Pub Date : 2025-04-02DOI: 10.1016/j.foodhyd.2025.111397
Pietro Marasco , Ali Kozlu , Anna Mascellani Bergo , Jaroslav Havlík , Iveta Klojdová , Diana Karina Baigts-Allende
Gelatin is a widely used polymer in several industrial sectors, principally in the pharmaceutical and food industries. Its popularity stems from its biocompatibility, biodegradability, colorlessness, and provider of stability and texture in different food systems. In Europe, the primary source of gelatin is pig skin; however, due to religious dietary restrictions, there is an increasing demand for alternative sources. This study analyzed the physicochemical and rheological properties of gelatin extracted from eland skin using alkaline (calcium hydroxide 2 %) and acid (acetic acid at 5 %) treatments compared to commercially available bovine and porcine gelatins. The acid-treated eland-skin collagen more effectively preserved the β and α structures. It showed a higher propensity to form triple helices more effectively than all commercial and alkaline-treated samples. It was evidenced by more intense electrophoretic bands, FTIR spectra peaks in the amide I, II, and II regions, and lower relative intensities of side chains of the amino acid residues quantified by NMR.
Rheological properties (small and large deformation) improved with increasing gelatin concentration (3, 5, and 6.67 %. w/v). Type A eland-skin gelatin resulted in a higher storage modulus (G′) and firmer gels than all samples. Electrostatic hydrogels formed at different ratios of protein: polysaccharides (1:1, 1:2, and 1:3) showed excellent texture and water-holding capacity after lyophilization compared to control samples. Our findings demonstrated that eland skin has the potential to serve as an alternative source of food additives and promise delivery system.
{"title":"Structural and functional qualities of gelatin derived from the skin of the common eland antelope (Taurotragus oryx)","authors":"Pietro Marasco , Ali Kozlu , Anna Mascellani Bergo , Jaroslav Havlík , Iveta Klojdová , Diana Karina Baigts-Allende","doi":"10.1016/j.foodhyd.2025.111397","DOIUrl":"10.1016/j.foodhyd.2025.111397","url":null,"abstract":"<div><div>Gelatin is a widely used polymer in several industrial sectors, principally in the pharmaceutical and food industries. Its popularity stems from its biocompatibility, biodegradability, colorlessness, and provider of stability and texture in different food systems. In Europe, the primary source of gelatin is pig skin; however, due to religious dietary restrictions, there is an increasing demand for alternative sources. This study analyzed the physicochemical and rheological properties of gelatin extracted from eland skin using alkaline (calcium hydroxide 2 %) and acid (acetic acid at 5 %) treatments compared to commercially available bovine and porcine gelatins. The acid-treated eland-skin collagen more effectively preserved the β and α structures. It showed a higher propensity to form triple helices more effectively than all commercial and alkaline-treated samples. It was evidenced by more intense electrophoretic bands, FTIR spectra peaks in the amide I, II, and II regions, and lower relative intensities of side chains of the amino acid residues quantified by NMR.</div><div>Rheological properties (small and large deformation) improved with increasing gelatin concentration (3, 5, and 6.67 %. w/v). Type A eland-skin gelatin resulted in a higher storage modulus (G′) and firmer gels than all samples. Electrostatic hydrogels formed at different ratios of protein: polysaccharides (1:1, 1:2, and 1:3) showed excellent texture and water-holding capacity after lyophilization compared to control samples. Our findings demonstrated that eland skin has the potential to serve as an alternative source of food additives and promise delivery system.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"167 ","pages":"Article 111397"},"PeriodicalIF":11.0,"publicationDate":"2025-04-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143777133","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-04-01DOI: 10.1016/j.foodhyd.2025.111407
Songsong Jiang , Yutong Huang , Qian Li , Tingting Luo , Tianzhu Guan
In this study, three polyphenols, including gallic acid (GA), quercetin (QR) and rutin (RH) were added into goose myofibrillar protein (GMP) to explore the effects on the gel properties and structures of GMP. Results showed that after adding polyphenols, the water holding capacity (WHC), and texture characteristics of GMP gel were significantly improved. Scanning electron microscopy results revealed that the structure of the GMP gel became denser after the addition of polyphenols. Fourier transform infrared spectroscopy (FTIR) results indicated that the secondary structure of GMP in QR group changed significantly, accompanied by a significant increase in β-sheet content (P < 0.05). Ultraviolet (UV) spectroscopy showed that the maximum absorption peak of the GMP was decreased apparently in the polyphenol supplement groups, especially in QR group, suggesting alterations in the tertiary structure of GMP. Additionally, molecular docking analysis confirmed that the polyphenols interacted with GMP primarily through hydrogen bonds and hydrophobic interactions. However, perhaps due to the denser protein gel microstructure, the digestion of GMP was decreased. In conclusion, although digestion was reduced, all three polyphenols improved the gel properties of GMP, with QR demonstrating the most significant effect, which was associated with structural changes in GMP.
{"title":"Effects of three polyphenols on the gel properties and structures of goose myofibrillar protein","authors":"Songsong Jiang , Yutong Huang , Qian Li , Tingting Luo , Tianzhu Guan","doi":"10.1016/j.foodhyd.2025.111407","DOIUrl":"10.1016/j.foodhyd.2025.111407","url":null,"abstract":"<div><div>In this study, three polyphenols, including gallic acid (GA), quercetin (QR) and rutin (RH) were added into goose myofibrillar protein (GMP) to explore the effects on the gel properties and structures of GMP. Results showed that after adding polyphenols, the water holding capacity (WHC), and texture characteristics of GMP gel were significantly improved. Scanning electron microscopy results revealed that the structure of the GMP gel became denser after the addition of polyphenols. Fourier transform infrared spectroscopy (FTIR) results indicated that the secondary structure of GMP in QR group changed significantly, accompanied by a significant increase in β-sheet content (<em>P < 0.05</em>). Ultraviolet (UV) spectroscopy showed that the maximum absorption peak of the GMP was decreased apparently in the polyphenol supplement groups, especially in QR group, suggesting alterations in the tertiary structure of GMP. Additionally, molecular docking analysis confirmed that the polyphenols interacted with GMP primarily through hydrogen bonds and hydrophobic interactions. However, perhaps due to the denser protein gel microstructure, the digestion of GMP was decreased. In conclusion, although digestion was reduced, all three polyphenols improved the gel properties of GMP, with QR demonstrating the most significant effect, which was associated with structural changes in GMP.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"167 ","pages":"Article 111407"},"PeriodicalIF":11.0,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143777129","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-04-01DOI: 10.1016/j.foodhyd.2025.111404
Yaxin Zhao , Tingting Li , Jiajia Zhao , Waleed AL-Ansi , Mingcong Fan , K. AboGhaneima Wafaa , Haifeng Qian , Yan Li , Li Wang
Fluctuations in temperature during freeze-thaw (F/T) cycles can lead to large ice crystal formation and recrystallization, resulting in the deterioration of the dough gluten network and degradation of the final product. This study aimed to explore the influence of protein hydrolysate of sea buckthorn residue (SRPH) on moisture status, gluten network structure, and prebaked bread-making properties during F/T cycles, as compared with a commercially available ice-structured protein (ISP). The results demonstrated that following six F/T cycles, the freezable moisture content of the blank control (BC), ISP, and SRPH groups exhibited increases of 12.25 %, 6.35 %, and 5.92 %, respectively. Furthermore, the free sulfhydryl groups decreased by 18.95 % and 19.32 %, the disulfide bonds increased by 16.1 % and 21.38 %, and the α-helical structure increased by 3.61 % and 3.09 % in the ISP and SPPH groups, respectively, compared to the BC group. These results indicate that the addition of SRPH to doughs can maintain the intact structure and functional properties of doughs by controlling moisture migration. This may be attributed to the fact that SRPH exhibits certain thermal hysteretic activity (0.18 °C), contains a substantial amount of hydrophilic amino acids (64.86 %), and has a high supercooling point (−11.40 °C). These results substantiate the protective effects against the freezing activity of SPPH on frozen dough during F/T cycles, thereby providing a foundation for the future creation of prebaked frozen food items.
{"title":"Effects of sea buckthorn residue protein hydrolysate on the quality of frozen pre-baked bread: Water state and gluten structures","authors":"Yaxin Zhao , Tingting Li , Jiajia Zhao , Waleed AL-Ansi , Mingcong Fan , K. AboGhaneima Wafaa , Haifeng Qian , Yan Li , Li Wang","doi":"10.1016/j.foodhyd.2025.111404","DOIUrl":"10.1016/j.foodhyd.2025.111404","url":null,"abstract":"<div><div>Fluctuations in temperature during freeze-thaw (F/T) cycles can lead to large ice crystal formation and recrystallization, resulting in the deterioration of the dough gluten network and degradation of the final product. This study aimed to explore the influence of protein hydrolysate of sea buckthorn residue (SRPH) on moisture status, gluten network structure, and prebaked bread-making properties during F/T cycles, as compared with a commercially available ice-structured protein (ISP). The results demonstrated that following six F/T cycles, the freezable moisture content of the blank control (BC), ISP, and SRPH groups exhibited increases of 12.25 %, 6.35 %, and 5.92 %, respectively. Furthermore, the free sulfhydryl groups decreased by 18.95 % and 19.32 %, the disulfide bonds increased by 16.1 % and 21.38 %, and the α-helical structure increased by 3.61 % and 3.09 % in the ISP and SPPH groups, respectively, compared to the BC group. These results indicate that the addition of SRPH to doughs can maintain the intact structure and functional properties of doughs by controlling moisture migration. This may be attributed to the fact that SRPH exhibits certain thermal hysteretic activity (0.18 °C), contains a substantial amount of hydrophilic amino acids (64.86 %), and has a high supercooling point (−11.40 °C). These results substantiate the protective effects against the freezing activity of SPPH on frozen dough during F/T cycles, thereby providing a foundation for the future creation of prebaked frozen food items.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"167 ","pages":"Article 111404"},"PeriodicalIF":11.0,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143786234","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-04-01DOI: 10.1016/j.foodhyd.2025.111405
Tian Gao , Chao Yuan , Bo Cui , Pengfei Liu , Zhengzong Wu , Yishan Fang , Lu Lu
Edible films developed from food biopolymers have made significant progress in recent years. In this work, water-soluble edible packaging films formed by soluble soybean polysaccharide (SSPS) and soybean peptides (SPEs) with different molecular weights (500, 1000, and 3000 Da) were developed and characterized. The results demonstrated that the incorporation of SPEs markedly enhanced the performance of the SSPS film, improving its optical properties, mechanical strength, and thermal stability. As the molecular weight increased, both the tensile strength and the elongation at break of the composite film improved, reaching 7.9 ± 0.3 MPa and 41.4 ± 2.7 %, respectively. The FTIR results indicated that SPEs primarily interacted with SSPS through intermolecular hydrogen bonding. The incorporation of 3000 Da SPEs enhanced the internal orderliness, constructing a more compact network structure, which significantly improved the heat resistance of film networks. Additionally, the incorporation of SPEs enhanced the disintegration property and contact angle value of composite films. The composite film carrying clove essential oil had obvious inhibition activity to S. aureus and E. coli. The study could contribute to developing the novel type of instant edible films and provide a basis for the load of active substances.
{"title":"Effect of soybean peptides on structure and functional properties of soluble soybean polysaccharide edible films","authors":"Tian Gao , Chao Yuan , Bo Cui , Pengfei Liu , Zhengzong Wu , Yishan Fang , Lu Lu","doi":"10.1016/j.foodhyd.2025.111405","DOIUrl":"10.1016/j.foodhyd.2025.111405","url":null,"abstract":"<div><div>Edible films developed from food biopolymers have made significant progress in recent years. In this work, water-soluble edible packaging films formed by soluble soybean polysaccharide (SSPS) and soybean peptides (SPEs) with different molecular weights (500, 1000, and 3000 Da) were developed and characterized. The results demonstrated that the incorporation of SPEs markedly enhanced the performance of the SSPS film, improving its optical properties, mechanical strength, and thermal stability. As the molecular weight increased, both the tensile strength and the elongation at break of the composite film improved, reaching 7.9 ± 0.3 MPa and 41.4 ± 2.7 %, respectively. The FTIR results indicated that SPEs primarily interacted with SSPS through intermolecular hydrogen bonding. The incorporation of 3000 Da SPEs enhanced the internal orderliness, constructing a more compact network structure, which significantly improved the heat resistance of film networks. Additionally, the incorporation of SPEs enhanced the disintegration property and contact angle value of composite films. The composite film carrying clove essential oil had obvious inhibition activity to <em>S. aureus</em> and <em>E. coli</em>. The study could contribute to developing the novel type of instant edible films and provide a basis for the load of active substances.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"167 ","pages":"Article 111405"},"PeriodicalIF":11.0,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143786211","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-04-01DOI: 10.1016/j.foodhyd.2025.111391
Giorgia Frutaz , Pedro J. Fito , María Victoria Traffano-Schiffo , Rafael Gadea-Girones , Marta Castro-Giraldez
Gastro-oesophageal reflux disease (GORD) is a current global clinical problem, which negatively affects patients’ quality of life, causing symptoms like heartburn, acid regurgitation and/or mucosal damage. The administration of scopoletin represents a promising alternative therapy against GORD, due to its antisecretory and prokinetic activities. Encapsulation in a calcium alginate matrix enables the sustained release of bioactive compounds, especially when secondary excipients are incorporated. The release kinetic of encapsulated substances can be studied through permittivity measurements in radiofrequency range, serving as a novel, continuous, and quantitative method for measuring the release of active compounds in the digestive media.
In this work, three systems of scopoletin beads were prepared, using an alginate (AS); alginate and guar gum (ASGG); and alginate and arabic gum (ASAG) matrix, respectively. The swelling of each system in simulated gastric medium (SGM) was evaluated by optical microscopy, and the release kinetic of scopoletin was obtained through radiofrequency spectroscopy. Eventually, an irreversible thermodynamic model was developed to determine the driving forces of scopoletin release in each case. The results showed that the addition of gums, especially guar gum, provokes an increased expansion of the system in SGM and a reduction of the flux of scopoletin within the gastric phase. Gums provide more elasticity to the beads, which store mechanical energy during the drying process and release it when rehydrated in SGM. As consequence, a hydrodynamic flux against the diffusion of scopoletin is generated, and the release is prolonged over time. The present study provides the basis for the design and development of encapsulations to treat gastrointestinal diseases.
{"title":"Scopoletin release modulation in alginate-gums beads analysed by a novel spectrophotometric technique in radiofrequency spectra","authors":"Giorgia Frutaz , Pedro J. Fito , María Victoria Traffano-Schiffo , Rafael Gadea-Girones , Marta Castro-Giraldez","doi":"10.1016/j.foodhyd.2025.111391","DOIUrl":"10.1016/j.foodhyd.2025.111391","url":null,"abstract":"<div><div>Gastro-oesophageal reflux disease (GORD) is a current global clinical problem, which negatively affects patients’ quality of life, causing symptoms like heartburn, acid regurgitation and/or mucosal damage. The administration of scopoletin represents a promising alternative therapy against GORD, due to its antisecretory and prokinetic activities. Encapsulation in a calcium alginate matrix enables the sustained release of bioactive compounds, especially when secondary excipients are incorporated. The release kinetic of encapsulated substances can be studied through permittivity measurements in radiofrequency range, serving as a novel, continuous, and quantitative method for measuring the release of active compounds in the digestive media.</div><div>In this work, three systems of scopoletin beads were prepared, using an alginate (AS); alginate and guar gum (ASGG); and alginate and arabic gum (ASAG) matrix, respectively. The swelling of each system in simulated gastric medium (SGM) was evaluated by optical microscopy, and the release kinetic of scopoletin was obtained through radiofrequency spectroscopy. Eventually, an irreversible thermodynamic model was developed to determine the driving forces of scopoletin release in each case. The results showed that the addition of gums, especially guar gum, provokes an increased expansion of the system in SGM and a reduction of the flux of scopoletin within the gastric phase. Gums provide more elasticity to the beads, which store mechanical energy during the drying process and release it when rehydrated in SGM. As consequence, a hydrodynamic flux against the diffusion of scopoletin is generated, and the release is prolonged over time. The present study provides the basis for the design and development of encapsulations to treat gastrointestinal diseases.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"167 ","pages":"Article 111391"},"PeriodicalIF":11.0,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143792593","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-04-01DOI: 10.1016/j.foodhyd.2025.111394
Raul Remor Dalsasso , Karina Cesca , Gérman Ayala Valencia , Alcilene Rodrigues Monteiro , Zhenyu J. Zhang , Peter J. Fryer
Ginger oleoresins contain bioactive phenolic compounds that are more storage-stable but less studied than the volatile oil fraction. This study aimed to produce a stable nanoemulsion from ginger oleoresin to use as an active material for food application. Ginger coarse emulsion (GCE) was prepared by high-shear homogenization (7000 rpm). Nanoemulsions also used ultrasound (power 750 W) at 20 %, 30 %, or 45 % of amplitude for 1, 3, or 9 min. The optimized nanoemulsion (GEN) (average particle size 105 nm, Zeta potential −18 mV) showed stability for at least 56 days stored at 4 or 20 °C, while GCE precipitated within 7 days. GEN showed an antimicrobial effect against S. aureus and E. coli. GEN was incorporated into a gelatin hydrogel (1.50 % and 0.75 % oleoresin), and active films were obtained by casting. The films were applied as slice separators for mozzarella and stored at 4 °C to control the oleoresin release to cheese slices. Oleoresin migration to the food surface, color, pH, weight loss, visual mold formation, and colony growth were monitored over 56 days. Nanoemulsion acted as a plasticizer, increasing films' elongation (31–71 %) and reducing tensile strength (35-20 MPa). Oleoresin blocked 200–400 nm wavelength radiation. The films exhibited high barriers against CO2 (4.8–6.3 × 10−9 mol μm/m2·Pa·s) and O2 (4.8–6.5 × 10−9 mol μm/m2·Pa·s), and low barrier against water vapor (0.43–0.47 g mm/h·m2·Pa). Oleoresin was released from the films for at least 56 days, increasing the media's antioxidant activity to 624 mg. Trolox/mL and delaying the visual mold incidence in sliced mozzarella cheese from 28 to 42 days.
{"title":"Active films produced using ginger oleoresin nanoemulsion: Characterization and application on mozzarella cheese","authors":"Raul Remor Dalsasso , Karina Cesca , Gérman Ayala Valencia , Alcilene Rodrigues Monteiro , Zhenyu J. Zhang , Peter J. Fryer","doi":"10.1016/j.foodhyd.2025.111394","DOIUrl":"10.1016/j.foodhyd.2025.111394","url":null,"abstract":"<div><div>Ginger oleoresins contain bioactive phenolic compounds that are more storage-stable but less studied than the volatile oil fraction. This study aimed to produce a stable nanoemulsion from ginger oleoresin to use as an active material for food application. Ginger coarse emulsion (GCE) was prepared by high-shear homogenization (7000 rpm). Nanoemulsions also used ultrasound (power 750 W) at 20 %, 30 %, or 45 % of amplitude for 1, 3, or 9 min. The optimized nanoemulsion (GEN) (average particle size 105 nm, Zeta potential −18 mV) showed stability for at least 56 days stored at 4 or 20 °C, while GCE precipitated within 7 days. GEN showed an antimicrobial effect against <em>S. aureus</em> and <em>E. coli</em>. GEN was incorporated into a gelatin hydrogel (1.50 % and 0.75 % oleoresin), and active films were obtained by casting. The films were applied as slice separators for mozzarella and stored at 4 °C to control the oleoresin release to cheese slices. Oleoresin migration to the food surface, color, pH, weight loss, visual mold formation, and colony growth were monitored over 56 days. Nanoemulsion acted as a plasticizer, increasing films' elongation (31–71 %) and reducing tensile strength (35-20 MPa). Oleoresin blocked 200–400 nm wavelength radiation. The films exhibited high barriers against CO<sub>2</sub> (4.8–6.3 × 10<sup>−9</sup> mol μm/m<sub>2</sub>·Pa·s) and O<sub>2</sub> (4.8–6.5 × 10<sup>−9</sup> mol μm/m<sup>2</sup>·Pa·s), and low barrier against water vapor (0.43–0.47 g mm/h·m<sup>2</sup>·Pa). Oleoresin was released from the films for at least 56 days, increasing the media's antioxidant activity to 624 mg. Trolox/mL and delaying the visual mold incidence in sliced mozzarella cheese from 28 to 42 days.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"167 ","pages":"Article 111394"},"PeriodicalIF":11.0,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143777128","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-04-01DOI: 10.1016/j.foodhyd.2025.111402
Hao Li , Michael Nigen , Christian Sanchez , Denis Renard
Acacia gum is a naturally occurring, heterogeneous mixture of arabinogalactan-proteins, valued for its surface properties in industrial applications. However, the impact of enzymatic treatments on its structural and functional characteristics remains poorly understood. In this study, the effect of four proteases (papain, subtilisin A, proteinase K, pronase) and three glycosidases (β-galactosidase, β-glucuronidase, α-rhamnosidase) on the structure and surface properties of Acacia senegal (A. senegal) gum were investigated using high-performance size exclusion chromatography with multiangle laser light scattering (HPSEC-MALLS), small angle X-ray scattering (SAXS), and quartz crystal microbalance with dissipation monitoring (QCM-D). The proteolysis effects on A. senegal gum were dependent on the molecular weight (Mw) and protein content of its macromolecular fractions separated by hydrophobic interaction chromatography. The high-Mw arabinogalactan-protein (AGP) fraction, HIC-F2, which constitutes ∼10 % of the total gum with an average Mw of ∼1.6 × 106 g mol−1, was significantly hydrolyzed by all tested proteases, albeit to varying extents. By contrast, the arabinogalactan-peptide (AG-peptide) fraction, HIC-F1, which represents the predominant fraction (∼90 %) with a Mw of ∼3 × 105 g mol−1, exhibited negligible proteolysis. Notably, HIC-F2 hydrolyzed by mixed proteases yielded species with a Mw comparable to HIC-F1. SAXS structural analysis revealed three distinct correlation lengths in both HIC-F2 and HIC-F1, which remained unchanged following proteolysis, likely reflecting multiple length scales of the carbohydrate units. Also, HIC-F2 population was primarily responsible for the surface adsorption of A. senegal gum, whereas HIC-F1 demonstrated minimal interfacial activity. Regardless of their specificity, all proteases significantly reduced the surface load and interfacial viscoelasticity of A. senegal gum, with a strong correlation between the Mw of hydrolyzed AGPs and their adsorption capacity. Conversely, the tested glycosidases did not affect the macromolecular structure of A. senegal gum. This study offers valuable insights into how the structural and functional properties of Acacia gums can be tailored through enzymatic treatments.
{"title":"Enzymatic hydrolysis alters the structure and surface properties of Acacia senegal Gum","authors":"Hao Li , Michael Nigen , Christian Sanchez , Denis Renard","doi":"10.1016/j.foodhyd.2025.111402","DOIUrl":"10.1016/j.foodhyd.2025.111402","url":null,"abstract":"<div><div>Acacia gum is a naturally occurring, heterogeneous mixture of arabinogalactan-proteins, valued for its surface properties in industrial applications. However, the impact of enzymatic treatments on its structural and functional characteristics remains poorly understood. In this study, the effect of four proteases (papain, subtilisin A, proteinase K, pronase) and three glycosidases (β-galactosidase, β-glucuronidase, α-rhamnosidase) on the structure and surface properties of Acacia <em>senegal (A. senegal)</em> gum were investigated using high-performance size exclusion chromatography with multiangle laser light scattering (HPSEC-MALLS), small angle X-ray scattering (SAXS), and quartz crystal microbalance with dissipation monitoring (QCM-D). The proteolysis effects on <em>A. senegal</em> gum were dependent on the molecular weight (M<sub>w</sub>) and protein content of its macromolecular fractions separated by hydrophobic interaction chromatography. The high-M<sub>w</sub> arabinogalactan-protein (AGP) fraction, HIC-F2, which constitutes ∼10 % of the total gum with an average M<sub>w</sub> of ∼1.6 × 10<sup>6</sup> g mol<sup>−1</sup>, was significantly hydrolyzed by all tested proteases, albeit to varying extents. By contrast, the arabinogalactan-peptide (AG-peptide) fraction, HIC-F1, which represents the predominant fraction (∼90 %) with a M<sub>w</sub> of ∼3 × 10<sup>5</sup> g mol<sup>−1</sup>, exhibited negligible proteolysis. Notably, HIC-F2 hydrolyzed by mixed proteases yielded species with a M<sub>w</sub> comparable to HIC-F1. SAXS structural analysis revealed three distinct correlation lengths in both HIC-F2 and HIC-F1, which remained unchanged following proteolysis, likely reflecting multiple length scales of the carbohydrate units. Also, HIC-F2 population was primarily responsible for the surface adsorption of <em>A. senegal</em> gum, whereas HIC-F1 demonstrated minimal interfacial activity. Regardless of their specificity, all proteases significantly reduced the surface load and interfacial viscoelasticity of <em>A</em>. <em>senegal</em> gum, with a strong correlation between the M<sub>w</sub> of hydrolyzed AGPs and their adsorption capacity. Conversely, the tested glycosidases did not affect the macromolecular structure of <em>A. senegal</em> gum. This study offers valuable insights into how the structural and functional properties of Acacia gums can be tailored through enzymatic treatments.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"167 ","pages":"Article 111402"},"PeriodicalIF":11.0,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143786235","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-04-01DOI: 10.1016/j.foodhyd.2025.111400
Hongwei Cao , Xiaotong Zhuang , Haojie Liu , Man Wang , Kai Huang , Hongdong Song , Sen Li , Yu Zhang , Zhenliang Sun , Xiao Guan
In this study, the underlying mechanism by which high-intensity ultrasonic treatment combined with β-glucan enhances the stability of highland barley milk (HBM) was investigated. The results demonstrated that protein solubility increased from 0.78 % to 1.05 % as the duration of ultrasonic treatment was extended. Foam stability reached its maximum value of 73.08 % after 16 min of treatment. Emulsification performance was significantly improved, with the emulsification activity peaking at 1.77 m2/g and stability reaching 17.34 min at 16 min of treatment. Measurements of contact angle and interfacial tension revealed that the contact angle increased from 23.9° to 45.1° with prolonged ultrasound treatment, stabilizing at 16 min. These results indicate that the combination of β-glucan and ultrasonic treatment improved the stability of HBM by modulating physicochemical properties, enhancing protein interactions, and mitigating phase separation and sedimentation. This study provides a novel approach for improving the stability of plant-based dairy products.
{"title":"Mechanism of high intensity ultrasonic treatment combined with β-glucan affecting the structure of highland barley protein to improve the stability of highland barley milk","authors":"Hongwei Cao , Xiaotong Zhuang , Haojie Liu , Man Wang , Kai Huang , Hongdong Song , Sen Li , Yu Zhang , Zhenliang Sun , Xiao Guan","doi":"10.1016/j.foodhyd.2025.111400","DOIUrl":"10.1016/j.foodhyd.2025.111400","url":null,"abstract":"<div><div>In this study, the underlying mechanism by which high-intensity ultrasonic treatment combined with β-glucan enhances the stability of highland barley milk (HBM) was investigated. The results demonstrated that protein solubility increased from 0.78 % to 1.05 % as the duration of ultrasonic treatment was extended. Foam stability reached its maximum value of 73.08 % after 16 min of treatment. Emulsification performance was significantly improved, with the emulsification activity peaking at 1.77 m<sup>2</sup>/g and stability reaching 17.34 min at 16 min of treatment. Measurements of contact angle and interfacial tension revealed that the contact angle increased from 23.9° to 45.1° with prolonged ultrasound treatment, stabilizing at 16 min. These results indicate that the combination of β-glucan and ultrasonic treatment improved the stability of HBM by modulating physicochemical properties, enhancing protein interactions, and mitigating phase separation and sedimentation. This study provides a novel approach for improving the stability of plant-based dairy products.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"167 ","pages":"Article 111400"},"PeriodicalIF":11.0,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143799079","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-04-01DOI: 10.1016/j.foodhyd.2025.111399
Ana Catarina Ribeiro , Carlo Bravo , Rui Miguel Ramos , Ricardo Dias , Nuno Mateus , Victor de Freitas , Rosa Pérez-Gregorio , Susana Soares
The rising interest in alternative protein sources, such as yeast protein extracts (YPEs), has recently brought attention to their interactions with polyphenols, which can enhance their structural and technological properties while providing health-beneficial properties, such as antioxidant activity. In this study, a multi-technique approach was employed to investigate the effects of a green tea extract (GTE), rich in flavanols, and a blueberry extract (BE), rich in anthocyanins, on the conformational and functional properties of enolase (ENO), the most abundant protein in YPE, and ovalbumin (OVA), representing chicken egg proteins. Overall, results highlighted the formation of non-covalent complexes with higher affinity under acidic conditions (pH 3.5). UV–vis and fluorescence quenching analyses revealed that ENO formed stronger molecular interactions with the extracts than OVA. FTIR spectroscopy showed a decrease in α-helices and a concurrent increase in random coil structures of ENO, with BE inducing greater protein unfolding and structural disorganization than GTE. In addition, 3D fluorescence spectra also highlighted conformational changes in BE structure upon binding with ENO. Electrochemical analysis proved that both GTE and BE antioxidant moieties were partially embedded within the protein structure, preserving their antioxidant capacity. The ENO emulsification activity index remained consistent after the addition of polyphenols, while its emulsion stability improved in the presence of BE (+48 %). The findings in this study suggest that ENO-polyphenol complexes have the potential to be applied as novel functional food ingredients.
最近,人们对酵母蛋白提取物(YPE)等替代蛋白质来源的兴趣日益浓厚,这使人们开始关注它们与多酚类物质的相互作用,因为多酚类物质可以增强蛋白质的结构和技术特性,同时提供有益健康的特性,如抗氧化活性。本研究采用多种技术方法研究了富含黄烷醇的绿茶提取物(GTE)和富含花青素的蓝莓提取物(BE)对烯醇化酶(ENO)(YPE 中含量最高的蛋白质)和卵清蛋白(OVA)(代表鸡卵蛋白)构象和功能特性的影响。总之,研究结果表明,在酸性条件下(pH 值为 3.5)形成的非共价复合物具有更高的亲和力。紫外可见光和荧光淬灭分析表明,ENO 与提取物形成的分子相互作用比 OVA 更强。傅立叶变换红外光谱显示,ENO 的 α 螺旋结构减少,同时无规线圈结构增加,与 GTE 相比,BE 诱导的蛋白质解折和结构紊乱程度更大。此外,三维荧光光谱也突显了 BE 与 ENO 结合后结构的构象变化。电化学分析证明,GTE 和 BE 的抗氧化分子都部分嵌入了蛋白质结构中,从而保持了其抗氧化能力。添加多酚后,ENO 的乳化活性指数保持不变,而其乳化稳定性在 BE 的存在下有所提高(+48 %)。这项研究结果表明,ENO-多酚复合物具有作为新型功能性食品配料的潜力。
{"title":"Polyphenols as enhancers of emulsifying and antioxidant properties of egg and yeast protein emulsions: Understanding the molecular interactions behind their technological and functional potential","authors":"Ana Catarina Ribeiro , Carlo Bravo , Rui Miguel Ramos , Ricardo Dias , Nuno Mateus , Victor de Freitas , Rosa Pérez-Gregorio , Susana Soares","doi":"10.1016/j.foodhyd.2025.111399","DOIUrl":"10.1016/j.foodhyd.2025.111399","url":null,"abstract":"<div><div>The rising interest in alternative protein sources, such as yeast protein extracts (YPEs), has recently brought attention to their interactions with polyphenols, which can enhance their structural and technological properties while providing health-beneficial properties, such as antioxidant activity. In this study, a multi-technique approach was employed to investigate the effects of a green tea extract (GTE), rich in flavanols, and a blueberry extract (BE), rich in anthocyanins, on the conformational and functional properties of enolase (ENO), the most abundant protein in YPE, and ovalbumin (OVA), representing chicken egg proteins. Overall, results highlighted the formation of non-covalent complexes with higher affinity under acidic conditions (pH 3.5). UV–vis and fluorescence quenching analyses revealed that ENO formed stronger molecular interactions with the extracts than OVA. FTIR spectroscopy showed a decrease in α-helices and a concurrent increase in random coil structures of ENO, with BE inducing greater protein unfolding and structural disorganization than GTE. In addition, 3D fluorescence spectra also highlighted conformational changes in BE structure upon binding with ENO. Electrochemical analysis proved that both GTE and BE antioxidant moieties were partially embedded within the protein structure, preserving their antioxidant capacity. The ENO emulsification activity index remained consistent after the addition of polyphenols, while its emulsion stability improved in the presence of BE (+48 %). The findings in this study suggest that ENO-polyphenol complexes have the potential to be applied as novel functional food ingredients.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"167 ","pages":"Article 111399"},"PeriodicalIF":11.0,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143777131","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-03-31DOI: 10.1016/j.foodhyd.2025.111388
Fengzhao Wang , Jinfeng Bi , Yuting Huang , Jian Lyu
In order to explore the interaction mechanism between pectin and sugar molecules, a simulation system containing peach pectin and trehalose was constructed. The compared studies were carried out based on the changes in structural characteristics of pectin (P), pectin with heat treatment (HP) and pectin compounding with trehalose with heat treatment (TP). Firstly, pectin from peaches was characterized by the molecular weight, monosaccharide, chemical group and nanostructure. Furthermore, the isothermal titration calorimetry (ITC) and molecular docking were applied to explain the bonding force between pectin and trehalose. Results showed that the highest molecular weight (4.17 × 105 g/mol) depicted in TP illustrated the retarded effect of trehalose on the depolymerization or decomposition of pectin during thermal processing, which might ascribed to the branched chain structure of pectin and the intact three-dimensional network structure. Fourier transform infrared (FT-IR) spectroscopy and nuclear magnetic resonance (NMR) spectra revealed the imbedding of trehalose molecules within the pectin chains. ITC analysis suggested the exothermic binding between trehalose and pectin (ΔH = −27.89 kJ/mol) was primarily driven by enthalpy, and the binding stoichiometry (trehalose/pectin) was above 3:1. Molecular docking confirmed that hydrogen bond with a binding energy of −6.061 kcal/mol was the bonding force between trehalose and pectin. The results will provide a theoretical foundation for elucidating the effect of osmotic dehydration on the structural changes in pectin, which will significantly affect the textural formation of dehydrated fruits and vegetables.
{"title":"Revealing the interaction mechanism between pectin and sugar: A case study of peach pectin and trehalose","authors":"Fengzhao Wang , Jinfeng Bi , Yuting Huang , Jian Lyu","doi":"10.1016/j.foodhyd.2025.111388","DOIUrl":"10.1016/j.foodhyd.2025.111388","url":null,"abstract":"<div><div>In order to explore the interaction mechanism between pectin and sugar molecules, a simulation system containing peach pectin and trehalose was constructed. The compared studies were carried out based on the changes in structural characteristics of pectin (P), pectin with heat treatment (HP) and pectin compounding with trehalose with heat treatment (TP). Firstly, pectin from peaches was characterized by the molecular weight, monosaccharide, chemical group and nanostructure. Furthermore, the isothermal titration calorimetry (ITC) and molecular docking were applied to explain the bonding force between pectin and trehalose. Results showed that the highest molecular weight (4.17 × 10<sup>5</sup> g/mol) depicted in TP illustrated the retarded effect of trehalose on the depolymerization or decomposition of pectin during thermal processing, which might ascribed to the branched chain structure of pectin and the intact three-dimensional network structure. Fourier transform infrared (FT-IR) spectroscopy and nuclear magnetic resonance (NMR) spectra revealed the imbedding of trehalose molecules within the pectin chains. ITC analysis suggested the exothermic binding between trehalose and pectin (Δ<em>H</em> = −27.89 kJ/mol) was primarily driven by enthalpy, and the binding stoichiometry (trehalose/pectin) was above 3:1. Molecular docking confirmed that hydrogen bond with a binding energy of −6.061 kcal/mol was the bonding force between trehalose and pectin. The results will provide a theoretical foundation for elucidating the effect of osmotic dehydration on the structural changes in pectin, which will significantly affect the textural formation of dehydrated fruits and vegetables.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"167 ","pages":"Article 111388"},"PeriodicalIF":11.0,"publicationDate":"2025-03-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143746837","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}