Lupin Protein Research Articles

Encapsulation of yarrow phenolic compounds in lupin protein nanoemulsions increases stability during gastrointestinal transit and delivery in the colon

This study aimed to assess the behaviour of phenolic compounds from yarrow extract encapsulated in nanoemulsions during in vitro gastrointestinal digestion. Oil-in-water nanoemulsions were developed using grape seed oil and lupin protein (LPI) as oil phase and emulsifier, respectively. The use of 6 % LPI including 1 mg/mL of yarrow extract resulted in nanoemulsions with a homogeneous particle size distribution (200 nm) and an encapsulation efficiency of 85.6 %. During in vitro gastrointestinal digestion, most of the phenolics remained encapsulated, being protected from degradation. The in vitro bioavailability of the encapsulated phenolics was measured using a cell co-culture model (Caco-2/HT-29MTX). In this regard, nanoemulsions did not increase the bioavailability of yarrow phenolics, instead, they promoted their access to the colon. Finally, the antiproliferative activity was determined in Caco-2 cells, observing that the apical fraction inhibited cancer cells, indicating the bioefficacy of the non-absorbed phenolics.Thus, this study underscores the potential of LPI-stabilized nanoemulsions as a vehicle for protecting and delivering yarrow phenolics to the colon.

Inside Cover, Volume 141, Issue 42

The cover image is based on the Article Impact of oxidized sucrose as a bio‐based crosslinker on thermoformable films made from lupin protein isolate (Lupinus angustifolius L.) by Maximilian Maidl et al., https://doi.org/10.1002/app.56109. image

Lupine protein enzymatic hydrolysates obtained in a simultaneous extraction-hydrolysis process as foaming agents

In most experimental protocols described in the literature, a plant seed protein extraction and its enzymatic hydrolysis are separated. A simultaneous extraction and hydrolysis process was proposed as a much simpler and less energy-demanding alternative. The enzymatic lupine protein hydrolysates obtained in the simultaneous process were tested for their ability to produce and maintain foams, showing that the proposed process simplification did not compromise foaming properties of the hydrolysates. Two animal-sourced (trypsin and pancreatin) and one plant-sourced proteolytic enzyme (papain) were employed at variable specific enzymatic activity, ranging from 60 nkat/g protein (for pancreatin) to 189 μkat/g protein (for papain) and temperatures (37 °C, 50 °C and 65 °C, respectively). The enzymatic hydrolysis improved foaming properties of the extracts, both in the subsequent (when the extraction and the hydrolysis were performed in separated steps) and simultaneous (when the extraction and hydrolysis were taking place simultaneously) modes: foam capacity (FC) increased from ∼100 % to ∼270 % (for papain) with >50 % initial foam volume retained after 10 min. The obtained hydrolysates could be employed to provide a foaming activity of cosmetic, pharmaceutical or food products; when using the plant-sourced papain - also of the fully vegan ones.

PH-induced conformational changes of lupin protein-pectin mixtures and its effect on air-water interfacial properties and foaming functionality

Lupin protein isolate (LPI) has high nutritional value and good foaming properties around neutral pH; however, its functionality becomes poor at acidic pH, due to reduced protein solubility. The addition of pectin to LPI can increase its solubility at acidic pH and hence improve protein functionality. Here, we investigated the air-water interfacial and foaming properties of LPI-pectin (1:1) mixtures at pH 3.5–7.0. We used interfacial shear and dilatational rheology, characterized the air-water interfacial microstructure with AFM of Langmuir-Blodgett films, and linked the results to the foaming properties of the LPI-pectin mixtures. Based on the phase diagram, LPI and pectin formed co-soluble mixtures at pH 6.0 and 7.0, while LPI-pectin electrostatic complexes were formed at pH 3.5 and 4.0. In the co-soluble mixtures, proteins diffused faster towards the air-water interface than the electrostatic complexes, due to smaller particle sizes of the proteins. Their air-water interfaces showed distinct differences with respect to microstructure and mechanical properties. The interfaces stabilized by co-soluble mixtures were dominated by protein aggregates, leading to weaker interfaces in response to shear and dilatational deformation, while the complexes formed thicker and denser polymeric air-water interfaces that were stiffer and more solid-like. As a result, the complex-stabilized foams were more stable than those stabilized with co-soluble mixtures. Findings from this study indicate that soluble LPI-pectin complexes formed at pH 3.5 and 4.0 were more efficient in improving interfacial and foaming properties of LPI than the co-soluble mixtures at pH 6.0 and 7.0, which can be used to tailor the properties of acid aerated products stabilized by LPI.

Impact of oxidized sucrose as a bio‐based crosslinker on thermoformable films made from lupin protein isolate (Lupinus angustifolius L.)

AbstractThis study investigates the effect of oxidized sucrose (OS) on selected functional properties of cast films from lupin protein isolate (LPI). LPI with a protein content larger than 0.9 g g−1 was obtained by alkaline extraction and isoelectric precipitation from bitter narrow‐leaved lupins (Lupinus angustifolius L.). OS was synthesized by vicinal diol cleavage using sodium periodate and was successfully characterized by Fourier‐transform infrared‐, 1H‐nuclear magnetic resonance spectroscopy, and aldehyde titration. Films were produced from heated (85°C, 30 min), alkaline (pH 10), aqueous solutions of LPI (0.1 mL−1), glycerol (300 mg g−1 of LPI) and OS (25, 50, 75, and 100 mg g−1 of LPI). The effect of covalent crosslinking between OS and protein chains was studied by investigating mechanical properties, moisture content, total soluble matter, water vapor permeability, and protein solubility for all films. LPI films produced with the addition of OS showed increased mechanical performance as the tensile strength was increased from 3.5 up to 9.3 MPa and elongation at break values could be raised from 118% to 176%. Taken together with the facts that these films are thermoformable and show improved wet strength compared with control films, make them promising materials for sustainable packaging and short‐term applications in agriculture and forestry.

Impact of Seed Germination on the Physicochemical Properties of Lupin Flours and the Physicochemical and Techno-functional Properties of Their Protein Isolates

AbstractNowadays , lupin seeds have emerged as a novel and valuable source of proteins representing a sustainable alternative to current raw materials of plant-based proteins, such as soybean. In this regard, lupin demonstrates superior adaptation to the Mediterranean climate with improved tolerance to water stress. However, its suitability for human consumption is limited due to the presence of anti-nutritional and anti-technological factors, including alkaloids, polyphenols, tannins, and lipids, which can have adverse nutritional consequences and/or impact on the purity and yield of protein extraction. In this study, the Lupinus luteus seeds were germinated for 1, 2, 3, and 6 days and the effect of germination on the anti-nutritional and anti-technological factors of flours and derived protein isolates was analyzed. Additionally, changes on techno-functional properties of lupin protein isolates were also studied. Results showed that prolonged germination decreased fat content whereas antioxidant activity, polyphenols, saponin, and alkaloid content of flours increased. However, alkaloids were completely removed during protein extraction. Furthermore, protein isolates derived from germinated seeds exhibited higher water and oil absorption capacities, as well as improved foaming and emulsifying capabilities in comparison to isolates from non-germinated seeds. Nevertheless, prolonged germination periods were associated with diminished foam and emulsion stability. Therefore, germination of lupin seeds for no longer than 3 days should be recommended in order to minimize the levels of anti-nutritional and anti-technological factors, while enhancing techno-functional properties of the isolate.

Extraction of water-soluble polysaccharides from lupin beans and their function of protein dispersion and stabilization under acidic conditions

In the current environment whereby new sources of proteins are extracted from plant material, it is also important to study the potential use of the resulting side streams. Although a number of studies have been conducted on various polysaccharides extracted from plant raw material, a polysaccharide fraction extracted from lupin bean is yet to be explored, in spite of the emerging interest in this crop as a source of food ingredients. In this work lupin soluble polysaccharide (LuPS) was obtained with a recovery as high as 46 % by extraction at pH 8, 120 °C, for 90 min. This fraction, named LuPS-8, was composed of a mostly linear pectic polysaccharide with a weight average molecular mass of 6608 kg/mol, and containing 71.0 % galactose, with minor amounts of arabinose (16.0 %), glucuronic acid 4.6 %, and galacturonic acid 4.1 %. When added to an acid milk dispersion, LuPS-8 improved its dispersibility, providing storage stability against sedimentation over a wider pH range than a HM-pectin reference, between 3.6–4.4. This research demonstrated the potential for upcycling of a side stream of lupin protein production, by the creation of value-added novel functional polysaccharide.

Mayonnaise produced by ultrasound-assisted emulsification using plant-based and “clean label” ingredients

Recently, nanoemulsions have gained significant attention for their improved stability and their wide range of potential uses in the food industry. This study aimed to create a novel type of mayonnaise with 23.6% (w/w) of oil using ultrasound-assisted emulsification for 6 min to incorporate lupin protein (3.4%, w/w) in the nanoemulsion stabilized by a combination of citrus fibre (2.5%, w/w) and psyllium (0.3%, w/w) or modified starch (3.0%, w/w). Nanoemulsions were produced using a cold-water bath and characterised by their stability and structural properties and used for the production of the mayonnaise. Results showed that the use of lupin protein led to stable nanoemulsions for 50 days stored at 4 °C. The smallest mean droplet size for lupin protein was 505.5 ± 43.5 nm and a polydispersity value 0.434 ± 0.045. Then, the selected nanomulsion was used to produce mayonnaise at room temperature. Mayonnaise were characterised in terms of its rheological and morphological properties, and through sensorial evaluation. The texture of the plant-based formulations was very close to one commercial mayonnaise, with similar resistance to deformation. The consistency (k) and flow index (n) were similar between samples and indicate that the samples are viscous due to the considerable value of k. A sensory analysis with a panel of consumers showed that the proposed formulations had a similar organoleptic profile compared to the benchmark sample. However, the tests showed that formulation developed with fibres had a slightly lower overall liking score.Ultrasound seems to be an effective strategy for developing plant-based nanoemulsions, foreseeing their use in the production of mayonnaise.

Use of supercritical CO2 to improve the quality of lupin protein isolate

Lupins are an excellent source of protein which can be used to obtain protein isolates with potential use in the food industry. Some studies use supercritical CO2 (SC-CO2) to defat legume flours, but no study analyzes the effect of applying this technology directly to the protein isolate. This article has proposed the use of SC-CO2 to improve lupin protein isolate (LPI) quality. SC-CO2 increased the LPI purity while reducing oil and other antitechnological factors (saponins and polyphenols). The treatment significantly improved the LPI color due to the elimination of the lipid fraction and lipophilic pigments (carotenoids). No changes in amino acid contents or chemical score were observed due to the SC-CO2. Finally, the treatment improved or did not affect the main LPI technofunctional properties. Therefore, SC-CO2 is a promising technique to enhance the quality of protein isolates, without affecting or improving their functional properties.

Development and Evaluation of Vegan Yogurts and Sour Milk Alternatives from White Lupin (Lupinus albus L.)

Cow milk allergy (CMA) triggers a clinically abnormal immunological response to cow milk proteins. To address this issue, extensive studies have explored milk alternatives from various animal and plant sources. This study introduces a method for producing white lupin milk, resulting in fermented dairy-like products (vegan yogurt and sour milk alternatives). Four commercial yogurt cultures, including two mesophilic (CHN-11, CHN-22) and two thermophilic (YC-380, YC-X11) mixed bacterial cultures, were tested, with thermophilic ones yielding superior sensory outcomes for lupin-based yogurt alternatives. Incorporating inulin (2%) enhanced sensory appeal, particularly evident in strawberry and peach-flavoured variants, which achieved sensory scores comparable to cow milk yogurts. Furthermore, white lupin-based yogurts demonstrated superior water-holding capacity (up to 47.11 g/100 g in comparison with 42.35 g/100 g measured for cow milk yogurt), influencing texture and mouthfeel. They also exhibited favourable fatty acid profiles, notably rich in beneficial unsaturated fatty acids such as linoleic and linolenic acid (up to 10.15% and 8.43%, respectively), indicating potential health benefits. Sensory evaluation underscored the impact of starter cultures on product attributes, with certain cultures yielding more favourable results. In conclusion, white lupin emerges as a promising alternative protein source with the potential to produce high-quality dairylike products. While white lupin-based products hold promise as functional foods for individuals with specific dietary needs, further research is necessary to address potential allergenic concerns associated with white lupin proteins.

Heat-induced lupin-whey protein emulsion-filled gels: Microstructural and rheological insights

This work investigates the rheological properties of lupin-whey emulsion-filled gels (EFGs) formed using a pilot scale plate heat exchanger. Samples were prepared with either lupin, whey, or a lupin-whey stabilized emulsion, mixed in a whey protein continuous phase. While whey protein in the continuous phase was mainly responsible for the formation of a primary gel network, differences were observed depending on the droplet-whey protein matrix interactions. Full or partial replacement of interfacial proteins with lupin proteins resulted in softer, more ductile gels. Amplitude sweeps showed that the structure was not only affected by the interactions between the droplets and the continuous network, but also by the droplet distribution within the matrix. This work demonstrates the importance of fine tuning the interactions and the distribution of oil droplets within the gel, as these properties will lead to structural heterogeneity at the micro-scale, causing profound differences in the rheological properties. Finally, continuous heating led to stiffer, more particulate gels compared to quiescent conditions, but similar mechanisms underpinned gel formation. Thus, it is demonstrated that the design of the interactions can be screened using an in situ rheometer, although the rheological properties are affected by the shear effect of the plate heat exchanger.

Characteristics of lacto-fermented whey, milk, hemp and lupine proteins

Lacto-fermentation of proteins not only improves their biological and functional value but also causes nutritional and biochemical alteration as well as the formation of undesirable compounds, which needs to be monitored. The aim of this study was to evaluate the changes in whey, milk, hemp and lupine protein characteristics (acidity, microbiological parameters, color characteristics, free amino acid (AA) profile, biogenic amine (BA) and gamma-aminobutyric acid (GABA) concentrations) during lacto-fermentation with Pediococcus acidilactici LUHS29 and Pediococcus pentosaceus LUHS183 strains. Greater lactic acid bacteria growth and drop in pH was found in fermented plant proteins than in the animal ones. The contents of free essential and non-essential AAs were increased in all proteins fermented with the LUHS29 strain. This strain also possessed a greater GABA-producing ability in all fermented proteins. Compared to plant proteins, fermented animal proteins exhibited less GABA and total BA contents. Fermented hemp proteins had the highest BA content (on average, 215.8 mg/kg), while milk proteins fermented with LUHS183 for 48 h had the lowest value. P. acidilactici LUHS29 strain could be beneficial for a notable enhancement of AA and GABA in proteins, while the monitoring of BA synthesis in fermented hemp proteins needs specific attention.

Interfacial and foaming properties of soluble lupin protein isolates: Effect of pH

Lupins are rich in proteins (∼40%) and fibers (∼40%), and have been widely used for animal feed, but limitedly for human consumption due to the presence of alkaloids. Due to their high protein content, lupins have a high potential to be used as protein sources in diverse food manufacturing processes, including emulsion and foam stabilization. However, the interfacial properties of lupin protein isolates (LPI), especially their performance at different pH values, are not well understood so far. Here, we systematically investigated the air-water interfacial and foaming properties of the soluble fraction of LPI at pH 7.0, pH 6.0, pH 4.0, and pH 3.5. We observed that LPI at pH 4.0 (LPI-4) and pH 3.5 (LPI-3.5) adsorbed faster at the air-water interface than at pH 7.0 (LPI-7) and pH 6.0 (LPI-6) due to a smaller particle size and higher surface hydrophobicity of LPI-4 and LPI-3.5. This resulted in a higher foam overrun of LPI-4 and LPI-3.5 (300% and 331%, respectively). The air-water interfaces formed by LPI at different pH values were dramatically different in terms of interfacial structure and mechanical properties. LPI-4 and LPI-3.5 formed stiff and solid-like interfaces, leading to higher foam stability. In contrast, for LPI-7 there were clearly more protein aggregates at the interface, and this structure was weaker and less stretchable in response to shear and dilatational deformation, causing lower foam stability. LPI-6 also showed weaker air-water interfaces and thus formed less stable foams. Overall, LPI at acid pH (3.5 and 4) has a better performance in foam stabilization than at a pH close to neutral (6 and 7). Our results suggest that LPI can be potentially used as a plant-based clean-label additive in the production of foam-based food products in acidic environments.

Enhancing the Retention and Oxidative Stability of Volatile Flavors: A Novel Approach Utilizing O/W Pickering Emulsions Based on Agri-Food Byproducts and Spray-Drying.

Spray-drying is a commonly used method for producing powdered flavors, but the high temperatures involved often result in the loss of volatile molecules. To address this issue, our study focused on a novel approach: developing O/W Pickering emulsions with agri-food byproducts to encapsulate and protect D-limonene during spray-drying and storage. Emulsions formulated with lupin hull, lupin-byproduct (a water-insoluble protein-fiber byproduct derived from the production of lupin protein isolate), and camelina press-cake were subjected to spray-drying at 160 °C. The results revealed that these emulsions exhibited good stability against creaming. The characteristics of the dry emulsions (powders) were influenced by the concentration of byproducts. Quantitative analysis revealed that Pickering emulsions enhanced the retention of D-limonene during spray-drying, with the highest retention achieved using 3% lupin hull and 1% camelina press-cake. Notably, lupin-stabilized emulsions yielded powders with enhanced oxidative stability compared to those stabilized with camelina press-cake. Our findings highlight the potential of food-grade Pickering emulsions to improve the stability of volatile flavors during both processing and storage.

Plant and animal protein mixed systems as wall material for microencapsulation of Mānuka essential Oil: Characterization and in vitro release kinetics

Combination of plant and animal protein diet is becoming a valuable source of nutrition in the modern diet due to the synergistic functional properties inherent in these protein complexes. Moreover, the synergy between animal and plant proteins can contribute to the high stability and improved solubility of the encapsulated bioactive ingredients (e.g., essential oils). Therefore, the study was designed to evaluate the plant (pea protein (PP) and lupine protein (LP)) and animal protein (whey protein, WP) mixed systems as a wall material for microencapsulation of mānuka essential oil, as an example of bioactive compound. Moreover, physicochemical properties and in vitro release profile of encapsulated mānuka essential oil were studied. Mānuka essential oil microcapsules exhibited low moisture content (5.3–7.1 %) and low water activity (0.33–0.37) with a solubility of 53.7–68.1 %. Change in wall material ratio significantly affected the color of microcapsules, while microcapsules prepared with 1:1 protein/oil ratio demonstrated a high encapsulation efficiency (90.4 % and 89.4 %) for protein mixed systems (PP + WP and LP + WP), respectively. Microcapsules further showed low values for lipid oxidation with a high oxidative stability and antioxidant activity (62.1–87.0 %). The zero order and Korsmeyer–Peppas models clearly explained the release mechanism of encapsulated oil, which was dependent on the type and concentration of the protein mixed used. The findings demonstrated that the protein mixed systems successfully encapsulated the mānuka essential oil with controlled release and high oxidative stability, indicating the suitability of the protein mixed systems as a carrier in encapsulation and application potential in development of encapsulated functional foods.

Drivers of the In-Mouth Interaction between Lupin Protein Isolate and Selected Aroma Compounds: A Proton Transfer Reaction-Mass Spectrometry and Dynamic Time Intensity Analysis.

Plant proteins often carry off-notes, necessitating customized aroma addition. In vitro studies revealed protein-aroma binding, limiting release during consumption. This study employs in vivo nose space proton transfer reaction-time-of-flight-mass spectrometry and dynamic sensory evaluation (time intensity) to explore in-mouth interactions. In a lupin protein-based aqueous system, a sensory evaluation of a trained "green" attribute was conducted simultaneously with aroma release of hexanal, nonanal, and 2-nonanone during consumption. Results demonstrated that enlarging aldehyde chains and relocating the keto group reduced maximum perceived intensity (Imax_R) by 71.92 and 72.25%. Protein addition decreased Imax_R by 30.91, 36.84, and 72.41%, indicating protein-aroma interactions. Sensory findings revealed a perceived intensity that was lower upon protein addition. Aroma lingering correlated with aroma compounds' volatility and hydrophobicity, with nonanal exhibiting the longest persistence. In vitro mucin addition increased aroma binding four to 12-fold. Combining PTR-ToF-MS and time intensity elucidated crucial food behavior, i.e., protein-aroma interactions, that are pivotal for food design.

A lupin protein hydrolysate protects the central nervous system from oxidative stress in WD-fed ApoE-/- mice.

Oxidative stress plays a crucial role in neurodegenerative diseases like Parkinson's and Alzheimer's. Studies indicate the relationship between oxidative stress and the brain damage caused by a high-fat diet. It is previously found that a lupin protein hydrolysate (LPH) has antioxidant effects on human leukocytes, as well as on the plasma and liver of Western diet (WD)-fed ApoE-/- mice. Additionally, LPH shows anxiolytic effects in these mice. Given the connection between oxidative stress and anxiety, this study aimed to investigate the antioxidant effects of LPH on the brain of WD-fed ApoE-/- mice. LPH (100 mg kg-1) or a vehicle is administered daily for 12 weeks. Peptide analysis of LPH identified 101 amino acid sequences (36.33%) with antioxidant motifs. Treatment with LPH palliated the decrease in total antioxidant activity caused by WD ingestion and regulated the nitric oxide synthesis pathway in the brain of the animals. Furthermore, LPH increased cerebral glutathione levels and the activity of catalase and glutathione reductase antioxidant enzymes and reduced the 8-hydroxy-2'-deoxyguanosine levels, a DNA damage marker. These findings, for the first time, highlight the antioxidant activity of LPH in the brain. This hydrolysate could potentially be used in future nutraceutical therapies for neurodegenerative diseases.

Improving functional properties of lupin protein by physical modification: high pressure homogenisation

SummaryAqueous dispersions of commercially produced lupin protein isolate with pH 5 and 9 were treated using high pressure homogenisation (HPH) at 25–200 MPa with one to ten homogenisation cycles. Particle size, zeta potential, solubility, molecular weight and rheological properties were analysed. HPH reduced the particle size for lupin protein at pH 5 from 54 to 5 μm and from 14 to <2 μm at pH 9 at 25–100 MPa. However, at 200 MPa, the particle size had less reduction. HPH did not have any significant impact on the zeta potential where it was maintained at −13 mV for pH 5 and −25 mV for pH 9. After HPH, solubility increased significantly for both pH 5 and 9 lupin protein samples. However, prolonged homogenisation decreased solubility. HPH impacted the viscosity of lupin protein at pH 5 and 9, depending on pressure and homogenisation cycles. The highest viscosity (~10 Pa.s) was achieved at 200 MPa with 10 passes. HPH increased the loss modulus where the viscoelastic properties were improved for both pH 5 and 9 at 200 MPa. The storage modulus profile indicated that HPH improved the gelling properties of lupin protein both at pH 5 and 9 at 200 MPa.

Lupin protein-stabilized oil droplets contribute to structuring whey protein emulsion-filled gels

This work aimed to understand the role of lupin protein or mixed lupin-whey protein stabilized oil droplets on the texture and microstructure of a heat-induced whey protein gel. Protein-stabilized emulsions were compared to surfactant-stabilized emulsions to investigate the potential of their interfacial interactions to impart unique structures in the filled gels. The structure development was followed in situ using rheology and the final heat-induced gels were characterized by small and large amplitude oscillatory rheology and confocal microscopy. The development of the gel modulus as well as the final gel properties were linked to the type of interactions between the whey protein matrix and the protein adsorbed at the oil interface. The final gels were selectively dissolved in various buffers, and the results showed that replacing interfacial whey protein with lupin protein resulted in a reduced amount of disulfide bridges, explaining the softer gel in the lupin containing gels compared to those with whey protein. Non-covalent interactions were the main forces involved in the formation of actively filled droplets in the gel network. This work demonstrated that by modulating the interfacial composition of the oil droplets, differing gel structures could be achieved due to differences in the protein–protein interactions between the continuous and the interfacial phase. There is therefore potential for the development of innovative products using lupin-whey protein mixtures, by careful control of the processing steps and the matrix composition.

Seeking the best alternatives: A systematic review and meta‐analysis on replacing fishmeal with plant protein sources in carnivorous fish species

AbstractThe price of fishmeal (FM) has been increasing continuously due to the expansion of the gap between its stable production and rising demand. Therefore, plant protein sources are widely applied in the aquaculture industry to accomplish the protein requirement of farmed fish species. However, the massive number of results produced under various experimental conditions appended challenges for comprehensive summarization and comparison of the effects of plant protein sources on carnivorous fish species. Thus, a systemic review and meta‐analysis were conducted to compare the impacts of various plant protein sources on growth, feed utilization efficiencies, blood lipid, and liver health of representative carnivorous species. Supported by the data from 256 articles, our results indicated that Atlantic salmon, African catfish, Black seabass, and Hybrid striped bass were better at utilizing plant protein sources than Grouper and Japanese seabass. Cottonseed and lupin proteins were promising protein alternatives, while rapeseed showed significant growth suppression effects for these carnivorous fish species. Besides, deep processing methods such as fermentation and enzymolysis alleviated undesirable consequences effectively when less than half of FM was replaced by plant protein sources. Moreover, the optimal plant protein sources are discussed for each fish species. Overall, this article depicts the impact patterns of major plant protein sources on carnivorous farmed fish species and lays a solid foundation for further investigation on mechanisms for improving plant protein utilization.