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The proteins from two conventionally (CC1 and CC2) and one organically cultivated (OC) hempseed samples were extracted (by alkaline solubilization followed by isoelectric precipitation) and compared in terms of their physicochemical, digestibility and in vitro bioactivity properties. The OC hempseed had higher total protein and lower nonprotein nitrogen content. Protein extracts showed bimodal particle size distributions, with OC showing the smallest and CC1 the largest mean particle diameter (d(0.5)), i.e., 89.0 and 120.0 µm, respectively. Chromatographic analysis showed similar protein profiles for all three protein extracts. The protein extracts were subjected to in vitro simulated gastrointestinal digestion (SGID). Degree of hydrolysis (DH) measurement showed that the highest extent of digestion upon SGID was associated with CC1 (11.0 ± 1.5%), which also had the lowest in vitro antioxidant activity. Only the OC and OC digested samples had lipase inhibitory activity. The results indicate that the cultivation method impacted the composition, physicochemical, digestibility, and biofunctional properties of hempseed proteins. [ABSTRACT FROM AUTHOR]

The search for allergy friendly texturized vegetable proteins (TVP) has prompted the use of novel protein sources over conventional wheat and soy proteins. Hempseed protein (HP) offers promising nutritional characteristics. This work assessed the effect of feed moisture content (FMC) and screw rotation speed (SRS) on the textural, functional and colour characteristics of texturized HP. The HP was extruded using a co-rotation twin screw extruder at 30–60% FMC and 200–400 rpm SRS. Results showed that significant differences were observed from FMC, SRS and the interaction of FMC and SRS on the product expansion index, integrity index, water and oil absorption capacity (WAC and OAC), some texture profile parameters and colour characteristics. Decreasing FMC and increasing SRS tended to increase the texturization index, expansion index, WAC, OAC, integrity index and texture profile characteristics but decrease density, L* and b* values. These results contribute to our understanding of the properties of texturized HP which are important for application in food industry. [ABSTRACT FROM AUTHOR]

There has been an increasing interest on the utilization of industrial hempseed as a potential food ingredient with health-promoting properties. The objective was to produce hempseed protein (HPI) hydrolysates with antioxidant and anti-inflammatory properties. HPI was isolated from hempseed hearts and hydrolyzed by Alcalase (A-HPI) and bromelain (B-HPI). Hydrolysates were characterized and tested for their antioxidant and anti-inflammatory properties. A-HPI has better inhibitory activity than B-HPI in lipopolysaccharide-induced inflammation in macrophages by reducing nitric oxide, interleukin-6, tumor necrosis factor-α production. On the other hand, the ORAC values of both hydrolysates are similar while B-HPI scavenged DPPH radical stronger than A-HPI. Our results showed the potential of HPI hydrolysates to serve as natural antioxidant food ingredients with health promoting properties by inhibiting aberrant inflammation.

The rising demand for sustainable proteins leads to increased interest in plant proteins like hemp protein (HP). However, commercial HP's poor functionality, including heat aggregation, limit its use. This study explored the heat-induced interactions of hemp protein particles (HPPs) with milk proteins, specifically whey proteins and caseins. Using various analysis techniques—static light scattering, TEM, SDS electrophoresis, surface hydrophobicity, and free sulfhydryl content—results showed that co-heating HPPs with whey protein isolate (WPI) or sodium caseinate (NaCN) at 95 °C for 20 min reduced HPPs aggregation. HPPs/WPI particles had a d 4,3 of ∼3.8 μm, while HPPs/NaCN were ∼1.9 μm, compared to ∼27.5 μm for HPPs alone. SDS-PAGE indicated that whey proteins irreversibly bound to HPPs, through disulfide bonds, whereas casein bound reversibly, possibly involving the chaperone-like property of casein. This study proposes possible mechanisms by which HPPs interact with milk proteins and impact protein aggregation. This may provide opportunities for developing hybrid protein microparticles. • Both WPI and NaCN restricted the aggregation of hempseed protein particles (HPPs). • Thiol-disulfide interchange occurred between HPPs and WPI during heating. • No evidence of covalent interactions was found in the HPPs and NaCN mixture. • Thermal stable HPPs/WPI particles were created by heat treatment. • The association of caseins with HPPs were temperature-dependent reversible. [ABSTRACT FROM AUTHOR]

This study explored the effect of microfluidization on the dispersibility of hempseed protein (HP) and the interactions of microfluidised HP particles with β-lactoglobulin (β-lg) after heat treatment. Microfluidization increased the dispersible protein fraction from 10% (non-microfluidised) to a maximum of 58% (200 MPa, 6 passes) in HP dispersions. Dispersible HP particles were within the micro-sized range (d 4,3 ≤ 2 μm) after microfluidization. Heat treatment (95 °C, 10–60 min) of HP particles with β-lactoglobulin (β-lg) induced protein association by sulphydryl-disulphide exchange reactions; β-lg association with HP particles initiated within the first 20 min. Additionally, the particle size (d 4,3) values of co-heated HP particles with β-lg were significantly smaller than those found in HP particle dispersions heated alone, results that were in line with microscopy analysis. This suggests that β-lg could have restricted HP particle aggregation. In conclusion, combining microfluidization and heat treatment could offer a venue to modify the physical properties of plant/milk protein mixtures. • Microfluidization formed greater proportion of water-dispersible HP microparticles. • Thiol–disulfide interchange occurred between HP and β-lg during the heat treatment. • The association of β-lg with HP markedly restricted HP aggregation. • The association of β-lg with HP mostly happened in the first 20 min of heating. [ABSTRACT FROM AUTHOR]

Hempseed (Cannabis sativa) protein is an important source of bioactive peptides. H3 (IGFLIIWV), a transepithelial transported intestinal peptide obtained from the hydrolysis of hempseed protein with pepsin, carries out antioxidant and anti-inflammatory activities in HepG2 cells. In this study, the main aim was to assess its hypocholesterolemic effects at a cellular level and the mechanisms behind this health-promoting activity. The results showed that peptide H3 inhibited the 3-hydroxy-3-methylglutaryl co-enzyme A reductase (HMGCoAR) activity in vitro in a dose-dependent manner with an IC50 value of 59 μM. Furthermore, the activation of the sterol regulatory element binding proteins (SREBP)-2 transcription factor, followed by the increase of low-density lipoprotein (LDL) receptor (LDLR) protein levels, was observed in human hepatic HepG2 cells treated with peptide H3 at 25 µM. Meanwhile, peptide H3 regulated the intracellular HMGCoAR activity through the increase of its phosphorylation by the activation of AMP-activated protein kinase (AMPK)-pathways. Consequently, the augmentation of the LDLR localized on the cellular membranes led to the improved ability of HepG2 cells to uptake extracellular LDL with a positive effect on cholesterol levels. Unlike the complete hempseed hydrolysate (HP), peptide H3 can reduce the proprotein convertase subtilisin/kexin 9 (PCSK9) protein levels and its secretion in the extracellular environment via the decrease of hepatic nuclear factor 1-α (HNF1-α). Considering all these evidences, H3 may represent a new bioactive peptide to be used for the development of dietary supplements and/or peptidomimetics for cardiovascular disease (CVD) prevention. [ABSTRACT FROM AUTHOR]

The proteins from two conventionally (CC1 and CC2) and one organically cultivated (OC) hempseed samples were extracted (by alkaline solubilization followed by isoelectric precipitation) and compared in terms of their physicochemical, digestibility and in vitro bioactivity properties. The OC hempseed had higher total protein and lower nonprotein nitrogen content. Protein extracts showed bimodal particle size distributions, with OC showing the smallest and CC1 the largest mean particle diameter (d(0.5)), i.e., 89.0 and 120.0 µm, respectively. Chromatographic analysis showed similar protein profiles for all three protein extracts. The protein extracts were subjected to in vitro simulated gastrointestinal digestion (SGID). Degree of hydrolysis (DH) measurement showed that the highest extent of digestion upon SGID was associated with CC1 (11.0 ± 1.5%), which also had the lowest in vitro antioxidant activity. Only the OC and OC digested samples had lipase inhibitory activity. The results indicate that the cultivation method impacted the composition, physicochemical, digestibility, and biofunctional properties of hempseed proteins.

Hempseed (Cannabis sativa) protein is an important source of bioactive peptides. H3 (IGFLIIWV), a transepithelial transported intestinal peptide obtained from the hydrolysis of hempseed protein with pepsin, carries out antioxidant and anti-inflammatory activities in HepG2 cells. In this study, the main aim was to assess its hypocholesterolemic effects at a cellular level and the mechanisms behind this health-promoting activity. The results showed that peptide H3 inhibited the 3-hydroxy-3-methylglutaryl co-enzyme A reductase (HMGCoAR) activity in vitro in a dose-dependent manner with an IC50 value of 59 μM. Furthermore, the activation of the sterol regulatory element binding proteins (SREBP)-2 transcription factor, followed by the increase of low-density lipoprotein (LDL) receptor (LDLR) protein levels, was observed in human hepatic HepG2 cells treated with peptide H3 at 25 µM. Meanwhile, peptide H3 regulated the intracellular HMGCoAR activity through the increase of its phosphorylation by the activation of AMP-activated protein kinase (AMPK)-pathways. Consequently, the augmentation of the LDLR localized on the cellular membranes led to the improved ability of HepG2 cells to uptake extracellular LDL with a positive effect on cholesterol levels. Unlike the complete hempseed hydrolysate (HP), peptide H3 can reduce the proprotein convertase subtilisin/kexin 9 (PCSK9) protein levels and its secretion in the extracellular environment via the decrease of hepatic nuclear factor 1-α (HNF1-α). Considering all these evidences, H3 may represent a new bioactive peptide to be used for the development of dietary supplements and/or peptidomimetics for cardiovascular disease (CVD) prevention.

With the global population on the rise, challenges in meeting protein demands are amplified by recent crises, prompting a swift shift to alternative protein sources due to disruptions in the supply chain. Plant-based proteins are gaining momentum due to economic, cultural, and environmental considerations, aligning with the preference for sustainable diets and resulting in more affordable plant-based products. The distinction between drug and industrial hemp fuels demand for its nutritional value, digestibility, low allergenicity, and bioactive properties. Industrial hempseed, featuring minimal Δ 9 -Tetrahydrocannabinol (THC) content (<0.2 %), emerges as a promising crop, offering high-quality protein and oil. The de-oiled hempseed cake stands as an eco-friendly and promising protein source enriched with phenolic compounds and fiber. Ongoing research seeks to enhance techno-functional properties of hempseed protein, surmounting initial limitations for integration into various foods. A range of techniques, both conventional and innovative, optimize protein characteristics, while modifying plant-based protein structures augments their application potential. Modification approaches like ultrasound, high-pressure homogenization, conjugation, complexation, fibrillization, and enzymatic methods enhance hempseed protein functionality. The review critically evaluates the techno-functional attributes of hempseed protein and explores strategies for customization through structural modifications. Lastly, the review assesses its composition, potential as a plant-based source, addresses challenges, and discusses strategies for enhanced functionality. [Display omitted] • Global population growth increases the demand for protein sources. • Hempseed is a promising plant-based protein and oil source. • Issues with hemp protein include functionality, color, and sensory attributes. • Research focuses on enhancing hemp protein functionality in food applications. • Emerging technologies are revolutionizing hemp protein modifications. [ABSTRACT FROM AUTHOR]

The increasing demand for plant proteins, along with rising awareness of the nutritional and functional roles of dietary proteins, has prompted the nutrition and food industry to explore nontraditional protein sources. Hempseed protein with its excellent nutritional value and superior digestibility has drawn great interest in both scientific and industrial fields. In this review, the chemistry and nutritional quality of hempseed protein and the health benefits of bioactive peptides derived thereof are highlighted. Processing, functionality, and application of various hemp protein products, including hempseed meal, hemp protein concentrates, and hemp protein isolates, are discussed. Moreover, recent advances in technological innovation to improve hempseed protein functionality are introduced. The objective of this review is to provide an updated summary of the research on hempseed protein and to fill the knowledge gap in the exploitation of potential nutritional, health, and processing benefits of this emerging protein source. [ABSTRACT FROM AUTHOR]

The effects of heating (90 °C/30 min) or ultrasound (200/400/600 W) treatment on antioxidant and angiotensin-converting enzyme inhibitory (ACEI) activity of hydrolysates from hempseed protein isolates (HPI) were studied. The secondary structure, surface hydrophobicity, intrinsic fluorescence, scanning electron microscopy (SEM) and sodium dodecyl sulfate–polyacrylamide gel electrophoresis of HPI treated by heating or ultrasound were measured. The results showed that hydrolysate from HPI treated with ultrasound at 200 W showed higher hydrolysis degree, proportion of lower molecular mass components (1.0–3.0 kDa), antioxidant and ACEI activity than those from heating or high-power treated. The changes in secondary structure, surface hydrophobicity and intrinsic fluorescence indicated the unfolding of HPI after ultrasound. The SEM results showed that HPI treated with ultrasound at 200 W exhibited decrease in particle size and deformation and further increased in power caused the aggregates of HPI. In conclusion, the ultrasound treatment at low-power was superior to 90 °C/30 min treatment in facilitating enzymatic release of antioxidant and ACEI peptides from HPI. [ABSTRACT FROM AUTHOR]

Hemp (Cannabis Sativa L.) is an annual crop cultivated mainly for its use as medicinal, food, oil, and fiber sources. Hempseeds contain about 30% protein, 30% oil, and 25% fiber. The objective of this study is to obtain a high protein concentrate with controlled use of mechanochemical process such as ball milling in combination with extraction pH. Use of ball milling reduced the particle size and broke open the plant cell wall, which was previously reported to increase the yield, solubility, foaming capacity, and hydrophobicity. In our study, the defatted hempseeds were ball milled, and the protein was extracted at pH 8, 9, and 10 followed by isoelectric point precipitation at pH 4.5. The extraction pH and ball milling introduced a significant change in yield and protein functional properties such as surface activity, solubility, hydrophobicity, zeta potential, droplet size, emulsion stability, water holding capacity, and oil holding capacity. According to the surface activity results, the amount of amphiphilic protein decreased with increasing extraction pH. The results indicated that ball milling significantly improved the solubility of proteins extracted at pH 8. As the extraction pH increased, the water holding capacity was increased due to reduced particle size and higher solubility. This study shows that adjustment of extraction parameters can increase the yield and optimize functionality by using ball milling. Depending on the designated use of hemp seed protein, the extraction process can be designed to target the most profitable functional properties. [Display omitted] • Ball milling improved the protein yield, solubility, and emulsion stability. • Low pH extraction preserved the native state of protein. • At pH ≤ 5, ball milling improved the solubility of proteins extracted at pH 8. • WHC increased and OHC decreased with increase in extraction pH. • Hemp protein functionality can be optimized by ball milling. [ABSTRACT FROM AUTHOR]

Hempseed protein concentrate (HPC) was extracted from hempseed press cake with a protein content of 85.7% and co-extruded with oat fibre residue (OFR) to produce high-moisture meat analogues (HMMA) at different moisture contents (60, 63, 66%), screw speeds (500, 700, 900) and temperature profiles (40-70-110-130 °C and 40-70-120-150 °C). The effect of extrusion processing parameters such as moisture content, screw speed, and different temperature profiles on the properties of the extrudates was investigated. The produced meat analogues had a fibrous structure and brown colour, which may be due to the derived hempseed protein. The specific mechanical energy (SME) required in this study was low and ranged from 63 to 185 kJ/kg. As moisture content increased, it was discovered that hardness, chewiness, and cutting strength values decreased. Nevertheless, cutting strength values increased when a higher temperature profile was used. By using a higher temperature profile, the protein was completely denatured, leading to the formation of stronger fibres in the meat analogues with a higher quality in terms of texture. The study demonstrated the possibility for both materials from underutilised side-streams to be converted into meat analogues, which would provide variety for the HMMA on the market. • HME turned side-stream materials from a mixture of hempseed protein concentrate and oat fibre residue into novel meat analogues. • HMMA from hempseed protein concentrate – oat fibre residue mixture cooked at a high temperature offered greater texture quality and consumed less energy. • The technique used in this study could enhance the use of hempseed press cake and oat fibre residue in the food industry. [ABSTRACT FROM AUTHOR]

• Casein (CN) and hempseed protein (HPI) were catalyzed by transglutaminase (TGase). • CN-HPI complex had higher surface hydrophobicity, zeta potential & viscosity. • TGase cross-linked CN-HPI enhanced its emulsifying and gelation properties. In present study, microbial transglutaminase (MTGase) was applied to strengthen the interaction between casein and hempseed protein (HPI) through crosslinking. The structural and functional characteristics of this heteropolymers were investigated. Both homologous and heterologous crosslinking were achieved by adding MTGase in casein-HPI system, and thus enhanced zeta potential, surface hydrophobicity, viscosity, emulsifying and gelation properties of the complex. However, HPI hindered the crosslinking due to unbalanced Lys/Gln ratios. Emulsifying and gelling properties were significantly correlated with the secondary structures. When MTGase activity was < 30 U/g or treatment time was < 2 h, the α-helix content decreased by 9% while the β-sheet content increased by 12%, respectively, with MTGase activity and treatment time increase. The structural alterations resulted in the better emulsifying activity, gel networks and water holding capacity of the complex. This work represents a novel interaction mode between casein and HPI via MTGase to elevate functional properties of complex. [ABSTRACT FROM AUTHOR]

Abstract: Hempseeds have not been utilised to any significant extent by the industrial food markets. A novel antioxidant peptide derived from hempseed by-product was investigated. Hempseed protein isolate was prepared by alkaline extraction and subsequent isoelectric precipitation. Its enzymatic hydrolysate, obtained by Alcalase® treatment, was subjected to DA201-C macroporous absorption resin, with simultaneous desalting and concentrating of hydrophobic fragments with improved free radical-scavenging activities. The active fraction was further separated by gel filtration and reversed-phase high performance liquid chromatography to obtain two purified peptides; the peptides were characterised as NHAV and HVRETALV, by MALDI-TOF/TOF MS/MS. The protective effects of the purified peptides on hydrogen peroxide-induced cell apoptosis were investigated in rat pheochromocytoma line PC12 cells. The peptides, at a concentration of 10μg/ml, possessed protective effects (P <0.05) against cell death and oxidative apoptosis. The findings are significant for the discovery and development of natural antioxidants from hempseed by-products. [Copyright &y& Elsevier]

The thermal co-aggregates from mixed egg white protein (EWP) and hempseed protein isolate (HPI), named mixed EWP/HPI aggregates, was produced by heating the mixture solutions (5.0% w/v) at different EWP/HPI weight ratios (0/100, 75/25, 50/50, 25/75 and 100/0) under alkaline pH. Subsequent, the acid gelation of the thermal aggregates was induced by adding glucono-δ-lactone (GDL). The thermal treatment at alkaline pH produced the aggregates assembled by both disulfide and non-disulfide covalent bonds, and they exhibited low viscosity, and high solubility EWP alone formed gels of high mechanical strength in the presence of GDL, whereas no gels were obtained from the thermal aggregates of HPI alone. The EWP/EWP aggregates of different EWP/HPI ratios formed acid-induced self-supported gels. With increasing HPI content, the elastic modulus, tan δ, creep performance, texture parameters, fracture stress/strain, and microstructural homogeneity of the mixed EWP/HPI gels tended to decrease. Treatment with transglutaminase (TGase) relatively improved the mechanical properties of mixed gels, but not enough to completely off-sets the weakening effects. This research has offered insight into the fabrication of cold-set gels from different protein aggregates and the generated information may provide the opportunity to develop functional food formulations enriched in plant proteins. Image 1 • Mixed aggregates of egg white and hempseed protein were formed by heating at alkaline pH. • Acid gelation of the thermal mixed aggregates was induced by adding glucono-δ-lactone. • Gel strength decreased with the hempseed protein content in the mixed aggregates. • Treatment with transglutaminase significantly offset such weakening effects. [ABSTRACT FROM AUTHOR]

• Hempseed protein digests were prepared by simulated gastrointestinal digestion. • Heating improved the digestibility of isolated hempseed proteins. • Heating reduced the bioactivity of hempseed proteins digests. The objective was to investigate the effects of heat pretreatment and simulated gastrointestinal digestion on potential antioxidant, anticancer and anti-inflammatory activities of hempseed (Cannabis sativa L.) proteins. Unheated isolated hempseed protein (IHP) and its heated counterparts (100 °C, 15 min and 30 min, termed as HP15D and HP30D) were hydrolyzed sequentially with pepsin and pancreatin and analyzed for digestibility and bioactivity (antioxidant, anti-proliferative and anti-inflammatory properties). Heat pretreatment led to an increase of low molecular weight proteins and degree of hydrolysis, and decrease of concentration of soluble protein, which means heat pretreated can significantly improve the digestibility of IHP. Pepsin-pancreatin digests released from heat pretreated IHP possessed less antioxidant, antiproliferative and anti-inflammatory properties than digests from unheated IHP. In conclusion, heat pre-treatment improved the digestibility of IHP but the resulting digests from heated IHP had lower bioactivity. [ABSTRACT FROM AUTHOR]