Physicochemical characterization and amino acid profiling of Ferula foetida (Bunge) regel resin cultivated in the Turkestan region

Caracterização físico-química e perfil de aminoácidos da resina de Ferula Foetida (Bunge) regel cultivada na região do Turquestão

Abstract

This study presents the results of physicochemical and biochemical analysis of the root resin of Ferula foetida (Bunge) Regel. (Apiaceae), cultivated in the Turkestan region of the Republic of Kazakhstan. The main physicochemical parameters of the resin, including moisture, ash, and protein contents, were determined. The moisture content was 8.84%, ash content 1.28%, protein content 5.42%, and protein nitrogen content 0.86%. The amino acid composition of resin proteins was determined using high-performance liquid chromatography (HPLC). A total of 17 amino acids, including essential amino acids, were identified. The total amino acid content was 621.38 mg/g, of which essential amino acids accounted for 225.75 mg/g. The highest concentrations were observed for leucine, alanine, aspartic acid, and proline. Infrared spectroscopic analysis confirmed the presence of characteristic functional groups of protein compounds. The obtained results indicate the presence of protein components and biologically active compounds in the resin of Ferula foetida and confirm the potential of this plant material for further biochemical studies.

Keywords:
Ferula foetida; resin; amino acid composition; protein; HPLC; physicochemical analysis

Resumo

Este estudo apresenta os resultados da análise físico-química e bioquímica da resina da raiz de Ferula foetida (Bunge) Regel (Apiaceae), cultivada na região do Turquestão, na República do Cazaquistão. Os principais parâmetros físico-químicos da resina, incluindo os teores de umidade, cinzas e proteínas, foram determinados. O teor de umidade foi de 8,84%, o de cinzas de 1,28%, o de proteínas de 5,42%, e o de nitrogênio proteico, de 0,86%. A composição de aminoácidos das proteínas da resina foi determinada por cromatografia líquida de alta eficiência (CLAE). Um total de 17 aminoácidos, incluindo aminoácidos essenciais, foi identificado. O teor total de aminoácidos foi de 621,38 mg/g, dos quais 225,75 mg/g corresponderam a aminoácidos essenciais. As maiores concentrações foram observadas para leucina, alanina, ácido aspártico e prolina. A análise espectroscópica por infravermelho confirmou a presença de grupos funcionais característicos de compostos proteicos. Os resultados obtidos indicam a presença de componentes proteicos e compostos biologicamente ativos na resina de Ferula foetida e confirmam o potencial desse material vegetal para futuros estudos bioquímicos.

Palavras-chave:
Ferula foetida; resina; composição de aminoácidos; proteína; HPLC; análise físico-química

1. Introduction

Ferula foetida (Bunge) Regel is a representative of one of the largest and taxonomically as well as biochemically significant genera within the Apiaceae family. The genus is widely distributed across the Irano-Turanian floristic region, which represents a major center of species diversity and endemism (Korovin, 1968; Pimenov and Ostroumova, 2012). The highest species richness of Ferula is concentrated in Central Asia, as well as in adjacent territories of Iran and Afghanistan, where xerophytic plant communities have evolved under arid and semi-arid climatic conditions. F. foetida is considered a typical Irano-Turanian floristic element, and its distribution range extends over a substantial part of the ancient Mediterranean region. Such a broad geographical distribution indicates its high ecological plasticity, environmental resilience, and considerable adaptive potential (Pavlov, 1961).

F. foetida is a perennial monocarpic plant reaching 2–3 m in height, characterized by a thick spindle-shaped root containing a milky latex. From this latex, a gum-resin is obtained that possesses a distinctive pungent odor due to the presence of sulfur-containing compounds (Iranshahy and Iranshahi, 2011). In Kazakhstan, the species is widely distributed across Mangyshlak, the Aral Sea region, the Kyzylkum Desert, the Turkestan region, the Chu-Ili Mountains, and the Karatau range, where it forms stable natural populations (Pavlov, 1961; Mota et al., 2020).

The resin of F. foetida is of particular scientific and practical interest, as it contains a complex of biologically active substances, including sulfur-containing compounds, sesquiterpene coumarins, essential oils, resinous substances, and other constituents that determine its pharmacological properties and biological activity (Iranshahy and Iranshahi, 2011; Mishra et al., 2019; Mota et al., 2020).

Despite the substantial body of research devoted to the investigation of secondary metabolites in plants of the genus Ferula, the protein components of the resin and their amino acid composition remain insufficiently studied. Proteins are essential biopolymers that perform structural, enzymatic, and regulatory functions in living organisms and play a central role in metabolic processes (Voet and Voet, 2016; Nelson and Cox, 2017; Damodaran and Parkin, 2017; Mustafina et al., 2025; Jamalova Ne'matilla Qizi et al.., 2025).

The amino acid composition of proteins is a key parameter determining their biological value, as well as their physicochemical and functional properties. Particular importance is attributed to essential amino acids, such as leucine, valine, isoleucine, threonine, phenylalanine, and lysine, which cannot be synthesized by the human body and must be obtained from external sources (Wu, 2016; Millena and Sagum, 2018).

Currently, one of the most accurate and informative methods for determining the amino acid composition of proteins is high-performance liquid chromatography (HPLC), which enables both qualitative and quantitative analysis of amino acids with high precision and reproducibility (Vakhrushev and Gorbunov, 2016; Siqueira et al., 2017; Zhang et al., 2021; Henderson et al., 2000; Liu et al., 2019). The application of this method allows for detailed characterization of the amino acid profile of proteins and evaluation of their biological value.

Therefore, the investigation of the protein composition and amino acid profile of the resin of F. foetida cultivated in the Turkestan region of the Republic of Kazakhstan is of considerable scientific and practical interest and represents a relevant task in the modern biochemistry of plant-derived raw materials.

The present study aimed to determine the total protein content, analyze the amino acid composition of resin proteins, and perform Fourier-transform infrared (FTIR) spectroscopic analysis of the protein fractions of F. foetida resin using high-performance liquid chromatography.

2. Materials and Methods

The Ferula foetida plants were cultivated under plantation conditions in the Turkestan region of the Republic of Kazakhstan. The region is characterized by a sharply continental, hot and dry climate, with relatively short and mild winters and hot, dry summers. In the Turkestan area, the average annual air temperature is approximately 12.8 °C, while the mean monthly temperature in July reaches approximately 28.4–28.7 °C. Annual precipitation is relatively low, at approximately 238 mm, with most precipitation occurring during the colder part of the year. The summer period generally extends from May to September and is characterized by high temperatures, low atmospheric humidity, and high solar radiation.

The soils of the region are predominantly light-textured and include light loamy, sandy-loam, and in some areas loamy soils, which are characteristic of the arid and semi-arid landscapes of southern Kazakhstan. These soils generally have good drainage and relatively low moisture-retention capacity, conditions that are favorable for the development of the deep root system of F. foetida. The combination of dry climatic conditions, high solar radiation, and well-drained soils provides environmental conditions suitable for the growth and resin formation of F. foetida. These climatic and edaphic conditions were considered as important environmental factors influencing plant growth and resin production (Figure 1).The underground plant organs used for resin extraction are shown in Figure 2. The distribution of herbarium specimens by year of collection is presented in Table 1, providing a historical perspective on the occurrence and collection of F. foetida in the region.

Figure 1
Cultivation of Ferula foetida under plantation conditions: (a) general view of the plant; (b) plant arrangement; (c) Ferula foetida plantation; (d) row planting of the plants.

Figure 2
Underground organs of Ferula foetida used for resin extraction: (a) root; (b) root in soil with measurement.

Table 1
Ferula foetida herbarium specimens from South-East Kazakhstan, by year of collection.

Year	Collector(s)	No. of specimens	Locality / notes
1939	N.V. Pavlov (South Kazakhstan Expedition of the Kazakh Branch of the USSR Academy of Sciences)	1	Trans-Karatau desert near Chulak-Kurgan settlement, wormwood plain (Muyunkum/Balkhash/Betpak-Dala region, South-East Kazakhstan); coll. No. 176, 6 May 1939
1951	N.V. Pavlov (expedition of the Academy of Sciences of the Kazakh SSR)	1	Chu-Iley Mountains, Dzhambul Region (Northern/Central Tian Shan, South-East Kazakhstan); coll. No. 61, 6 May 1951
1977	M.G. Pimenov, M.E. Pimenova, Yu.V. Baranova	1	Chu-Iley Mountains, near Khantau station, foothill plain, Dzhambul Region (South-East Kazakhstan); coll. No. 93, 27 April 1977

• Source: Seregin (2026).

For physicochemical analysis, the resin samples were ground to a homogeneous state using a porcelain mortar and pestle. A representative analytical sample was selected using the quartering method. The prepared samples were stored in airtight glass containers at room temperature until analysis.

2.1. Determination of resin moisture content

The moisture content of the resin was determined gravimetrically by drying the sample to a constant weight. For the analysis, approximately 0.5 g of resin was placed into a pre-dried and weighed crucible and dried in a drying oven at 100–105 °C for 4 hours. After drying, the crucible with the sample was cooled in a desiccator for 10–15 minutes and weighed on an analytical balance with an accuracy of ±0.0001 g. Drying and weighing were repeated until a constant weight was achieved, defined as a difference of no more than 0.001 g between two consecutive weighings.

The moisture content (W, %) was calculated using the following Formula 1:

$$\text{W}=\left(\left({\text{m}}_1-{\text{m}}_2\right)/\text{m}\right)\times 100$$ (1)

where:

m₁ – mass of the crucible with the sample before drying, g;

m₂ – mass of the crucible with the sample after drying, g;

m – mass of the resin sample, g.

2.2. Determination of resin ash content

The ash content of the resin was determined by the dry ashing method. A resin sample weighing 1.0–1.2 g was placed into a pre-calcined and weighed porcelain crucible. Ashing was carried out in a muffle furnace at 600–800 °C for 3 hours until all organic matter was completely removed. After ashing, the crucibles were cooled in a desiccator and weighed on an analytical balance.

The ash content (A, %) was calculated using the following Formula 2:

$$\text{A}=\left(\left({\text{m}}_2-{\text{m}}_0\right)/\text{m}\right)\times 100$$ (2)

where:

m₀ – mass of the empty crucible, g;

m₂ – mass of the crucible with ash, g;

m – mass of the resin sample, g.

2.3. Determination of protein content

The protein content was determined after preliminary mineralization of the resin sample with concentrated sulfuric acid, followed by the quantification of protein nitrogen using a colorimetric method with Nessler’s reagent. For the analysis, a resin sample weighing 0.401 g was placed into a heat-resistant flask, and concentrated sulfuric acid was added. The sample was then mineralized by heating until complete decomposition of organic matter and formation of a clear solution. After cooling, the mineralizate was diluted to a predetermined volume with distilled water. Protein nitrogen was measured spectrophotometrically using a V-5000 Metash spectrophotometer (Metash Instruments Co., China) at a wavelength of 400 nm.

The protein content (%) was calculated using the Formula 3:

$$\text{Protein (\%)}=\text{N}\times \mathrm{6,25}$$ (3)

where:

• N – protein nitrogen content, %;

• 6.25 – nitrogen-to-protein conversion factor.

2.4. Isolation and purification of resin proteins

For protein isolation, the resin sample was extracted with a 0.2 M sodium hydroxide solution (NaOH) under constant stirring on a magnetic stirrer at 1000 rpm for 2 hours. To enhance extraction efficiency, ultrasonic treatment was additionally applied for 15 minutes. The obtained extracts were centrifuged at 6000 rpm for 20 minutes. Proteins were precipitated by adding ammonium sulfate to 80% saturation and incubated at 4 °C for 24 hours. The protein precipitate was separated by centrifugation, dissolved in a minimal volume of NaOH solution, and dialyzed against distilled water for 24 hours. The resulting proteins were then lyophilized for further use (Wang et al., 2018).

2.5. Determination of amino acid composition

The amino acid composition of the resin proteins was determined by high-performance liquid chromatography (HPLC). Before analysis, the proteins were subjected to acid hydrolysis in a hydrochloric acid solution under vacuum at 160 °C for 70 minutes. After hydrolysis, amino acids were derivatized with phenylisothiocyanate to form phenylthiocarbamyl derivatives (Song et al., 2019).

Chromatographic analysis was performed using an Agilent Technologies 1200 system (Agilent, USA) equipped with a diode-array detector. The analysis conditions were as follows: column – Discovery HS C18 (75 × 4.6 mm); mobile phase A – 0.14 M sodium acetate + 0.05% triethylamine (pH 6.4); mobile phase B – acetonitrile; flow rate – 1.2 mL/min; detection wavelength – 269 nm; injection volume – 5 µL.

Amino acids were identified by comparing their retention times with those of standard samples. Quantitative determination was carried out using the external standard method (Henderson and Brooks, 2010).

2.6. Fourier-Transform Infrared (FTIR) spectroscopic analysis

The FTIR spectra of the proteins were recorded using a Perkin-Elmer System 2000 Fourier-transform infrared spectrometer (PerkinElmer, USA). Samples were prepared in the form of KBr pellets, and spectra were recorded in the range of 4000–400 cm⁻¹.

Statistical Analysis. Experimental data were statistically processed using OriginPro 2021 software (OriginLab Corporation, 2021, USA). All measurements were performed in triplicate. Results are presented as mean (M) ± standard deviation (SD). The significance of differences was assessed using Student’s t-test at a significance level of p ≤ 0.05.

3. Results and Discussion

3.1. Physicochemical properties of Ferula foetida resin

The moisture content of Ferula foetida resin was determined to be 8.84%. The low moisture content indicates a high degree of drying of the analyzed sample and ensures the stability of its chemical composition during storage. It is well known that moisture content is an important quality parameter for plant-derived raw materials, as it affects both the stability and preservation of biologically active compounds (Belitz et al., 2018) (Table 2).

Table 2
Results of moisture determination of Ferula foetida resin.

Research Object	Crucible Weight, g	Crucible Weight with Initial Sample, g	Sample Weight, g	Weighing Results After Drying	Dry Matter, %
Resin from Ferula Root	17,562	18,071	0,509	18,026	8,84

The ash content in the studied sample is 1.28%, reflecting the total mineral matter (Table 3). Ash content is an important indicator of the purity of plant raw materials and allows for the assessment of inorganic components (AOAC, 2019).

Table 3
Results of ash content determination of Ferula foetida resin.

Crucible Weight, g	Crucible Weight with Initial Sample, g	Sample Weight, g	Weighing Results After Incineration, g	Ash, %
16,763	17,927	1,164	16,778	1,28

The protein content in Ferula foetida resin was 5.42%, with protein nitrogen at 0.86% (Table 4). Plant-derived proteins are important biopolymers that perform structural and functional roles and also serve as a source of amino acids (Voet and Voet, 2016; Nelson and Cox, 2017).

Table 4
Results of total protein analysis of Ferula foetida resin.

Research Object	Sample Weight, g	Aliquot, mL	400 nm	Protein, %	Nitrogen, %
Root Resin of Ferula	0,401	0,3	0,116	5,42	0,86

The obtained results indicate the presence of protein compounds in the studied sample. Plant-derived proteins play an important role in the biological activity of plant raw materials, as they serve as a source of amino acids and participate in various metabolic processes.

Thus, the results of the physicochemical analysis show that F. foetida resin is characterized by low moisture content and minimal mineral impurities while containing protein components, confirming the potential of this sample for further biochemical studies.

3.2. Amino acid composition of proteins in F. foetida resin

The amino acid composition of proteins in F. foetida resin was determined using high-performance liquid chromatography (HPLC). Amino acids were identified by comparing the retention times of peaks in the sample with those of a standard amino acid mixture (Figure 3). HPLC is one of the most accurate and widely used methods for analyzing the amino acid composition of proteins (Vakhrushev and Gorbunov, 2016; Henderson et al., 2000; Liu et al., 2019; Zhang et al., 2021).

Figure 3
HPLC chromatograms of amino acids after derivatization with phenylisothiocyanate: (a) standard amino acid mixture; (b) Ferula foeti da resin sample.

The analysis revealed the presence of 17 amino acids, including essential ones. The total amino acid content was 621.38 mg/g, of which essential amino acids accounted for 225.75 mg/g, indicating the biological value of the proteins in the studied sample.

The highest contents were observed for leucine (72.26 mg/g), alanine (64.28 mg/g), aspartic acid (63.96 mg/g), and proline (62.04 mg/g). The high levels of these amino acids suggest a significant proportion of structural and functional protein components. It is known that leucine plays an important role in metabolic processes and protein synthesis (Wu, 2016).

Among essential amino acids, considerable amounts were found for threonine (44.97 mg/g), valine (37.43 mg/g), phenylalanine (25.03 mg/g), and lysine (18.20 mg/g). Essential amino acids are particularly important because they cannot be synthesized by the human body and must be obtained from external sources (Udenigwe and Aluko, 2012; FAO, 2013).

The results indicate the presence of a complete set of essential amino acids, highlighting the biological value of Ferula foetida resin proteins. Similar data on the presence of essential amino acids in plant-derived proteins have been reported in the literature (Niimi et al., 2017; Millena and Sagum, 2018). The quantitative amino acid content was calculated based on chromatographic peak areas using the external standard method. The results of the quantitative amino acid determination are presented in Table 5.

Table 5
Amino acid composition of proteins in Ferula foetida resin.

Amino Acid	Amino acid concentration, mg/g
Nonessential amino acids
Monoaminomonocarboxylic acids
1. Glycine, Gly	24,04
2. Alanine, Ala	64,28
Hydroxy monoaminocarboxylic acid
3. Serine, Ser	30,89
Monoaminodicarboxylic acids
4. Aspartic acid, Asp	63,96
5. Glutamic acid, Glu	46,45
Aromatic amino acid
6. Tyrosine, Tyr	37,51
Total nonessential AA	267,13
Essential amino acids
Monoaminomonocarboxylic acids
1. Valine, Val	37,43
2. Isoleucine, Ile	15,55
3. Leucine, Leu	72,26
Hydroxy monoaminocarboxylic acid
4. Threonine, Thr	44,97
Sulfur‑containing acid
5. Methionine, Met	12,31
Diaminomonocarboxylic acid
6. Lysine, Lys	18,20
Aromatic amino acids
7. Phenylalanine, Phe	25,03
Total essential AA	225,75
Partially replaceable amino acids
Sulfur‑containing acid
1. Cysteine, Cys	24,55
Heterocyclic acids (imino acids)
2. Proline, Pro	62,04
3. Histidine, His	27,07
Diaminomonocarboxylic acid
4. Arginine, Arg	14,83
Total partially replaceable AA	128,49
Total amino acids	621,38

• Note: –essential amino acids. Amino acid content was determined by high-performance liquid chromatography (HPLC) following acid hydrolysis of proteins and derivatization with phenylisothiocyanate. Amino acid identification was carried out by comparing the retention times of peaks in the sample with those of a standard amino acid mixture. Quantitative amino acid content was calculated using the external standard method and expressed in mg/g of the studied sample. Experimental data processing was performed using OriginPro 2021 software (OriginLab Corporation, 2021, USA).

The total amino acid content was 621.38 mg/g, of which the essential amino acids accounted for 225.75 mg/g, representing 36.3% of the total amino acid content.

The analysis revealed that the highest amino acid contents in Ferula foetida resin were observed for leucine (72.26 mg/g), alanine (64.28 mg/g), aspartic acid (63.96 mg/g), and proline (62.04 mg/g), highlighting their key role in the protein structure of the studied sample. Among essential amino acids, leucine (72.26 mg/g), threonine (44.97 mg/g), valine (37.43 mg/g), and phenylalanine (25.03 mg/g) were most abundant. The total content of branched-chain amino acids (leucine, valine, isoleucine) was 125.24 mg/g, representing approximately 20.1% of the total amino acids.

Moderate levels were observed for glutamic acid (46.45 mg/g), tyrosine (37.51 mg/g), serine (30.89 mg/g), and histidine (27.07 mg/g), while methionine (12.31 mg/g) was the least abundant, consistent with the typical profile of plant-derived proteins. The predominance of acidic amino acids, such as aspartic and glutamic acids, underscores their important role in maintaining the structural and functional properties of proteins.

Overall, the high content of leucine and other essential amino acids demonstrates the biological value of Ferula foetida resin proteins. These findings indicate that the resin proteins have a balanced amino acid composition and contain a complete set of essential amino acids, confirming the potential of this plant material as a source of biologically active compounds.

3.3. FTIR spectroscopic analysis of ferula foetida resin proteins

FTIR spectroscopic analysis of Ferula foetida resin proteins revealed characteristic absorption bands corresponding to functional groups of protein compounds (Figure 4). The absorption band at 3299 cm⁻¹ corresponds to the stretching vibrations of N–H bonds in amino groups, which are typical for proteins (Smith, 2011).

Figure 4
FTIR spectrum of proteins in Ferula foetid a resin.

Absorption bands at 2924 cm⁻¹ are attributed to C–H stretching vibrations of aliphatic groups. Bands observed at 1659 cm⁻¹ (amide I) and 1554 cm⁻¹ (amide II) correspond to peptide bond vibrations, confirming the presence of protein structures (Smith, 2011; Damodaran and Parkin, 2017).

The presence of these absorption bands indicates amide groups characteristic of protein compounds. The results are consistent with the amino acid analysis and confirm the protein nature of the studied material. The FTIR spectrum of the studied sample is presented in Figure 4.

The physicochemical characteristics of Ferula foetida resin obtained in the present study can be compared with previously reported data for related Ferula species. In a recent study of Ferula assa-foetida oleo-gum-resin, protein was reported at 13.45–14.28 g/100 g, whereas the present F. foetida resin contained 5.42% protein. The lower protein concentration observed in our samples may be related to interspecific differences, geographical origin, cultivation conditions, stage of plant development, resin processing, and differences in analytical procedures. The moisture content of the present sample (8.84%) was also relatively low, suggesting a comparatively dry resin material. Such differences highlight the influence of species and environmental conditions on the physicochemical characteristics of Ferula oleo-gum-resins (Attarian et al., 2024).

The low ash content recorded in the present study (1.28%) indicates a relatively low proportion of inorganic residues in the purified resin. Previous investigations of Ferula oleo-gum-resins have demonstrated considerable variation in their chemical composition according to species and geographic origin. For example, Jalali et al. (2011) reported that the oleo-gum-resin of Ferula gummosa consisted predominantly of ethanol-soluble terpenes and terpenoids, while the insoluble fraction contained an arabinogalactan structurally associated with a protein complex. These findings indicate that Ferula resins are chemically complex materials and that the relative proportions of their components may differ substantially among species and growing regions (Jalali et al., 2011; Mamadalieva et al., 2026).

The amino acid composition observed in the present study also shows both similarities and differences compared with previously investigated Ferula species. In F. foetida resin, leucine (72.26 mg/g), alanine (64.28 mg/g), aspartic acid (63.96 mg/g), and proline (62.04 mg/g) were the predominant amino acids. In contrast, a comparative metabolomic investigation of F. assa-foetida, F. jaeschkeana, and commercial F. assa-foetida oleo-gum-resin identified serine, arginine, asparagine, isoleucine, and phenylalanine among the major amino acids quantified. The differences in the dominant amino acids may be associated with species-specific metabolic characteristics, plant tissue, environmental conditions, physiological stage, and analytical methodology (Singh et al., 2023).

The essential amino acid fraction in the present study amounted to 225.75 mg/g, corresponding to 36.3% of the total amino acids. The relatively high concentration of leucine, together with threonine, valine, phenylalanine, and lysine, demonstrates that the resin contains a diverse set of essential amino acids. Nevertheless, direct quantitative comparisons with previous Ferula studies should be interpreted cautiously because published investigations have used different plant materials, extraction procedures, analytical platforms, and units of expression. For instance, Singh et al. (2023) applied UHPLC-PDA-QTOF-IMS-based metabolomic profiling to different tissues and commercial resin samples of F. assa-foetida, whereas the present study specifically examined root resin of cultivated F. foetida using HPLC.

The protein-related characteristics observed in the present study are also consistent with previous structural investigations of Ferula oleo-gum-resins. Saeidy et al. (2018) demonstrated that the gum fraction isolated from F. assa-foetida oleo-gum-resin contained an arabinogalactan structure associated with protein. Similarly, Jalali et al. (2011) reported an arabinogalactan structurally associated with a protein complex in F. gummosa oleo-gum-resin. These findings provide additional evidence that protein-associated polysaccharide components can occur in Ferula resinous materials and are consistent with the protein-related FTIR bands detected in the present study (Saeidy et al., 2018; Jalali et al., 2011).

Overall, comparison with previously published studies suggests that F. foetida resin cultivated in the Turkestan region possesses a distinct physicochemical and amino acid profile while sharing several general compositional characteristics with related Ferula oleo-gum-resins. The relatively low moisture and ash contents, together with the substantial proportion of essential amino acids, provide useful baseline information for further comparative biochemical and phytochemical studies of F. foetida from Central Asia.

Thus, the results of the physicochemical analysis, amino acid profiling, and FTIR spectroscopy confirm the presence of protein compounds in Ferula foetida resin and indicate the potential for further investigation of this plant material.

4. Conclusion

The conducted study established the physicochemical and biochemical characteristics of the root resin of Ferula foetida (Bunge) Regel., cultivated in the Turkestan region of the Republic of Kazakhstan. It was determined that the moisture content of the studied resin is 8.84%, and the ash content is 1.28%, indicating low levels of mineral impurities and a high degree of purity of the plant raw material. The protein content was 5.42%, with protein nitrogen at 0.86%, confirming the presence of protein components in the resin. Amino acid analysis showed that the resin proteins contain 17 amino acids, including essential ones. The total amino acid content was 621.38 mg/g, of which essential amino acids accounted for 225.75 mg/g. The highest contents were observed for leucine, alanine, aspartic acid, and proline. The presence of a complete set of essential amino acids indicates the biological value of the proteins in the studied sample. FTIR spectroscopic analysis confirmed the presence of characteristic functional groups of protein compounds, including amino and carbonyl groups, which is consistent with the amino acid analysis results.

Thus, Ferula foetida resin is characterized by the presence of protein compounds and a balanced amino acid composition, confirming the potential of this plant material as a source of biologically active compounds and justifying further investigation of its chemical composition and biological properties.

The data presented in the paper were obtained during the dissertation research on the topic "Phytocenological studies of Ferula foetida (Bunge) Regel in the Turkestan region.

Acknowledgments

This research was conducted within the framework of the state research program “Digital Nature” (2025–2029), supported by the Academy of Sciences of the Republic of Uzbekistan. The authors express their sincere gratitude to the Laboratory of Molecular Phylogeny and Biogeography for their contributions and scientific support under the research initiative titled “The Phenomenon of Endemism in Central Uzbekistan and Its Molecular-Genetic Basis.” We also thank the fieldwork team and Fundamental Research Project No. FL-9524115063, “Bio-climatic and geospatial analysis of the resource potential, adaptive mechanisms, and distribution patterns of medicinal plants of the Republic (with a case study on the genus Ferula L.)”, for providing additional scientific guidance and resources.

Data Availability Statement

The data supporting the findings of this study are available from the corresponding author upon reasonable request.

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*

e-mail: [e-mail]; [e-mail]

Editor:

Takako Matsumura Tundisi

Publication Dates

• Publication in this collection
  19 Oct 2026
• Date of issue
  2026

History

• Received
  19 July 2026
• Accepted
  02 Sept 2026