Functional Properties Of Protein Isolates Research Articles

Pecan (Carya illinoinensis (Wangenh.) K. Koch) nuts as an emerging source of protein: extraction, physicochemical and functional properties.

The increasing demand for sustainable alternatives to traditional protein sources, driven by population growth, underscores the importance of protein in a healthy diet. Pecan (Carya illinoinensis (Wangenh.) K. Koch) nuts are currently underutilized as plant-based proteins but hold great potential in the food industry. However, there is insufficient information available on pecan protein, particularly its protein fractions. This study aimed to explore the physicochemical and functional properties of protein isolate and the main protein fraction glutelin extracted from pecan nuts. The results revealed that glutelin (820.67 ± 69.42 g kg-1) had a higher crude protein content compared to the protein isolate (618.43 ± 27.35 g kg-1), while both proteins exhibited amino acid profiles sufficient for adult requirements. The isoelectric points of protein isolate and glutelin were determined to be pH 4.0 and pH 5.0, respectively. The denaturation temperature of the protein isolate (90.23 °C) was higher than that of glutelin (87.43 °C), indicating a more organized and stable conformation. This is further supported by the fact that the protein isolate had a more stable main secondary structure than glutelin. Both proteins demonstrated improved solubility, emulsifying, and foaming properties at pH levels deviating from their isoelectric points in U-shaped curves. Compared to the protein isolate, glutelin displayed superior water and oil absorption capacity along with enhanced gelling ability. The protein isolate and glutelin from pecan nuts exhibited improved stability and competitive functional properties, respectively. The appropriate utilization of these two proteins will support their potential as natural ingredients in various food systems. © 2024 Society of Chemical Industry.

Evaluation of physicochemical and functional properties of protein isolates from 5 edible mushroom species

Evaluation of physicochemical and functional properties of protein isolates from 5 edible mushroom species

Effect of pH‐shifting treatment on the structural characteristics and nutritional quality of the ultrasonically extracted protein isolate from soybean meal

AbstractSoybean meal is an underutilized byproduct of the soybean oil processing industry, which is rich in high quality protein but mostly used as an animal feed. Valorization of soybean meal on a large scale is possible by extracting protein isolate and modifying its structural characteristics through pH‐shifting or ultrasonic treatment, which has a direct association with the better functional properties of protein isolate. The present study aimed to evaluate the impact of pH‐shifting treatment on the structural characteristics and nutritional quality of ultrasonically extracted soybean meal protein isolate (SMPI). The results showed that the pH shifted SMPI had higher hydrophobicity (60.5–104.3) and free sulfhydryl group (22.67–24.45 μmol/g) than without pH shifted SMPI (53.5 and 19.67 μmol/g, respectively). The fluorescence intensity of the SMPI treated at extreme acidic and alkaline pH was higher than that of other pH‐treated samples. The ꞵ‐sheet (39.68%) components of SMPI treated at pH 10 showed the highest value when compared to other pH‐treated (38.18–39.26%). The alkaline pH‐treated sample had higher concentration of essential amino acids (36.16 g/100 g) than other acidic or near neutral pH‐treated sample (30.06–32.30 g/100 g). The quality parameters such as biological value (67.62), and amino acid index (72.77) were higher for the SMPI treated at pH 10 as compared to the SMPI treated at other pH conditions. Hence, the pH‐treatment method can be utilized as an effective technique to improve the characteristics of SMPI, which will increases its applications in various food sectors.Practical ApplicationsThe current investigation demonstrated that pH‐shifting treatment had a substantial impact on the structural and nutritional quality of the soybean meal protein isolate extracted by ultrasonication. Improvements in soybean meal protein's surface hydrophobicity, free sulfhydryl groups, and secondary structural components will expand its uses in the dairy, bread, meat, and infant food development industries, among other food sectors as these structural changes improve the functionality of protein. Furthermore, the treatment of soybean meal protein isolate with pH shifting led to a considerable increase in nutritional quality, as measured by the essential amino acid composition, essential amino acid index, and protein efficiency ratio, which is expected to increase its utilization in novel food product development.

Polyphenol removal with ultrasound-assisted ethanol extraction from defatted walnut powder: optimization of conditions and effect on functional properties of protein isolates.

Walnut kernels are high in polyphenols (PPs), which cause low protein solubility, limiting the use of walnut protein in the food industry. To obtain the best technical parameters of the dephenolization treatment, the defatted walnut powder was dephenolized using ultrasound-assisted ethanol extraction (UAE), and the response surface optimization was performed on the basis of single factor. On this basis, the effects of dephenolization on the solubility, emulsifying properties and foaming properties of walnut protein isolates (WPIs) were compared to those of defatted walnut powder without dephenolization. The results showed that PP extraction in the UAE could significantly increase PP yield. The optimal process parameters were as follows: 51% (v/v) ethanol concentration, 140 W ultrasound power, 10 min extraction time, 30 °C ultrasound temperature, and a material-liquid ratio of 1:30 (w/v). The results revealed that the UAE dephenolization treatment significantly improved the functionality of WPI and that the functionality of the dephenolized WPI by UAE was superior to that of the protein without dephenolization, and that the functionality of both walnut proteins was the worst at pH 5, with solubility of 5.31% and 4.86%, emulsifying activity index (EAI) of 24.95 and 19.91 m2 /g, and foaming capacity (FC) of 3.66% and 2.94%, respectively; and the best at pH 11, with solubility of 82.35% and 73.55%, EAI of 46.35 and 37.28 m2 /g, and FC of 35.85% and 18.87%, respectively. The study found that dephenolization by UAE can significantly improve the functionality of WPI, and this method should be promoted and used in walnut and walnut protein processing industries. © 2023 Society of Chemical Industry.

Functional and physiochemical properties of protein isolates from different body parts of North Atlantic sea cucumber (Cucumaria frondosa)

Sea cucumbers are a good source of proteins and essential amino acids. In this study, protein isolates were recovered from North Atlantic sea cucumber (Cucumaria frondosa) body wall (BWI) and processing by-products, including flower (FLI) and internal organs (INI), using the pH-shift method. Functional properties of protein isolates were investigated and compared with those of soy protein isolates (SPI). All protein isolates exhibited a typical U-shaped solubility curve showing a minimum solubility at their isoelectric points. Furthermore, emulsification and foaming properties of the sea cucumber protein isolates were also pH-dependent and corresponded with their solubility. The highest water holding capacity was observed in FLI, whereas SPI showed the lowest oil holding capacity among all tested protein isolates. Sea cucumber protein isolates exhibited significantly higher (p < 0.05) surface hydrophobicity and relatively lower sulfhydryl (SH) group and disulfide (SS) bonds compared to SPI. In addition, Fourier transform infrared (FTIR) spectra of sea cucumber protein isolates exhibited unique absorption peaks related to their secondary structures. Amino acid profiles of sea cucumber protein isolates revealed that they could be used as rich and complete sources of essential amino acids. These findings suggest that Atlantic sea cucumber protein isolates could serve as functional food ingredients.

Comparative evaluation of the functionality of faba bean protein isolates with major legume proteins in the market

AbstractBackground and ObjectivesThe production of faba beans (Vicia Faba L.) is emerging in the Canadian prairies. To investigate their utilization potential as value‐added ingredients, the physicochemical and functional properties of protein isolates prepared from three faba bean cultivars (Fabelle, Malik, and Snowbird) currently grown in Canada were compared with those of yellow pea (CDC Amarillo) and soybean (AAC 26‐15).FindingsHigher than pea (23.1%), the faba bean had protein contents of ~31.4% and a small amount of fat (~1.2%). The protein isolates of faba bean (FPI), pea (PPI), and soy (SPI) were broadly comparable in surface tension, protein solubility, and oil holding capacity; however, surface charge was higher for FPI. The interfacial tension, water holding capacity, foaming, and emulsifying properties were also generally similar between FPI and PPI but different from SPI. Among faba bean cultivars, Snowbird was richer in protein with a higher proportion of legumins and was better at stabilizing emulsions while having a lower emulsifying activity.ConclusionsThe functionalities of FPI broadly resembled those of PPI, while being comparable or higher to those of SPI, suggesting the potential of using FPI as an alternative functional ingredient in product formulations.Significance and NoveltyThe study on the representative cultivars of Canadian‐grown faba beans updated the knowledge base concerning the functional differences among cultivars and how they compete with major legume proteins in the market, while providing insights on possible applications of faba bean protein ingredients.

Physicochemical, structural and functional properties of protein isolates and major protein fractions from common vetch (Vicia sativa L.)

Common vetch (CV), a leguminous crop cultivated for green manure and fodder rich in protein and starch, is widespread over much area of the northern hemisphere. Its seeds can be used as a protein source to human consumption. CV protein isolates (CVPI) and major protein fractions (CV albumin protein, CVAP; CV globulin protein, CVGP; CV glutelin protein, CVGTP) from 4 samples were investigated the properties to facilitate full use of protein resources. Protein comprises 27.70 %–32.14 % of the dry CV seed weight, which is mainly composed by CVAP (26.79 %–56.12 %) and CVGP (22.78 %–52.42 %). CVPI, CVAP and CVGP mainly presented 7S and 11S components. CVGTP mainly contained the 11S component. They showed difference in thermal properties and surface hydrophobicity. Circular dichroism data showed that α-helix was their major secondary structure. CVPI and major protein fractions exhibited a U-shape protein solubility. CVPI and CVAP had advantages in emulsifying and foaming properties. This study provided novel insights on unexploited sources of CV proteins with interesting characteristics in terms of potential uses as protein-based foods.

Physicochemical and functional properties of protein isolate recovered from Rana chensinensis ovum based on different drying techniques

This work was dedicated to evaluating the drying methods (freeze drying, spray drying, and vacuum drying) of food Rana chensinensis ovum protein isolate (RCOPI) based on comparison of the physicochemical and functional properties. The characterization and evaluation were conducted using scanning electron microscopy, surface hydrophobicity, SDS-PAGE, amino acid composition and nutritional parameters, Fourier transform infrared spectroscopy, and autofluorescence spectroscopy. The results showed the protein structure and conformation of RCOPI were greatly affected by drying techniques, leading to different physicochemical and functional properties. RCOPI possessed four main subunit bands distributed around 110, 90, 35 and 32 kDa. Seven essential amino acids were detected, accounting for 43.27–43.65% of total amino acids. Freeze drying RCOPI (FD-RCOPI) showed superior functional features, including solubility, water holding capacity, oil holding capacity, stabilization of Pickering emulsion and antioxidant capacity. FD-RCOPI exhibited applicability for the manufacture of viscous foods, bakery products and Pickering emulsions.

Bioactive Peptides from Unconventional Food Sources: A Novel Radical Approach in Food Value Addition

Introduction: Bioactive peptides are small peptides of 2-20 amino acids encrypted in the proteins of protein-rich unconventionalfood sources. Bioactive peptides show therapeutic functions such as antioxidative, immunomodulatory, opioid, anti-hypertensive,antimicrobial, etc.Objective: Unconventional protein-rich food sources may be employed to fabricate bioactive peptides using enzyme technology.Methodology: Protein-rich unconventional food sources such as Bellamya bengalensis Lamellidense marginalis have been used to fabricatebioactive peptides using different proteases in vitro. The ultrafiltration technique isolated the peptides. Functional properties of proteinisolates from the meat of Bellamya bengalensis were characterized as foaming property, solubility index of protein, and emulsifyingproperty. The anti-hypertensive property of the bioactive peptides was determined and compared with lisinopril, a standard drug. Invitro experiments and in silico molecular docking studies were carried out to find the most powerful inhibitory peptide against ACE,the major enzyme of the Renin-Angiotensin System. Using isothermal titration calorimetry, the results were further authenticated, andthe actual mechanism of action of their anti-hypertensive property was found.Results: The hydrolysates were ultrafiltered, the smallest fraction was evaluated in MALDI-TOF MS, and five peptides were sequencedvia de novo sequencing. Lisinopril is a synthetic analog of the Angiotensin Converting Enzyme. The BP's binding affinity to ACE's activesite was compared with lisinopril. The thermodynamics of the inhibition was checked by ITC and further validated by in silico moleculardocking study. The ACE-inhibitory potential of the BP positively correlates with the presence of hydrophobic amino acids.Conclusion: BP from different food sources have been excised and studied for their functional properties. Some have anti-hypertensiveproperties and may be of particular interest in the context of hypertension. BP from dietary proteins exposes various biological activities.These BP with anti-hypertensive effects may serve as a value-added food and pharmaceutical product.

Effect of heat treatment on the structure, functional properties and composition of Moringa oleifera seed proteins

Knowledge on how food processing conditions and protein composition can modulate individual or food matrix protein functionality is crucial for designing new protein ingredients. In this regard, we investigated how heat treatment and protein composition influence physicochemical and functional properties of Moringa oleifera seed protein isolate. Results showed that changes in processing temperature induced modifications in the conformation affecting the hydrophobic core of proteins. Protein isolate was more soluble at room temperature whereas prolamin fraction presented high solubility at 70 °C. Glutelin showed higher emulsifying properties at all temperatures. Protein composition also significantly affected physicochemical and functional properties of protein isolate. Increasing soluble glutelin enhanced solubility while increasing albumin, globulin and glutelin decreased hydrophobicity of the isolate. Likewise, increasing soluble globulin improved emulsifying capacity, and emulsion stability of the isolate was negatively affected by increase in albumin and glutelin. These findings could enhance application of Moringa oleifera protein in food formulations.

Functional, amino acid composition and protein profiling of protein isolates from different pigmented, nonpigmented and improved rice varieties and their effects on starch thermal and dynamic rheological behaviour

SummaryThe amino acids composition, protein profiling and functional properties of protein isolates from different pigmented rice (PR), nonpigmented rice (NPR) and improved rice (IR) varieties were determined and their effects of incorporation on starch thermal, and dynamic rheological were evaluated to know the possible interactions in food matrix. Protein isolates (PI) from PR and IR showed better foaming capacity and, foam stability than those from NPR. PI from both the PR and IR showed higher proportion of histidine, threonine, valine, methionine, phenylalanine and isoleucine. PI from IR showed higher accumulations of glutelins (31 and 33kDa, 21 and 22 kDa) and prolamins (15kDa, 16kDa, 17 kDa and 20kDa) than those from rice types. Starches from IR showed higher storage modulus (Gʹ) and loss modulus (Gʺ) than that from PR, and NPR, and decreased on addition of PI. PI from PB1121 IR was more suitable for protein enrichment due to more lightness value, and superior functionality (emulsification and foaming properties). Starch‐protein interaction affects the functionality, and behaviour of matrix and, developing hypoallergenic infant formulations or other food products.

Functional properties of protein isolates from camelina (Camelina sativa (L.) Crantz) and flixweed (sophia, Descurainis sophia L.) seed meals

Camelina and flixweed (sophia) seed protein isolates were prepared using both the conventional extraction and ultrasonic-assisted extraction methods at 40 kHz for 20 min, and their functional properties investigated. SDS-PAGE showed that both ultrasound-assisted and conventional extractions resulted in a similar protein profile of the extract. The application of ultrasound significantly improved protein extraction/content and functional properties (water holding capacity, oil absorption capacity, emulsifying foaming properties, and protein solubility) of camelina protein isolate and sophia protein isolate. The water-holding and oil absorption capacities of sophia protein isolate were markedly higher than those of camelina protein isolate. These results suggest that camelina protein isolate and sophia protein isolate may serve as natural functional ingredients in the food industry.Graphical

Structure-function relationship of black cumin seeds protein isolates: Amino-acid profiling, surface characteristics, and thermal properties

• The extraction of black cumin seeds proteins was optimized using response surface methodology. • The black cumin seeds proteins isolate showed a semi-crystalline structure. • FTIR analysis revealed the typical peaks of protein. • Black cumin seeds proteins were thermally stable until approximately 90 °C. • Black cumin seeds proteins presented peculiar functional properties. The aim of the present investigation was to determine the chemical composition, the amino-acid profiling, the structural characteristics and the functional properties of protein isolates of two black cumin seeds varieties. Response surface methodology (RSM) was firstly carried out to determine optimal conditions of proteins extraction from black cumin seeds. Results indicated that the meal to solvent ratio, pH and extraction time were stated as the main influencing factors to obtain protein isolates of black cumin seeds. The protein content of cumin seeds protein isolates varied between 68.76%–78.41% showing the predominance of glutamic acid (12.73–14.59 %), aspartic acid (5.28–5.62 %) and arginine (4.94–5.49 %) amino acids. X-ray diffraction patterns of the protein isolates showed a semi-crystalline structure. Structural characterization by FTIR analysis showed the typical peaks of protein, namely, amide I, amide II and amide III. The thermal properties of protein isolates were investigated by differential scanning calorimetry. A denaturation temperature ranged from 88.11 °C to 90.65 °C. Black cumin seeds protein isolates were able to decrease the interfacial tension (down to 17.62 mN/m) leading to an interesting emulsifying (up to 159.53 m 2 /g) and foaming (up to 145.54 %) properties as function of pH.

Functional properties of gonad protein isolates from three species of sea urchin: a comparative study.

Sea urchin Mesocentrotus nudus, Glyptocidaris crenularis, and Strongylocentrotus intermedius gonad protein isolates (mnGPIs, gcGPIs, and siGPIs) were extracted by isoelectric solubilization/precipitation (ISP) from the defatted gonads, and their functional properties were compared. Sodium dodecyl sulfate polyacrylamide gel electrophoresis results showed the similar protein pattern between each protein isolate and defatted gonad, indicating the high efficiency of ISP processing for protein recovery. Amino acid profileconfirmed that the mnGPIs and siGPIs could be potential sources of essential amino acid in nature. As regard to functional properties, mnGPIs showed higher water- and oil- holding capacities followed bysiGPIs and gcGPIs and all protein isolates presented great foaming property. As for emulsifying activity index (EAI), mnGPIs, gcGPIs, and siGPIs showed the minimum solubility and EAI at pH 5, 3, and 4, respectively, and behaved a pH-dependent manner. The gcGPIs revealed the highest EAI from pH 6 to 8 among the samples. In addition, circular dichroism showed increased content of β-sheet at the expense of α-helix and β-turn, suggesting the structure denaturation of the protein isolates. Indeed, no statistical difference was observed between secondary structure of mnGPIs and siGPIs. Moreover, ISP processing increased free sulfhydryl content of sea urchin protein isolates, but no difference was observed among the samples. Furthermore, siGPIs revealed the highest amount of total sulfhydryl and disulfide bonds, whereas both defatted gonads and protein isolates from G. crenularis presented the maximum surface hydrophobicity. These results suggest that gonad protein isolates from three species of sea urchin possess various functionalities and therefore can be potentially applied in food system. PRACTICAL APPLICATION: Sea urchin M. nudus, G. crenularis, and S. intermedius gonads are edible, whereas the functional properties of protein isolates from sea urchin gonad remain unknown. In this case, the extraction and comparison of three species of sea urchin gonad protein isolates will not only confirm functional properties but also screen food ingredients with suitable functions. In this study, functionalities of protein isolates derived from M. nudus, G. crenularis, and S. intermedius gonads would provide potential application in bakery food and meat products or as emulsifier candidates in food system.

Biochemical, nutritional and functional properties of protein isolate and fractions from pumpkin (Cucurbita moschata var. Kashi Harit) seeds

Pumpkin seeds are rich source of nutritionally well-balanced proteins. The biochemical, nutritional, and functional properties of the protein isolate (PPI) and protein fractions from pumpkin seed were evaluated. Extraction method for PPI was optimized by varying NaCl (0, 0.5, 1 M) and flour-to-solution ratio (1:5, 1:10, 1:25), at pH 9.0. Proteins were extracted by Osborne procedure and the alkali fraction (AF, 45.82%) was found to be the predominant fraction. SDS-PAGE profile of PPI revealed major bands ranging from 50 to 7 kDa. AF contained all the essential amino acids (EAA) except lysine and threonine, as required by pre-school children (FAO/WHO). PPI and AF showed better protein efficiency ratio and EAA/TAA (total) %, indicating the presence of good quality proteins. Functional properties were found to be comparable with soybean protein isolate. Circular dichroism studies showed that water fraction comprised of α-helix and random coils, while salt and alkali fractions contained β-strand and coils.

Development of optimal method of obtaining pea isolated proteins for use in breeding for quality

The article provides the results of the experiments on determination of optimal parameters for obtaining isolated proteins from grains of cultivated and wild pea for use in breeding for quality. The flour of pea varieties Sophia, Rodnik and wild accession k-3370 (Pisum sativum L. ssp. Elatius) were used in the experiment. Isolated pea proteins were obtained based on alkaline extraction and isoelectric precipitation. The experiments were carried out with the use of complete and fractional factorial plans with two levels of factors. Extraction and precipitation of protein were conducted in two stages. One hundred grams of flour were used for extraction. Influence of factors (variety, pH, duration of extraction) on the yield of isolated protein, extraction efficiency, crude protein and fat content in protein isolates was studied. All isolates were characterized by high content of crude protein (90.2-93.1 %). It was determined that increase of pH higher than eight led to enhancement of protein yield and decrease of crude protein content. The results obtained raise the possibility of effective extraction at decreased level of pH that prevents the formation of toxic chemicals. Increase of pH promoted fat accumulation in protein isolate especially at the second stage of extraction. Thus, obtaining protein isolates for evaluation of pea genetic resources should be conducted during a single cycle of extraction and precipitation. The experiments have not revealed significant differences between cultivated and wild pea as to the technology of extraction. The results of the studies are important for evaluation of pea genetic resources according to functional properties of protein isolates.

Comparative study of the structural and functional properties of protein isolates prepared from edible vegetable leaves

ABSTRACT Isoelectric precipitation was used to produce protein isolates (>90% protein contents) from three edible vegetable leaves. Amaranth (ALI), eggplant (ELI) and fluted pumpkin (FLI) leaf protein were isolated to study their conformational structures. Intrinsic fluorescence indicated a loose structural conformation for ELI at all the pH values, whereas FLI and ALI had more compact structures at pH 3.0 and pH 9.0. The surface hydrophobicity showed a greater distribution of hydrophobic amino acid groups of the protein isolates at the basic than the acidic regions. The SDS-PAGE results showed that the leaf isolates had similar polypeptide bonds characterized by 20, 25, 40 and 200 kDa and some distinct bands above 200 kDa. The ELI formed emulsions with significantly (p < .05) smallest oil droplet sizes (<3.3 µm) when compared to FLI and ALI. However, foaming capacity was mostly pH-dependent with significantly (p < .05) higher values at pH 7.0 and 9.0. The leaf protein isolates may be considered as potential functional food ingredients.

Influence of phenolic compounds on physicochemical and functional properties of protein isolate from Cinnamomum camphora seed kernel

Cinnamomum camphora seeds are abundant in China. For high value utilization of Cinnamomum camphora seed kernel (CCSK) protein, the effects of phenolic compounds on physicochemical and functional properties of protein isolate (PI) from CCSK were investigated in this study. A total of 12 phenolic compounds in CCSK have, for the first time, been tentatively identified by HPLC-ESI-QTOF-MS2. PI had a higher level of protein content compared to that of protein-phenolic complex (PPC). The formation of PPC resulted in a reduction of free sulfhydryl groups content and surface hydrophobicity as well as an increase of particle size and zeta potential. Fourier-transform infrared spectroscopy showed that the contents of secondary structure of PI and PPC were not obviously different. However, a remarkable increase in β-sheet and a decrease in random coil of PPC compared to PI were found by circular dichroism. Differential scanning calorimetry analysis revealed that PPC was thermally more stable than that of PI. PI and PPC exhibited superior essential amino acid composition and similar protein subunits. Furthermore, PPC exhibited higher solubility, better foaming and emulsifying properties than those of PI. These results suggested that the protein products from CCSK may be used as natural functional materials in the food industry.

Effect of steaming and dehydration on the nutritional quality and functional properties of protein isolates produced from Lablab purpureus (L.) Sweet (hyacinth bean)

The study conducted was focused on investigating the effect of steaming and dehydration on the nutritional quality and functional properties of protein isolates produced from hyacinth bean. This was for obtaining value-added legume-derived protein ingredients for potential food applications. Protein isolates prepared by isoelectric precipitation from legume grains subjected to steaming and dehydration prior to soaking, respectively, displayed traits of high-quality proteins. The major protein polypeptides present among samples were vicilin (7S) and legumin (11S). Steaming was identified useful for producing protein ingredients for nutritional intervention with potential health benefits. Samples recorded improved Fischer's ratio (1.57–1.78), BCAA to tyrosine ratio (3.51–4.28), predicted biological values (44.84–54.70), foaming, and emulsion properties. Dehydration extensively preserved the nutritional qualities and functionality of steamed samples. Findings have the potential to diversify the use of hyacinth bean and help improve the competitiveness of the legume grain sector. Practical applications This study presents how processing strategies (soaking, steaming, and dehydration) may be employed for obtaining legume-derived protein ingredients with improved nutritional quality and functional properties for potential food applications. The underutilization of many indigenous crops is mainly attributed to both limited research and marketing. Thus, research findings could potentially improve the value of hyacinth bean by diversifying its use and help improve the competitiveness of the legume grain sector. This could be achieved through demand for possible food applications that require protein enrichment. Furthermore, results may assist in broadening dehydration technology preferences in existing markets for obtaining legume grain-based ingredients or products with maximum quality.

Characterisation, physicochemical and functional properties of protein isolates from Amygdalus pedunculata Pall seeds

Amygdalus pedunculata Pall is a kind of desert woody oil plant, and its seeds are high in protein. The protein of Amygdalus pedunculata Pall (API) was identified by SDS-PAGE, 2-DE and MS. More than 300 proteins were identified. The improved solubility, emulsifying properties and foaming properties of API were observed in a pH range of 2.0–12.0 and a sodium chloride concentration of 0–1.0 M. The results showed that API had a good solubility (94.2%), bulk density (0.107 g/mL), oil absorption capacity (3.54 g/g), thermal stability (91.58 °C), emulsifying property (70 m2/g) and foaming property (83.7%). The conformation changes of API were studied by fluorescence and differential scanning calorimetry (DSC). The degree of denaturation of denaturants for API was guanidine hydrochloride > urea > SDS. These results showed that API has good processing performance and can be used as a new type of plant protein resource.