surfactants worked together very effectively, resulting in the 48-h glucose yield of enzymatic hydrolysis increasing by 21.4 %, compared with a single surfactant. The surfactant mixture was particularly competitive at a lower enzyme loading and higher solid content of the enzymatic hydrolysis. Many plant-derived proteins were found to be useful in enzymatic hydrolysis. With the optimized mixture of surfactants, plant-derived protein, and accessory enzymes, the homemade cellulase preparation produced 170 g/L of fermentable sugars (∼ 90 % of the yield) from the enzymatic hydrolysis (2 mg/g dried substrate, 20 % (w/v), 72 h), which was promisingly economic and close to the starchy sugar. The homemade cellulase preparation by formulation with various surfactants and plant-derived proteins supplied a feasible solution for the development of a cost-effective enzymatic hydrolysis process.

Effect of protein concentration, pH, and ionic strength on the adsorption properties of rice bran protein concentrates at the oil-water interface

Changes in protein concentration (PC), pH, and ionic strength (IS) influenced the physicochemical, structural, and rheological properties of emulsions made with natural emulsifiers. This study used rice bran protein concentrates (RBPC) to create RBPC-stabilized emulsions (RBP-E) and examined their emulsifying function by changing protein concentration, ionic strength, and pH. The results showed that increasing the PC resulted in a decrease in particle size, which caused the creaming rate and viscosity of RBP-E to increase, leading to the depletion flocculation phenomenon. Incorporating PC into the emulsion system improved adsorbed protein performance in particular pH, which positively correlates to the reduction of emulsion capacity in 3 % PC at neutral conditions. The introduction of IS decreased viscosity, enhanced solubility, and increased protein adsorption, thereby improving emulsion stability within a 3 % protein concentration. FTIR analysis revealed that as the pH shifted from 3 to 7, the α-helical structures increased, while β-sheet and β-turn structures reduced compared to untreated protein, decreasing surface hydrophobicity. Incorporating 1 % PC improved RBP-E performance at pH 7 and 0.5 M, while 2 % PC optimized emulsion capacity at 0.25 M and pH 3. Increasing PC from 1 % to 2 % improved emulsion stability and capacity by 35.4 and 34.4 %, respectively, at 0 M, particularly at pH 5. Therefore, the study concludes that IS, pH, and PC affect the adsorption of plant-derived protein at the O/W interface and enhance the emulsification capabilities of RBPC and the stability of RBP-stabilized emulsions. RPB-E can potentially be used in cake batter, ice cream mix, and margarine premix, a sustainable substitute for animal-based proteins.

Exploring plant-derived phytochrome chaperone proteins for light-switchable transcriptional regulation in mammals

Synthetic biology applications require finely tuned gene expression, often mediated by synthetic transcription factors (sTFs) compatible with the human genome and transcriptional regulation mechanisms. While various DNA-binding and activation domains have been developed for different applications, advanced artificially controllable sTFs with improved regulatory capabilities are required for increasingly sophisticated applications. Here, in mammalian cells and mice, we validate the transactivator function and homo-/heterodimerization activity of the plant-derived phytochrome chaperone proteins, FHY1 and FHL. Our results demonstrate that FHY1/FHL form a photosensing transcriptional regulation complex (PTRC) through interaction with the phytochrome, ΔPhyA, that can toggle between active and inactive states through exposure to red or far-red light, respectively. Exploiting this capability, we develop a light-switchable platform that allows for orthogonal, modular, and tunable control of gene transcription, and incorporate it into a PTRC-controlled CRISPRa system (PTRCdcas) to modulate endogenous gene expression. We then integrate the PTRC with small molecule- or blue light-inducible regulatory modules to construct a variety of highly tunable systems that allow rapid and reversible control of transcriptional regulation in vitro and in vivo. Validation and deployment of these plant-derived phytochrome chaperone proteins in a PTRC platform have produced a versatile, powerful tool for advanced research and biomedical engineering applications.

Plant protein fibers obtained by microfluidic spinning technology: An insight into the fabrication, characterization, and digestive characteristics

Although protein-based biomimetic fibers are available, green and inexpensive protein-based fibers remain a challenge to develop. Herein, a microfluidic chip was designed to prepare protein-based fibers using cellulose nanofibers and various plant-derived proteins, including wheat gluten, zein, soy protein, pea protein, and rice bran protein. Furthermore, a comprehensive elucidation of the plant protein fiber formation mechanism was conducted. The results showed that plant protein fibers prepared by microfluidic spinning had smooth surfaces, strong mechanical properties, high thermal stability and antioxidative activity, good digestibility, and low sensitization. Additionally, the strong hydrodynamic shear force produced during microfluidic spinning changed the secondary structure of the protein, which promoted the binding of protein molecules to cellulose nanofibers, thus enhancing the molecular orientation of both protein and nanofiber. Consequently, this study may facilitate the development of natural, environmentally friendly, and functional protein-based fibers.

An Appraisal of Nonmicrobial Biostimulants' Impact on the Productivity and Mineral Content of Wild Rocket (Diplotaxis tenuifolia (L.) DC.) Cultivated under Organic Conditions.

Modern agriculture urgently requires viable alternatives to synthetic chemical substances, such as pesticides and fertilizers, to comply with new and stringent international regulations and meet the growing demands of consumers who prefer chemical-free food. Consequently, organic agriculture has garnered increasing interest over time. To compensate for yield reduction resulting from opting out of the use mineral fertilizers, research has focused on the use of biostimulants to sustain the productivity of horticultural crops. To this end, a greenhouse experiment was conducted to assess the effects of three nonmicrobial biostimulants (a plant extract, vegetable protein hydrolysate, and a seaweed extract) and an untreated control on the production and mineral content of wild rocket (Diplotaxis tenuifolia (L.) DC.) cultivated under organic conditions and harvested three times during the growth cycle. In general, the nitrate content, which defines the commercial quality of wild rocket, was not influenced by the application of biostimulants. At each harvest, the application of biostimulants resulted in improved production performance, although this was not always accompanied by an increase in mineral content. Specifically, the best results were obtained with the use of plant-derived protein hydrolysate and plant extract, which led to an improvement in total yield of 32.1% and 27.2%, respectively compared to that of control plants. These results reconfirm that biostimulants represent a valid and indispensable tool for organic growers.

Addressing the safety of new food sources and production systems.

New food sources and production systems (NFPS) are garnering much attention, driven by international trade, changing consumer preferences, potential sustainability benefits, and innovations in climate-resilient food production systems. However, NFPS can introduce new challenges for food safety agencies and food manufacturers. Most food safety hazards linked to new foods have been identified in traditional foods. However, there can be some food safety challenges that are unique to new foods. New food ingredients, inputs, and processes can introduce unexpected contaminants. To realize the full potential of NFPS, there is a need for stakeholders from governments, the food industry, and the research community to collectively work to address and communicate the safety of NFPS products. This review outlines known food safety hazards associated with select NFPS products on the market, namely, plant-derived proteins, seaweeds, jellyfish, insects, microbial proteins, as well asfoods derived from cell-based food production, precision fermentation, vertical farming, and 3D food printing. We identify common elements in emerging NFPS regulatory frameworks in various countries/regions. Furthermore, we highlight current efforts in harmonization of terminologies, use of recent scientific tools to fill in food safety knowledge gaps, and international multi-stakeholder collaborations to tackle safety challenges. Although there cannot be a one-size-fits-all approach when it comes to the regulatory oversight for ensuring the safety of NFPS, there is a need to develop consensus-based structured protocols or workflows among stakeholders to facilitate comprehensive, robust, and internationally harmonized approaches. These efforts increase consumers' confidence in the safety of new foods and contribute toward fair practices in the international trade of such foods.

Optimizing Apricot Yield and Quality with Biostimulant Interventions: A Comprehensive Analysis

Biostimulant products are recognized for their ability to improve the agronomic parameters of plants and the qualitative and nutraceutical parameters of fruits and confer greater resistance to plants under abiotic and biotic stress conditions. In our study, we tested three different biostimulants on cultivar “Lady Cot” apricot plants: animal-derived protein hydrolysate, plant-derived protein hydrolysate, and one based on algae to evaluate their effects on improving the agronomic parameters of plants and fruit quality. The product that stood out for providing positive effects was the protein hydrolysate-based product, which increased plant production by 53.80% and yield efficiency by 56.38%. At the same time, it also increased the fruit’s diameter growth by approximately 8.3%, showing positive effects on fruit weight as well. The animal-derived protein hydrolysate also reduced acidity by 13.8% and showed a significant increase compared to the control in terms of total polyphenols. Additional research is scheduled to validate these results and ascertain which categories of biostimulant products are most effective in enhancing the agronomic, qualitative, and sensory characteristics of other apricot cultivars.

Preharvest calcium application boosts the biostimulatory effect of protein hydrolysate by improving the postharvest life of gerbera cut flower

Among the various categories of plant biostimulants currently available on the market, protein hydrolysates, primarily composed of a heterogeneous mixture of peptides and amino acids, have gradually gained prominence. Nevertheless, the positive effects of these products on the production and longevity of cut flowers are still not well-explored. The purpose of this research was thus to fill this gap by assessing the impacts of a plant-derived protein hydrolysate, with and without the addition of calcium (PH and PH+Ca), on the growth, quality, and vaselife of two cultivars of gerbera with different pigmentation (Brunello and Tommy, red and yellow, respectively). Regardless of cultivar, foliar application of PH improved growth, flower production, absorption of key nutrients, and photosynthetic performance, compared to the control. On the other hand, the PH+Ca treatment exhibited the best results during vaselife. For both cultivars, the application of PH+Ca increased the durability of gerbera flowers, reducing the weight loss by an average of 19 % on day 10 compared to untreated flowers. Although cultivar-dependent, the positive effects of the PH+Ca biostimulant were also observed on petal pigmentation during vase life. For the Tommy cultivar, for instance, the Chroma values of treated flowers remained unchanged during the post-harvest period, unlike what was observed for untreated flowers. Therefore, considering the positive effects resulting from the use of PH and PH+Ca on gerbera, it would be interesting to further investigate the use of biostimulants in floriculture to increase the sustainability of the sector and especially with regard to cut flower production, without reducing or even improving the performance that is conventionally achieved.