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Article

Study of the Preparation and Properties of Chemically Modified Materials Based on Rapeseed Meal

by
Sara Aquilia
1,2,3,
Luca Rosi
2,
Michele Pinna
3,
Sabrina Bianchi
3,
Walter Giurlani
2,
Marco Bonechi
2,
Francesco Ciardelli
3,*,
Anna Maria Papini
1,2,* and
Claudia Bello
1,2
1
Interdepartmental Research Unit of Peptide and Protein Chemistry and Biology, University of Florence, Via della Lastruccia 13, I-50019 Sesto Fiorentino, Italy
2
Department of Chemistry “Ugo Schiff”, University of Florence, Via della Lastruccia 13, I-50019 Sesto Fiorentino, Italy
3
Spin-PET S.r.l., Viale R. Piaggio 32, I-56025 Pontedera, Italy
*
Authors to whom correspondence should be addressed.
Biomolecules 2024, 14(8), 982; https://doi.org/10.3390/biom14080982
Submission received: 25 June 2024 / Revised: 6 August 2024 / Accepted: 9 August 2024 / Published: 10 August 2024
(This article belongs to the Collection Feature Papers in 'Biological and Bio- Materials' Section)
Browse Figures
Versions Notes

Abstract

:
In recent years, there has been increasing interest in developing novel materials based on natural biopolymers as a renewable alternative to petroleum-based plastics. The availability of proteins derived from agricultural by-products, along with their favourable properties, has fostered a renewed interest in protein-based materials, promoting research in innovative technologies. In this study, we propose the use of rapeseed protein-rich meal as the main ingredient for the preparation of novel sustainable materials combining excellent environmental properties such as biodegradability and renewability. The application of sustainable products in the present high-tech society requires the modification of the basic native properties of these natural compounds. The original route proposed in this paper consists of preparation via the compression moulding of flexible biomaterials stabilized by crosslinkers/chain extenders. An investigation of the effects of different denaturing and disulfide bond reducing agents, crosslinkers, and preparation conditions on the material mechanical behaviour demonstrated that the novel materials have appreciable strength and stiffness. The results show the potential of utilizing full meal from vegetable by-products to prepare protein-based materials with guaranteed ecofriendly characteristics and mechanical properties adequate for specific structural applications.

1. Introduction

Polymeric organic materials are extensively used across various sectors in modern society. The remarkable properties and versatility of polymers, coupled with their cost-effectiveness, have resulted in their widespread usage. Nonetheless, the unregulated disposal of the huge amount of plastic waste generated has given rise to one of the most pressing environmental challenges of our era [1,2,3], which mainly concerns packaging and low-performance, short-life products.
Consequently, there is a growing interest in the development of environmentally friendly and biodegradable materials from renewable resources. This effort aims to replace the use of petroleum-based materials in sustainable applications, which raise significant concerns regarding pollution and sustainability [4]. However, at present, bioplastics and in general bioderived organic materials constitute less than one percent of the annual production of plastic, which exceeds 390 million tons [5]. Transition to a circular economy model is also necessary for the development of innovative strategies to optimize resource utilization and eliminate the concept of waste throughout the entire supply chain [6,7,8,9]. Bio-related plastics and organic materials derived from coproducts or waste materials offer the advantage of exploiting pre-existing, and often underutilized, resources. Furthermore, their utilization serves to mitigate disposal costs and to reduce environmental impacts [10].
Proteins from the agri-food industry are a good alternative to petrochemical-based polymers. Rapeseed is a crucial oilseed crop, ranking second only to soybean, with Canada and United States being the top producers, while Europe accounts for almost 25% of the global production [11,12]. Rapeseed is manly employed for oil production in the food and feed industry, as well as for biodiesel preparation. The residual product generated by oil extraction is the rapeseed meal, also called canola meal, which is collected as a by-product after oil pressing and subsequent solvent extraction [12]. Depending on the growth conditions, harvest methods, and processing techniques, the protein content in rapeseed meals may vary from 35% to 40% [13]. Cruciferin (12S globulin) and napin (2S napin) represent 60% and 20% of the total rapeseed crude protein, respectively. Cruciferin is a high-molecular-weight protein formed by six subunits each containing a heavy α-chain (30 KDa) and a light β-chain (20 KDa), linked by both disulfide bonds and non-covalent interactions. Napin is instead composed of one small (4–6 kDa) and one large (10–12 kDa) polypeptide chain that are held together by disulfide bonds [14,15].
Although rapeseed meal possesses significant nutritional potential and contains value-added compounds [16,17], its application in the food and feed sectors is limited by the presence of antinutritional compounds, such as glucosinolates, erucic acid, phytates, and phenols, which negatively affect the palatability and digestibility of the meal [12]. In recent years, because of its high storage protein content and low cost, the exploitation of canola meal for the production of cosmetics and bioplastic materials has emerged [13]. Rapeseed proteins offer indeed a promising ecofriendly alternative for the production of technical products such as polymers, coatings, adhesives, detergents and lubricants [18]. The development of a fully natural and potentially biodegradable protein-based material with acceptable mechanical properties could efficiently decrease the societal demand for fossil-based polymers in several applications [19].
However, the application of proteins, including proteins from rapeseeds, as bio-based polymers is limited by certain drawbacks, including slow biodegradability, limited mechanical properties and high water permeability [7,20,21,22]. Additives, such as plasticizers, are commonly integrated into the biopolymers to improve these limitations. Plasticizers break inter- and intra-molecular hydrogen bonds, resulting in the enhanced mobility of polymer chains, greater spacing between polymer molecules, and a reduction in the proportion of crystalline regions compared to amorphous regions. Glycerol and water are common plasticizers in protein-based materials, because of their low molecular mass and ability to interact with polar residues [23,24,25]. Additionally, crosslinkers are used to enhance the mechanical strength, the thermal and chemical stability, and to decrease the swelling properties of polymeric and biopolymeric materials [26,27]. Nevertheless, high crosslinking might lead to a decrease in the biodegradability of the material. Therefore, using eco-compatible crosslinkers and optimizing the amount of crosslinker in the material enable the exploitation of its favourable effects while minimizing the drawbacks.
The production of edible films and bio-composites from agricultural process by-products has been already reported [28,29,30,31]. However, the development of commercially suitable industrial products from raw rapeseed meal is very limited [19,23,32] and the studies involving rapeseed biomass are mainly focused on protein isolate-based bioplastics and on wet casting techniques [33,34,35,36] (Table 1).
On the other hand, our study aims to utilize the rapeseed meals as a matrix for the development of a cost-effective biodegradable composite for possible future industrial applications. Therefore, we describe herein an original route for the preparation of flexible biomaterials based on raw, protein-rich rapeseed meal stabilized by modulated crosslinking with selected epoxides, using compression moulding. Moreover, we investigated the effects of different denaturing and disulfide bond-reducing agents, cross-linkers, and preparation conditions on the mechanical behaviour. The thermal properties were also studied through TGA, thus showing the potential use of our approach in the preparation of novel biocompatible materials from vegetable waste.

2. Materials and Methods

2.1. Materials

The rapeseed meal (RM) was generously supplied by Italcol S.p.A. (Castelfiorentino, Italy). Rennet casein was provided by Fontana Enzo s.r.l. (Sarmato, Italy). Glycerol, poly(ethylene glycol) diglycidyl ether, neopentyl glycol diglycidyl ether, epoxidized soybean oil, sodium sulfite (Na2SO3), sodium dodecyl sulfate (SDS), urea, guanidinium chloride, and anhydrous KBr were purchased from Sigma-Aldrich (St. Louis, MO, USA). They were of analytical or reagent grade and were employed without additional purification.

2.2. Rapeseed Meal-Based (RM) Material Preparation

The rapeseed meal was dry milled at 1800 rpm for 15 min at room temperature. The resulting powder was placed in an oven overnight at 50 °C to remove moisture. Next, 40 g of rapeseed meal (53% w/w total) was mixed with 10 g of a protein-binding agent (Rennet casein, 13 w/w), 20 g of glycerol (27% w/w), 5 g of distilled water (7% w/w), and 2.5 g of Poly(ethylene glycol) diglycidyl ether (2 × mol lysine-based), using a blender blade for 15 min to obtain a homogeneous blend. Glycerol was used as a plasticizer, and Poly(ethylene glycol) diglycidyl ether was employed as a cross-linker. Subsequently, the mixture was heated to 150 °C for 15 min and pressed using a flat-bed press (CAMPANA model: PRESSA PM20/200) at 150 °C for 20 min at 250 Bar (mould dimensions: 8 cm × 16 cm × 1.5 mm). The resulting material (RM, Table 2) was then cooled to room temperature and stored in a desiccator with 75% humidity control.
Modified rapeseed meal specimens (see Table 2 for detailed composition) were prepared following the above-described procedure, except for the substitution of the distilled water with an aqueous solution of Na2SO3 (10% w/w), Na2SO3 (20% w/w), Urea (2 M), Guanidine (1 M), or SDS (3% w/w).

2.3. Mechanical Properties

After pressing, the rapeseed meal specimens were kept at 25 °C and 75% RH for 24 h, and then cut into three or four standard dumbbell-shaped moulds, each measuring 60 mm (length) × 5 mm (width) × 1.3 mm (thickness). The mechanical properties were evaluated using a Shimadzu instrument (Model AGS-X 5 KN, Milano, Italy) following the Standard Test Method for Tensile Properties of Plastics (ASTM D638-91). The testing speed was set at 5 mm/min. The tensile strength, elongation at break (%), and elastic modulus were determined based on measurements taken from at least three replicates.

2.4. Fourier-Transform Infrared Spectroscopy

Fourier-Transform Infrared Spectroscopy (FT-IR) analysis of the specimens was conducted in transmittance mode using a Jasco FT-IR-4200 instrument (Cremella, Italy). Prior to analysis, the materials were dried in an oven at 60 °C for 48 h. Subsequently, the dried samples were milled into powder using a mortar and pestle and blended with anhydrous KBr at a 1:50 ratio. The resulting mixture was then pressed to form transparent pellets. Spectra were collected over the range of 400 to 4000 cm−1 with 32 scans at a resolution of 4 cm−1. The spectra were further analyzed using Origin Pro 2021 by baseline subtraction and normalization in the range 1:100.

2.5. Thermogravimetric Analysis

The thermal stability of the protein-based materials was assessed via thermogravimetric analysis (TGA) conducted utilizing a Perkin Elmer 4000 instrument (Waltham, MA, USA). The samples were subjected to controlled heating under a continuous flow of nitrogen (30 mL/min) from room temperature to 815 °C at a programmed ramping rate of 10 °C/min.

2.6. Scanning Electron Microscopy

Scanning electron microscopy (SEM) analysis was performed with a variable pressure Hitachi SU3800 (Hitachi High-Tech, Tokyo, Japan) equipped with a Ultim Max 40 silicon drift EDS detector and AZtecLive software 6.1 (Oxford Instruments NanoAnalysis, Abingdon, UK). The measurements were performed at various magnifications with an accelerating voltage of 15 kV. Before the SEM analysis, the samples were metallized using a SC7640 Polaron Sputter Coater (Quorum Technologies, Laughton, UK) with a SC510-314B gold/palladium target. Both the surface and the section of the samples were analyzed. For sectioning, we opted for cryofracture: the samples were immersed for approximately one minute in liquid nitrogen to ensure that all the material reached the same temperature, and then it was split in two using two forceps while keeping the polymer immersed in liquid nitrogen.

3. Results and Discussion

Preliminary tests to assess the behavior of canola meal in hot pressing were carried out, and optimized temperature (150 °C) and pressure (250 bar) conditions were determined. Afterwards, the influence of the method used for blend preparation and of the addition of plasticizers and cross-linkers was evaluated. The best results were obtained using a blender blade as the mixing method, water and glycerol as plasticizers, and poly(ethylene glycol) diglycidyl ether (Epoxy-PEG) as a cross-linker.
Glycerol, an environmentally friendly, effective plasticizer for biopolymer-based materials [37], in particular those derived from proteins [38], was used in the same quantity as in applications reported in the literature [39,40,41]. Epoxy-PEG, a hydrophilic epoxidized compound, which can be also obtained from natural resources, was used in an amount based on the moles of Lys (2.86% of the full amino acid content) present in the meal proteins [42]. The epoxy groups exhibit high reactivity with the amine and carboxyl functional groups present on the side chains of the protein amino acids. Notably, even at 70 °C, the amine and epoxy groups demonstrate a significant reaction rate [19]. Further significant improvements were obtained when adding Rennet casein [43,44] and canola meal/casein in a 4:1 ratio to the preparation. The use of Casein derived from surplus milk not intended for the food industry constitutes a deliberate effort to optimize the use of environmental resources and reduce the ecological impact on our planet.
Those preliminary tests demonstrated that raw canola meal can be used in heat pressing processes to produce a compact material with promising mechanical properties even if still not at the level of fossil plastic polymers.

3.1. Influence of Different Crosslinkers on the Tensile Properties of the Specimens

Starting from the results obtained from the preliminary tests, the effect of three different epoxydic crosslinkers on the properties of our material was evaluated. We thus compared the hydrophilic Epoxy-PEG with epoxidized soybean oil, a biobased hydrophobic crosslinking agent already used as stabilizer and plasticizer in PVC and bio-based materials [45,46], and neopentyl glycol diglycidyl ether. The latter is hydrophobic in nature, with a smaller steric size and lower molecular weight than the other two. This may allow for better diffusion within the blend, compared to the epoxidized soybean oil [46,47,4]. The Young’s modulus and the stress at fracture of samples RM-ES and RM-NE decreased substantially, as reported in Table 3. The particularly low elongation is probably primarily due to the structural microfracture of the materials deriving from the not complete and uniform diffusion of the crosslinker in the protein-rich matrix and the heterogeneous chemical nature of the matrix itself. Moreover, only the material prepared using epoxidized soybean oil (RM-ES) and neopentyl glycol diglycidyl ether (RM-NE) showed an exudate on the surface a few hours after preparation, probably due to the migration of the non-reacted crosslinker.

3.2. Effects of Disulfide Bond Reducing Agents and Denaturant

Disulfide-bond-reducing or/and denaturing agents in different percentages were added to the blend to improve the mechanical properties of the material.
The tensile strength and Young’s modulus increased with the addition of a 10% w/v aqueous solution of Na2SO3 (RM-R1, Table 4) when compared to the unmodified RM material. However, the material made with a 20% w/v aqueous solution of Na2SO3 showed a comparable tensile strength to the RM material, but with a higher elastic modulus and elongation at fracture (Figure 1 and Table 4). The mechanical properties of the material exhibited a strong correlation with their molecular structures and constituent components. Na2SO3 acts as a reducing agent for the disulfide bonds within the proteins, thereby inducing protein denaturation. Certain functional groups, such as amino, carboxylic, and sulfhydryl groups, exhibit relatively high reactivity and can participate in reactions with both Epoxy-PEG and other functional groups, facilitating the formation of cross-links, particularly under the elevated temperatures of processing.
Modified RM materials such as RM-R1 and RM-R2, characterized by a high degree of denaturation, tend to develop a greater number of entanglements and crosslinks, resulting in enhanced mechanical strength. At higher concentrations, Na2SO3 primarily serves as a plasticizer, increasing the mobility of the protein chains. However, the elongation at fracture (Figure 1 and Table 4) remains low, thus suggesting that the mobility is limited to small domains inside the material surrounded and confined by densely crosslinked species. The use of TCEP (tris(2-carboxyethyl)phosphine) as an alternative reducing agent to sodium sulfite was not effective, as the tensile properties of the material worsened dramatically when a 10% w/v aqueous solution of TCEP (7% w/w) instead of 10% w/v Na2SO3 was added to the blend before heat pressing (Elastic modulus: 56.36 ± 5.64 N/mm2, stress at fracture: 0.55 ± 0.12 N/mm2).
The influence of SDS, urea, and guanidinium chloride, which are commonly employed denaturing agents for proteins, on the mechanical properties of RM-based materials was investigated. The Young’s modulus of the obtained slabs decreased by two orders of magnitude compared to the unmodified RM material, indicating the important role of the ordered structure on mechanical strength. However, the stress at fracture remained relatively constant and small, suggesting that the weak points remain the same (Figure 1 and Table 5). Urea destabilizes globular proteins by establishing robust hydrogen bonds with water molecules that surround the protein. Simultaneously, it interferes with the hydrogen bonds within the protein structure, leading to the formation of partially unfolded protein conformations and flexible peptide chains. Similarly, the interaction with SDS alters both tertiary and quaternary protein structures by disrupting the hydrophobic and electrostatic interactions within the protein without breaking covalent bonds. This results in the protein structure becoming partially unfolded and more flexible. The elongation remains relatively low due to fractures occurring in defective areas, which cause the material to break at the interface between distinct domains.
The above results suggest that a higher degree of denaturation and, consequently, a greater number of cross-links are achieved when a reducing agent such as Na2SO3 acts upon covalent S-S bonds, compared to the utilization of denaturing agents like urea, guanidinium chloride, and SDS.
As shown in Table 6, when both Na2SO3 and guanidinium chloride are employed in the production of RM-based materials, an increase in stress at fracture and in the elastic modulus was observed. Denaturation exposes the hydrophobic residues that are buried within the core of folded protein molecules at the molecular surface. Moreover, these hydrophobic groups are capable of engaging in more extensive hydrophobic interactions among protein molecules during the compression molding process [47,48]. Young’s modulus increases significantly due to the formation of cross-links between the protein chains and the cross-linker (Epoxy-PEG) due to the higher number of reactive groups exposed by the denaturing agent. Moreover, the plasticizer effect of water was observed when RM-R2D2 7% and RM-R2D2 14% were compared, as evidenced by the reduction in Young’s modulus and tensile stress. Indeed, water has a high dielectric constant and establishes strong interactions with the hydrophilic and charged groups of the proteins through the formation of hydrogen bonds [49].

3.3. Thermal Properties

To determine the effect of the different compositions on the thermostability of the material, we performed the thermogravimetric analysis of all the samples. The TGA and first-derivative curves (Figure S1 and Figure 2, respectively) show a weight loss profile for all materials, similar to what observed for other protein-based materials [47]. The initial weight loss, between 30 °C and ca 150 °C, is particularly evident in samples RM and RM-R2 (Figure 2) and corresponds to a loss of moisture. In particular, RM exhibits a higher amount of residual and eliminable moisture, which is therefore considered non-structural. In contrast, the other specimens did not display any water elimination, indicating their inability to absorb water due to increased reticulation or a higher structural water content. Additionally, the RM-D2 and RM-R2D2 samples, which have a greater reticulation degree, show an inversion of the area ratios between the first and second thermal degradation steps, reflecting a decline in quantity. The peak of the first degradation step (around 225 °C) shifts slightly to a higher temperature, suggesting a marginal increase in stability. The second stage (ca 150 °C–250 °C) can be attributed to the loss of glycerol (bp 290 °C). A third step weight loss from 250 °C to ca 400 °C is due to the degradation of residual protein-rich material. RM-D1 also shows an extra stage (400 °C–500 °C), probably due to the decomposition of urea with the loss of ammonia and carbon dioxide.
A slight shift to higher temperatures in the weight loss of glycerol can be observed going from RM to RM-R2D2 14%, except for RM-R2. That indicates an enhanced thermal stability of the material containing both the reducing and the denaturing agent (RM-R2D2 14%).

3.4. Protein Conformation Analysis

Untreated meal and the modified materials were analyzed by FT-IR spectroscopy. No substantial change can be observed when comparing the full spectra of the materials (Figure 3). To investigate eventual changes in the secondary structures of the protein components, we compared the amide I band region (from ca 1590 to 1700 cm−1), which is mainly due to the stretching vibration mode of the carbonyl in the amide groups and is representative of protein secondary structures (Figure 4).
The amide I bands of RM-R, RM-R2, RM-D1, RM-D2, and RM-R2D2 14% show slight differences in the range of 1625–1700 cm−1 that are more evident in the case of RM-D2 (Figure 4A). However, comparing the amide I band in the spectrum of the meal with the one in the spectra of RM, RM-R0, and RM-R2D2 14% (Figure 4B), a change in shape in the range of 1600–1625 cm−1 can be observed. This can be ascribed to the contribution of H-bonded β-sheets because of protein aggregation [49,50], as shown in the spectra reported in Figure S2. A notable difference was observed in the band areas of the new materials compared to the raw rapeseed meal, highlighting the impact of thermal treatment on secondary structures. Specifically, differences are significant at 1622–1624 cm−1, and can be attributed to the contribution of strongly hydrogen-bonded β-sheets (Table 7) [49,51]. Aggregation could also be ascribed to the isopeptide bond formation [52] that can be formed at high temperatures, mainly due to the presence of lysine and tyrosine residues (5.55% and 3.22%, respectively, present in the crude protein-based material).
Moreover, the higher contribution of the peak at 1745 cm−1 to the amide I band in the spectra indicates the formation of the desired cross-links through inter- or intra-molecular ester bonds between the Asp and Glu sidechains in the protein and in the lignin components of the meal and the epoxide [49,51].

3.5. Material Appearance

All the material obtained from compression molding were brown, compact and flexible.
Scanning electron microscopy was used to investigate the morphology of the material in more detail. When the materials were fractured at room temperature, it was possible to observe a clear change in their morphology, comparing both the section and the interior of the single specimens to each other (Figures S3 and S4). Indeed, the presence of casein and the crosslinker (comparison RM-R0/RM) gives a more compact aspect to the section of the material (Figure S3): it is still possible to distinguish layers in RM, but they are much less separated than in the case of R0. When 20% Na2SO3 is added (specimen RM-R2), the material appears more homogeneous. Different morphologies can be observed in the case of RM-D1 and RM-D2, probably because of the different effects of the denaturing agent used. Among all the specimens analyzed, RM-R2D2 14% is the one that looks the most compact and uniform. By taking images at a higher magnification (Figures S5–S8), it was possible to distinguish the cells of rapeseed: a well-defined cell wall was visible in RM-R0, while cells were more broken in the other specimens, which indicates that the high protein content in them disappeared and was more available for processing.
We also performed SEM measurements on cryogenic fractured RM-R0, RM-D2, and RM-R2D2 14% (Figure 5). In this case, the differences in the sections are striking: while RM-R0 is clearly still a simply pressed material, RM-D2 and RM-R2D2 14% are homogeneous and compact materials.

4. Conclusions

In this study, raw rapeseed meal was processed with appropriate interactive additives by pression molding to obtain a novel protein-rich material. Moreover, a series of investigations were performed to understand the effect of several treatments and additives on the final properties. The addition of Rennet casein increased the protein content of the material and clearly improved its mechanical resistance. Different reducing and denaturing agents were tested at various concentrations to induce protein denaturation and to understand the role of the molecular feature on the material’s ultimate properties. The polypeptide chain became more flexible and, at the same time, led to functional groups that were more accessible for the crosslinking reaction. The best results were obtained when a 20% w/w aqueous solution of Na2SO3, acting both as a disulfide-bond-reducing agent and as plasticizer, and 1 M guanidinium chloride, acting as a denaturing agent, were added to the blend (14%, w/w total), with a significant increase in Young’s modulus and very modest elongation at fracture. The study described up to now is certainly innovative and informative, despite the mechanical properties not yet being industrially competitive. However, our results suggest a promising pathway for developing a protein-rich material for future industrial application. A change in the protein structure was evidenced by the FT-IR analysis when comparing the amide I bands of the specimens with different compositions to each other and to the one comprising rapeseed meal, indicating effective protein denaturation. The presence of disulfide-bond-reducing and denaturing agents caused the partial unfolding of the proteins and led to a major exposure of the amino acid side chains of the protein. Thus, hydrophobic groups are capable of engaging in more extensive hydrophobic interactions among amino acids in the protein molecules and the reactive functional groups form more cross-links with the crosslinker. Moreover, TGA revealed the improved thermal stability of the material containing both the reducing and the denaturing agent (RM-R2D2 14%), suggesting the stronger interaction of glycerol with the other component of the material, particularly with the amino acid side chains of the denatured proteins. Taken together, the presented results demonstrate the potential use of cross-linked, rapeseed protein-rich meal-based materials obtained by pression molding as an alternative to environmentally demanding polymeric materials.

Supplementary Materials

The following supporting information can be downloaded at: https://www.mdpi.com/article/10.3390/biom14080982/s1, Figure S1: TG curves of specimens; Figure S2: Amide I band in the FT-IR spectra of the materials: (A) meal, (B) RM-R0, (C) R0, and (D) RM-R2D2 14%; Figure S3: SEM of the rapeseed meal-based materials (cross section, room temperature) at 500 or 300 μ m; Figure S4: SEM of the rapeseed meal-based materials (longitudinal section, room temperature); Figure S5: SEM of the rapeseed meal-based materials (cross section, room temperature) at 100 μ m, Figure S6: SEM of the rapeseed meal-based materials (longitudinal section, room temperature) RM-R0, RM and RM-R2; Figure S7: SEM of the rapeseed meal-based materials (longitudinal section, room temperature) D1 and D2; Figure S8: SEM of the rapeseed meal-based materials (longitudinal section, room temperature) RM-R2D2 14%.

Author Contributions

Conceptualization, F.C., A.M.P., C.B. and L.R.; methodology, S.A., F.C., A.M.P., C.B. and L.R.; validation, S.A., M.P. and S.B.; formal analysis, S.A., C.B. and M.P.; investigation—materials preparation and characterization, S.A.; investigation—Surface Electron Microscopy (SEM), W.G.; resources, F.C., L.R. and A.M.P.; data curation, S.A., F.C., A.M.P., C.B. and L.R.; writing—original draft preparation, S.A.; writing—review and editing, S.A., F.C., A.M.P., C.B., L.R., W.G. and M.B.; visualization, S.A., C.B., W.G. and M.B.; supervision, F.C., A.M.P. and L.R.; project administration, F.C. and A.M.P.; funding acquisition, F.C., A.M.P. and L.R. All authors have read and agreed to the published version of the manuscript.

Funding

S.A. is the recipient of the PhD fellowship PON Research and Innovation 2014–2020 (D.M 1061/2021) XXXVII Cycle in Chemical Sciences: “Development of macromolecular and cross-linked materials based on proteins/peptides from vegetable or animal sources”, funded by MUR/EU-FSE.

Institutional Review Board Statement

Not applicable.

Informed Consent Statement

Not applicable.

Data Availability Statement

No existing datasets or raw data have been analysed in the manuscript.

Acknowledgments

This study was supported by 5th Seed Funding Program of EUniWell “Technology Transfer of Peptides for the Well-being Economy (TTPep—Peptides for Well-being)”. S.A. thanks MUR-Italy for the PhD fellowship funded by PON Ricerca e Innovazione 2014–2020. Italcol S.p.A. is kindly acknowledged for the generous gift of raw canola meal. Cassa di Risparmio di Firenze Foundation for the financial support (ENFORCE PROJECT, Ricercatori a Firenze, 2021).

Conflicts of Interest

The authors declare no conflicts of interest.

References

  1. Hatti-Kaul, R.; Nilsson, L.J.; Zhang, B.; Rehnberg, N.; Lundmark, S. Designing Biobased Recyclable Polymers for Plastics. Trends Biotechnol. 2020, 38, 50–67. [Google Scholar] [CrossRef] [PubMed]
  2. North, E.J.; Halden, R.U. Plastics and Environmental Health: The Road Ahead. Rev. Environ. Health 2013, 28, 1–8. [Google Scholar] [CrossRef] [PubMed]
  3. Hahladakis, J.N.; Velis, C.A.; Weber, R.; Iacovidou, E.; Purnell, P. An Overview of Chemical Additives Present in Plastics: Migration, Release, Fate and Environmental Impact during Their Use, Disposal and Recycling. J. Hazard. Mater. 2018, 344, 179–199. [Google Scholar] [CrossRef] [PubMed]
  4. Liu, D.; Zhang, L. Structure and Properties of Soy Protein Plastics Plasticized with Acetamide. Macromol. Mater. Eng. 2006, 291, 820–828. [Google Scholar] [CrossRef]
  5. Bioplastics Facts & Figures. Available online: https://www.european-bioplastics.org/bioplastics-facts-figures/ (accessed on 9 August 2024).
  6. Ancuța, P.; Sonia, A. Oil Press-Cakes and Meals Valorization through Circular Economy Approaches: A Review. Appl. Sci. 2020, 10, 7432. [Google Scholar] [CrossRef]
  7. Álvarez-Castillo, E.; Felix, M.; Bengoechea, C.; Guerrero, A. Proteins from Agri-Food Industrial Biowastes or Co-Products and Their Applications as Green Materials. Foods 2021, 10, 981. [Google Scholar] [CrossRef] [PubMed]
  8. Dziuba, R.; Kucharska, M.; Madej-Kiełbik, L.; Sulak, K.; Wiśniewska-Wrona, M. Biopolymers and Biomaterials for Special Applications within the Context of the Circular Economy. Materials 2021, 14, 7704. [Google Scholar] [CrossRef] [PubMed]
  9. Aguilar, A.; Twardowski, T.; Wohlgemuth, R. Bioeconomy for Sustainable Development. Biotechnol. J. 2019, 14, 1800638–1800652. [Google Scholar] [CrossRef] [PubMed]
  10. Ryder, K.; Ali, M.A.; Billakanti, J.; Carne, A. Evaluation of Dairy Co-Product Containing Composite Solutions for the Formation of Bioplastic Films. J. Polym. Environ. 2020, 28, 725–736. [Google Scholar] [CrossRef]
  11. Production of Rapeseed by Main Producing Countries 2023/24. Available online: https://www.statista.com/statistics/263930/worldwide-production-of-rapeseed-by-country/ (accessed on 29 May 2024).
  12. Di Lena, G.; Sanchez del Pulgar, J.; Lucarini, M.; Durazzo, A.; Ondrejíčková, P.; Oancea, F.; Frincu, R.-M.; Aguzzi, A.; Ferrari Nicoli, S.; Casini, I.; et al. Valorization Potentials of Rapeseed Meal in a Biorefinery Perspective: Focus on Nutritional and Bioactive Components. Molecules 2021, 26, 6787. [Google Scholar] [CrossRef]
  13. Raboanatahiry, N.; Li, H.; Yu, L.; Li, M. Rapeseed (Brassica napus): Processing, Utilization, and Genetic Improvement. Agronomy 2021, 11, 1776. [Google Scholar] [CrossRef]
  14. Bhatty, R.S.; McKenzie, S.L.; Finlayson, A.J. The Proteins of Rapeseed (Brassica napus L.) Soluble in Salt Solutions. Can. J. Biochem. 1968, 46, 1191–1197. [Google Scholar] [CrossRef]
  15. Yang, C.; Wang, Y.; Vasanthan, T.; Chen, L. Impacts of pH and Heating Temperature on Formation Mechanisms and Properties of Thermally Induced Canola Protein Gels. Food Hydrocoll. 2014, 40, 225–236. [Google Scholar] [CrossRef]
  16. Gallorini, R.; Aquilia, S.; Bello, C.; Ciardelli, F.; Pinna, M.; Papini, A.M.; Rosi, L. Pyrolysis of Spent Rapeseed Meal: A Circular Economy Example for Waste Valorization. J. Anal. Appl. Pyrolysis 2023, 174, 106138–106147. [Google Scholar] [CrossRef]
  17. Wanasundara, J.P.D.; Kapel, R.; Albe-Slabi, S. Proteins from Canola/Rapeseed—Current Status. In Sustainable Protein Sources, 2nd ed.; Nadathur, S., Wanasundara, J.P.D., Scanlin, L., Eds.; Academic Press: Cambridge, MA, USA, 2024; pp. 285–309. [Google Scholar]
  18. Fetzer, A.; Müller, K.; Schmid, M.; Eisner, P. Rapeseed Proteins for Technical Applications: Processing, Isolation, Modification and Functional Properties—A Review. Ind. Crops Prod. 2020, 158, 112986–113004. [Google Scholar] [CrossRef]
  19. Li, S.; Ciardullo, K.; Donner, E.; Thompson, M.R.; Rempel, C.; Liu, Q. Reactive Processing Preparation of Sustainable Composites from Canola Meal Reinforced by Chemical Modification. Eur. Polym. J. 2018, 102, 187–194. [Google Scholar] [CrossRef]
  20. Álvarez-Castillo, E.; Bengoechea, C.; Felix, M.; Guerrero, A. Protein-Based Bioplastics from Biowastes: Sources, Processing, Properties and Applications. In Bioplastics for Sustainable Development; Kuddus, M., Roohi, Eds.; Springer: Singapore, 2021; pp. 137–176. [Google Scholar]
  21. Mensitieri, G.; Di Maio, E.; Buonocore, G.G.; Nedi, I.; Oliviero, M.; Sansone, L.; Iannace, S. Processing and Shelf Life Issues of Selected Food Packaging Materials and Structures from Renewable Resources. New Chall. Food Preserv. 2011, 22, 72–80. [Google Scholar] [CrossRef]
  22. Newson, W.R.; Kuktaite, R.; Hedenqvist, M.S.; Gällstedt, M.; Johansson, E. Oilseed Meal Based Plastics from Plasticized, Hot Pressed Crambe Abyssinica and Brassica Carinata Residuals. J. Am. Oil Chem. Soc. 2013, 90, 1229–1237. [Google Scholar] [CrossRef]
  23. Felix, M.; Perez-Puyana, V.; Romero, A.; Guerrero, A. Development of Protein-Based Bioplastics Modified with Different Additives. J. Appl. Polym. Sci. 2017, 134, 45430–45438. [Google Scholar] [CrossRef]
  24. Mekonnen, T.; Mussone, P.; Khalil, H.; Bressler, D. Progress in Bio-Based Plastics and Plasticizing Modifications. J. Mater. Chem. A 2013, 1, 13379–13398. [Google Scholar] [CrossRef]
  25. Krochta, J.M. Proteins as Raw Materials for Films and Coatings: Definitions, Current Status, and Opportunities. Protein-Based Film. Coat. 2002, 1, 1–40. [Google Scholar]
  26. Martinez, A.W.; Caves, J.M.; Ravi, S.; Li, W.; Chaikof, E.L. Effects of Crosslinking on the Mechanical Properties, Drug Release and Cytocompatibility of Protein Polymers. Acta Biomater. 2014, 10, 26–33. [Google Scholar] [CrossRef] [PubMed]
  27. Reddy, N.; Reddy, R.; Jiang, Q. Crosslinking Biopolymers for Biomedical Applications. Trends Biotechnol. 2015, 33, 362–369. [Google Scholar] [CrossRef] [PubMed]
  28. Lee, H.; Min, S.C. Development of Antimicrobial Defatted Soybean Meal-Based Edible Films Incorporating the Lactoperoxidase System by Heat Pressing. J. Food Eng. 2014, 120, 183–190. [Google Scholar] [CrossRef]
  29. Wu, Q.; Sakabe, H.; Isobe, S. Processing and Properties of Low Cost Corn Gluten Meal/Wood Fiber Composite. Ind. Eng. Chem. Res. 2003, 42, 6765–6773. [Google Scholar] [CrossRef]
  30. Petraru, A.; Amariei, S. A Novel Approach about Edible Packaging Materials Based on Oilcakes—A Review. Polymers 2023, 15, 3431. [Google Scholar] [CrossRef] [PubMed]
  31. Popović, S.; Hromiš, N.; Šuput, D.; Bulut, S.; Romanić, R.; Lazić, V. Chapter 3—Valorization of by-Products from the Production of Pressed Edible Oils to Produce Biopolymer Films. In Cold Pressed Oils; Ramadan, M.F., Ed.; Academic Press: Cambridge, MA, USA, 2020; pp. 15–30. [Google Scholar]
  32. Mirpoor, S.F.; Giosafatto, C.V.L.; Porta, R. Biorefining of Seed Oil Cakes as Industrial Co-Streams for Production of Innovative Bioplastics. A Review. Trends Food Sci. Technol. 2021, 109, 259–270. [Google Scholar] [CrossRef]
  33. Żelaziński, T. Properties of Biocomposites from Rapeseed Meal, Fruit Pomace and Microcrystalline Cellulose Made by Press Pressing: Mechanical and Physicochemical Characteristics. Materials 2021, 14, 890. [Google Scholar] [CrossRef]
  34. Zhang, Y.; Liu, Q.; Rempel, C. Processing and Characteristics of Canola Protein-Based Biodegradable Packaging: A Review. Crit. Rev. Food Sci. Nutr. 2018, 58, 475–485. [Google Scholar] [CrossRef]
  35. Jang, S.-A.; Lim, G.-O.; Song, K.B. Preparation and Mechanical Properties of Edible Rapeseed Protein Films. J. Food Sci. 2011, 76, C218–C223. [Google Scholar] [CrossRef]
  36. Li, S.; Donner, E.; Thompson, M.; Zhang, Y.; Rempel, C.; Liu, Q. Preparation and Characterization of Cross-Linked Canola Protein Isolate Films. Eur. Polym. J. 2017, 89, 419–430. [Google Scholar] [CrossRef]
  37. Jiang, Y.; Simonsen, J.; Zhao, Y. Compression-Molded Biocomposite Boards from Red and White Wine Grape Pomaces. J. Appl. Polym. Sci. 2011, 119, 2834–2846. [Google Scholar] [CrossRef]
  38. Ben, Z.Y.; Samsudin, H.; Yhaya, M.F. Glycerol: Its Properties, Polymer Synthesis, and Applications in Starch Based Films. Eur. Polym. J. 2022, 175, 111377–111393. [Google Scholar] [CrossRef]
  39. Ullsten, N.H.; Gällstedt, M.; Hedenqvist, M.S. Chapter 5 Plasticizers for Protein-Based Materials. In Viscoelastic and Viscoplastic Materials; El-Amin, M.F., Ed.; IntechOpen: Rijeka, Croatia, 2016. [Google Scholar]
  40. Bonnaillie, L.M.; Zhang, H.; Akkurt, S.; Yam, K.L.; Tomasula, P.M. Casein Films: The Effects of Formulation, Environmental Conditions and the Addition of Citric Pectin on the Structure and Mechanical Properties. Polymers 2014, 6, 2018–2036. [Google Scholar] [CrossRef]
  41. Johansson, E.; Spencer, G.M.; Bettini, E.; Cho, S.-W.; Marttila, S.; Kuktaite, R.; Gällstedt, M.; Hedenqvist, M.S. Biobased Materials Production from Biodiesel Residuals of Rapeseed. ISRN Mater. Sci. 2012, 2012, 193541. [Google Scholar] [CrossRef]
  42. Lu, S.; Wang, X.; Lu, Q.; Zhang, X.; Kluge, J.A.; Uppal, N.; Omenetto, F.; Kaplan, D.L. Insoluble and Flexible Silk Films Containing Glycerol. Biomacromolecules 2010, 11, 143–150. [Google Scholar] [CrossRef] [PubMed]
  43. Zahari, I.; Ferawati, F.; Purhagen, J.K.; Rayner, M.; Ahlström, C.; Helstad, A.; Östbring, K. Development and Characterization of Extrudates Based on Rapeseed and Pea Protein Blends Using High-Moisture Extrusion Cooking. Foods 2021, 10, 2397. [Google Scholar] [CrossRef] [PubMed]
  44. Audic, J.-L.; Chaufer, B.; Daufin, G. Non-Food Applications of Milk Components and Dairy Co-Products: A Review. Lait 2003, 83, 417–438. [Google Scholar] [CrossRef]
  45. Wusigale; Liang, L.; Luo, Y. Casein and Pectin: Structures, Interactions, and Applications. Trends Food Sci. Technol. 2020, 97, 391–403. [Google Scholar] [CrossRef]
  46. He, W.; Zhu, G.; Gao, Y.; Wu, H.; Fang, Z.; Guo, K. Combining Renewable Eleostearic Acid and Eugenol to Fabricate Sustainable Plasticizer and Its Effect of Plasticizing on PVC. Chem. Eng. J. 2020, 380, 122532–122551. [Google Scholar] [CrossRef]
  47. Xu, X.; Yu, J.; Yang, F.; Li, Y.; Ou, R.; Liu, Z.; Liu, T.; Wang, Q. Preparation of degradable chemically cross-linked polylactic acid films and its application on disposable straws. Int. J. Biol. Macromol. 2023, 251, 126394–126405. [Google Scholar] [CrossRef]
  48. Song, L.; Chi, W.; Zhang, Q.; Ren, J.; Yang, B.; Cong, F.; Li, Y.; Wang, W.; Li, X.; Wang, Y. Improvement of Properties of Polylactic Acid/Polypropylene Carbonate Blends Using Epoxy Soybean Oil as an Efficient Compatibilizer. Int. J. Biol. Macromol. 2023, 253, 127407–127412. [Google Scholar] [CrossRef] [PubMed]
  49. Singha, S.; Mahmutovic, M.; Zamalloa, C.; Stragier, L.; Verstraete, W.; Svagan, A.J.; Das, O.; Hedenqvist, M.S. Novel Bioplastic from Single Cell Protein as a Potential Packaging Material. ACS Sustain. Chem. Eng. 2021, 9, 6337–6346. [Google Scholar] [CrossRef]
  50. Rombouts, I.; Lagrain, B.; Brunnbauer, M.; Koehler, P.; Brijs, K.; Delcour, J.A. Identification of Isopeptide Bonds in Heat-Treated Wheat Gluten Peptides. J. Agric. Food Chem. 2011, 59, 1236–1243. [Google Scholar] [CrossRef] [PubMed]
  51. Kong, J.; Yu, S. Fourier Transform Infrared Spectroscopic Analysis of Protein Secondary Structures. Acta Biochim. Et Biophys. Sin. 2007, 39, 549–559. [Google Scholar] [CrossRef]
  52. Ye, X.; Junel, K.; Gällstedt, M.; Langton, M.; Wei, X.-F.; Lendel, C.; Hedenqvist, M.S. Protein/Protein Nanocomposite Based on Whey Protein Nanofibrils in a Whey Protein Matrix. ACS Sustain. Chem. Eng. 2018, 6, 5462–5469. [Google Scholar] [CrossRef]
Biomolecules 14 00982 g001
Figure 1. Histogram of tensile properties (left) and stress/strain diagram (right) of meal/casein/water/glycerol blends without or with the addition of Na2SO3 and/or a denaturing agent (for specimens’ composition refers to Table 2).
Figure 1. Histogram of tensile properties (left) and stress/strain diagram (right) of meal/casein/water/glycerol blends without or with the addition of Na2SO3 and/or a denaturing agent (for specimens’ composition refers to Table 2).
Biomolecules 14 00982 g001
Biomolecules 14 00982 g002
Figure 2. First-derivative curve of TGA of rapeseed meal protein-based materials, RM, RM-R2, RM-D1, RM-D2, and RM-R2D2 14%.
Figure 2. First-derivative curve of TGA of rapeseed meal protein-based materials, RM, RM-R2, RM-D1, RM-D2, and RM-R2D2 14%.
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Biomolecules 14 00982 g003
Figure 3. Overlapped full FT-IR spectra of rapeseed-meal-based materials.
Figure 3. Overlapped full FT-IR spectra of rapeseed-meal-based materials.
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Figure 4. FT-IR spectra of amide I band of: (A) RM-R0, RM, RM-R2, RM-D1, RM-D2, and RM-R2D2 14% materials. (B) Rapeseed meal, RM-R0, RM, and RM-R2D2 14% materials (baseline corrected).
Figure 4. FT-IR spectra of amide I band of: (A) RM-R0, RM, RM-R2, RM-D1, RM-D2, and RM-R2D2 14% materials. (B) Rapeseed meal, RM-R0, RM, and RM-R2D2 14% materials (baseline corrected).
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Biomolecules 14 00982 g005
Figure 5. Scanning electron microscopy images of surface (left) and cryofracture cross-section (right) of specimens RM-R0, RM-D2, and RM-R2D2 14%.
Figure 5. Scanning electron microscopy images of surface (left) and cryofracture cross-section (right) of specimens RM-R0, RM-D2, and RM-R2D2 14%.
Biomolecules 14 00982 g005
Table 1. Examples of feedstock and processing used to produce protein-based biomaterial.
Table 1. Examples of feedstock and processing used to produce protein-based biomaterial.
FeedstockProcessingReference
Albumen protein isolated and crayfish flourInjection moulding[23]
Defatted Soybean mealCasting[28]
Gluten meal and Wood fiberExtrusion[31]
Crambe and Carinata Oilseed MealCompression moulding[23]
Rapeseed mealCompression moulding[19]
Rapeseed Meal, Fruit Pomace and Microcrystalline CelluloseCompression moulding[33]
Red and White Wine Grape PomacesCompression moulding[30]
Rapeseed Protein IsolatesCasting[34]
Rapeseed Protein IsolatesCasting[35]
Rapeseed Protein IsolatesCasting[36]
Table 2. Rapeseed meal-based (RM) specimen formulation.
Table 2. Rapeseed meal-based (RM) specimen formulation.
SampleFormulation
Rapeseed Meal/CompatibilizerGlycerolWater SolutionEpoxy-PEG
RM-R0100:027%Distilled water 7%-
RM04:0127%Distilled water 7%2× mol
RM-R104:0127%(Na2SO3 10%) 7%2× mol
RM-R204:0127%(Na2SO3 20%) 7%2× mol
RM-D104:0127%(UREA 2 M) 7%2× mol
RM-D204:0127%(Guanidine 1 M) 7%2× mol
RM-D304:0127%(SDS 3%) 7%2× mol
RM-R1D2 (7%)04:0127%(Na2SO3 10% + Guanidine 1 M) 7%2× mol
RM-R1D2 (14%)04:0127%(Na2SO3 10% + Guanidine 1 M) 14%2× mol
RM-R2D2 (7%)04:0127%(Na2SO3 20% + Guanidine 1 M) 7%2× mol
RM-R2D2 (14%)04:0127%(Na2SO3 20% + Guanidine 1 M) 14%2× mol
Table 3. Tensile mechanical properties of blends with different crosslinkers.
Table 3. Tensile mechanical properties of blends with different crosslinkers.
SampleMechanical Properties
Stress at Fracture
(N/mm2)		Elastic Modulus
(N/mm2)		Elongation at Fracture
(%)
RM0.86 ± 0.24172.23 ± 2.170.83 ± 0.11
RM-ES0.38 ± 0.0655.91 ± 9.932.18 ± 0.25
RM-NE0.81 ± 0.0260.94 ± 0.854.70 ± 0.56
Table 4. Tensile mechanical properties of blends with different concentrations of reducing agent (Na2SO3).
Table 4. Tensile mechanical properties of blends with different concentrations of reducing agent (Na2SO3).
SampleMechanical Properties
Stress at Fracture
(N/mm2)		Elastic Modulus
(N/mm2)		Elongation at Fracture
(%)
RM0.86 ± 0.24172.23 ± 2.170.83 ± 0.11
RM-R12.00 ± 0.37234.82 ± 8.151.24 ± 0.37
RM-R21.13 ± 0.06103.60 ± 8.661.92 ± 0.06
Table 5. Tensile mechanical properties of blends containing denaturing agents (Urea, guanidinium chloride, Sodium Dodecyl Sulphate (SDS)).
Table 5. Tensile mechanical properties of blends containing denaturing agents (Urea, guanidinium chloride, Sodium Dodecyl Sulphate (SDS)).
SampleMechanical Properties
Stress at Fracture
(N/mm2)		Elastic Modulus
(N/mm2)		Elongation at Fracture
(%)
RM0.86 ± 0.24172.23 ± 2.170.83 ± 0.11
RM-D10.90 ± 0.2275.67 ± 2.001.96 ± 0.35
RM-D20.82 ± 0.1995.17 ± 0.101.70 ± 0.33
RM-D30.59 ± 0.1570.35 ± 1.771.49 ± 0.33
Table 6. Tensile mechanical properties of blends containing sodium sulfite and guanidinium chloride in different percentages.
Table 6. Tensile mechanical properties of blends containing sodium sulfite and guanidinium chloride in different percentages.
SampleMechanical Properties
Stress at Fracture
(N/mm2)		Elastic Modulus
(N/mm2)		Elongation at Fracture (%)
RM-R1D2 7%0.85 ± 0.13214.18 ± 4.270.88 ± 0.08
RM-R1D2 14%1.24 ± 0.20216.89 ± 0.981.20 ± 0.06
RM-R2D2 7%1.87 ± 0.34277.99 ± 1.951.38 ± 0.27
RM-R2D2 14%1.53 ± 0.20257.71 ± 9.400.18 ± 0.28
Table 7. Area (%) of the resolved peaks (Figure S2) present in the amide I region of the rapeseed meal and of the materials RM, RM-R0, and RM-R2D2 14%.
Table 7. Area (%) of the resolved peaks (Figure S2) present in the amide I region of the rapeseed meal and of the materials RM, RM-R0, and RM-R2D2 14%.
Peak
(ῦ, cm−1)		A%
Rapeseed Meal		A%
RM		A%
RM-R0		A%
RM-R2D2 14%
1622–162410.428.322.2117.4
1662–166577.030.560.3958.1
1711–172912.339.615.5422.2
17450.31.61.862.4
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Aquilia, S.; Rosi, L.; Pinna, M.; Bianchi, S.; Giurlani, W.; Bonechi, M.; Ciardelli, F.; Papini, A.M.; Bello, C. Study of the Preparation and Properties of Chemically Modified Materials Based on Rapeseed Meal. Biomolecules 2024, 14, 982. https://doi.org/10.3390/biom14080982

AMA Style

Aquilia S, Rosi L, Pinna M, Bianchi S, Giurlani W, Bonechi M, Ciardelli F, Papini AM, Bello C. Study of the Preparation and Properties of Chemically Modified Materials Based on Rapeseed Meal. Biomolecules. 2024; 14(8):982. https://doi.org/10.3390/biom14080982

Chicago/Turabian Style

Aquilia, Sara, Luca Rosi, Michele Pinna, Sabrina Bianchi, Walter Giurlani, Marco Bonechi, Francesco Ciardelli, Anna Maria Papini, and Claudia Bello. 2024. "Study of the Preparation and Properties of Chemically Modified Materials Based on Rapeseed Meal" Biomolecules 14, no. 8: 982. https://doi.org/10.3390/biom14080982

APA Style

Aquilia, S., Rosi, L., Pinna, M., Bianchi, S., Giurlani, W., Bonechi, M., Ciardelli, F., Papini, A. M., & Bello, C. (2024). Study of the Preparation and Properties of Chemically Modified Materials Based on Rapeseed Meal. Biomolecules, 14(8), 982. https://doi.org/10.3390/biom14080982

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