Protein Surface Hydrophobicity Research Articles

Hemp (Cannabis sativa L.) protein concentrates from wet and dry industrial fractionation: Molecular properties, nutritional composition, and anisotropic structuring

Hemp seeds stand as a rich source of globulins and albumins with all the essential amino acids and a balanced amino acid profile. Nevertheless, the potential of dry- and wet-extracted hemp protein concentrates to create plant-based, fibrous High Moisture Meat Analogues (HMMAs) remains unknown. In this study, five distinct hemp seed protein concentrates (55.9–76.4% protein, d.b.) produced at industrial scale using dry or wet fractionation were investigated and compared for their functionality and protein molecular properties. Furthermore, non-proteinaceous components were also analysed to elaborate on the underlying mechanisms for the structuring behaviour of hemp protein concentrates during wet extrusion. Although dry fractionation resulted in lower protein concentration, hemp proteins retained their native oligomeric state and their albumin fraction, thus showing higher surface hydrophobicity and solubility, and lower gelation concentration than wet-extracted counterparts. Furthermore, hemp samples were richer in bound polyphenols (>1800 mg/100 g), presumably phenolic acids, than the control pea sample (1363 mg/100 g), which resulted in dark colours in wet-extracted samples. Selected HMMA prototypes were developed and investigated for anisotropy, viscoelasticity, and proton NMR relaxometry. Visual and instrumental anisotropy dramatically increased with the use of hemp protein concentrates, from 0.69% using pea, to 0.98% and 1.41% using dry- and wet-fractionated fractionated hemp, respectively. Nonetheless, dry-fractionated hemp HMMA showed the highest proportion of free water in the system ( T 23 proton relaxation time), and an intermediate viscoelasticity between pea and wet-fractionated hemp HMMAs. Interestingly, SDS-PAGE revealed a significant contribution of disulphide bonds on hemp protein aggregation during processing. • Wet isolation decreased hemp protein surface hydrophobicity, solubility and lightness. • Hemp protein samples resulted in meat analogues with visible fibrous-like structures. • Dry-fractionated hemp extrudates had the highest proportion of free water. • Hemp extrudates showed up to 200% higher anisotropy than the pea protein counterpart. • Disulphide bonds played a key role on hemp protein aggregation during extrusion.

Changes in partial properties of glycosylated egg white powder during storage.

Glycosylation is an effective method to modify protein. However, there is a lack of research on the property changes of glycosylated protein during storage. In the present study, the changes in the physicochemical, functional, and structural properties of xylo-oligosaccharide (XOS) glycosylated egg white powder (EWP) (XOS-EWP conjugates) prepared with different glycosylation conditions (XOS/EWP ratio and reaction time) were investigated when stored at 25 °C and 60% relative humidity. In the 12 weeks of storage, the degree of grafting, browning, and the formation of Maillard reaction products of XOS-EWP conjugates increased. The increase in XOS/EWP ratio and reaction time led to an increase in protein aggregation, though a decrease in solubility, due to increased degree of glycosylation and structural changes. Furthermore, improved gel hardness of XOS-EWP conjugates deteriorated, while improved emulsification ability was kept stable during storage. For the sample with a lower XOS/EWP ratio and reaction time, the gel hardness and emulsifying properties underwent little or no deterioration even improving during storage. The results could be attributed to the limited degree of glycosylation, further unfolding of the protein structure, increased surface hydrophobicity of protein, and improved thermal characteristics. During storage, the Maillard reaction would continue to occur in the glycosylated EWP, further affecting the performance of modified EWP. Modified EWP prepared under different glycosylation conditions performed differently during storage. Modified EWP with a larger XOS/EWP ratio and reaction time meant it was harder to maintain good performance. Modified EWP with a smaller XOS/EWP ratio and reaction time changed significantly to better performances. © 2022 Society of Chemical Industry.

Enhanced salt-tolerance of Bacillus subtilis glutaminase by fusing self-assembling amphipathic peptides at its N-terminus.

Glutaminase (EC 3.5.1.2) can catalyze the deamidation of glutamine, which has been used to improve umami taste in oriental fermented foods. However, a high salt concentration is still a fundamental challenge for glutaminase application, especially in soy sauce production. To improve the salt tolerance of glutaminase, the self-assembling amphiphilic peptides EAK16 and ELK16 were fused to the N-terminus of a mutant (E3C/E55F/D213T) derived from Bacillus subtilis glutaminase, yielding the fusion enzymes EAK16-E3C/E55F/D213T and ELK16-E3C/E55F/D213T, respectively. As ELK16-E3C/E55F/D213T was expressed as insoluble active inclusion bodies, only the purified EAK16-E3C/E55F/D213T was subjected to further analyses. After the incubation with 18% (w/v) NaCl for 200 min, the residual activities of EAK16-E3C/E55F/D213T in a NaCl-free solution reached 43.6%, while E3C/E55F/D213T was completely inactivated. When the enzyme reaction was conducted in the presence of 20% NaCl, the relative activity of EAK16-E3C/E55F/D213T was 0.47-fold higher than that of E3C/E55F/D213T. As protein surface hydrophobicity and protein particle size analysis suggested, oligomerization may play an important role in the salt-tolerance enhancement of the fusions. Furthermore, EAK16-E3C/E55F/D213T achieved a 0.88-fold increase in the titer of glutamic acid in a model system of soy sauce fermentation compared to E3C/E55F/D213T. Therefore, the fusion with self-assembling amphiphilic peptides is an efficient strategy to improve the salt-tolerance of glutaminase.

Study on moisture migration mechanism of dough during subfreezing storage

AbstractBackground and ObjectivesThe objective of this study was to investigate the effects of subfreezing storage on gluten protein denaturation and water retention. On this basis, the surface hydrophobicity, secondary structure, thermal stability, microstructure, and moisture distribution of gluten protein were measured.FindingsThe results showed that at the end of storage, the hydrophobicity indexes of wheat gluten proteins (−9°C and −12°C) stored under subfreezing conditions were significantly lower than those stored at 4°C and slightly lower than those stored at −18°C. The secondary structure stability of wheat gluten stored at −18°C was similar. P21 stored at −18°C was significantly higher than those stored at 4°C and showed an upward trend. The quality of the dough was similar to those stored at −18°C.ConclusionsThe deformation and water retention of gluten during subfreezing storage are similar to those stored at −18°C.Significance and NoveltyThe changes in dough moisture and gluten protein structure during frozen storage at different freezing temperatures were explored to provide a theoretical basis for the application of subfrozen storage in the frozen flour products industry.

Changes in protein oxidation, structure, and thermal stability of chicken breast subjected to ultrasound-assisted immersion freezing during frozen storage

The influence of ultrasound-assisted immersion freezing (UF), immersion freezing (IF), and air freezing (AF) on the protein oxidation, structure, and thermal stability of chicken breast during frozen storage was evaluated in this study. Compared to IF and AF samples, the UF samples had a lower carbonyl content, dityrosine content, and surface hydrophobicity of myofibrillar protein (MP) (P < 0.05), as well as a higher free amino group content and total and reactive sulfhydryl content (P < 0.05). Moreover, UF significantly delayed the deterioration of protein secondary and tertiary structures and the decrease in protein thermal stability during frozen storage (P < 0.05). Additionally, the UF samples at 180 days had similar protein structures and quality characteristics to the IF samples at 90 days or the AF samples at 60 days. Overall, UF treatment can effectively retard protein oxidation, protein structure deterioration, and protein thermal stability loss caused by frozen storage.

Interaction mechanism between cereal phenolic acids and gluten protein: protein structural changes and binding mode.

Phenolic acids are antioxidant nutrients in cereals and affect the quality of wheat products and the properties of gluten protein. Gallic acid (GA), caffeic acid (CA), syringic acid (SA), and p-coumaric acid (p-CA) were selected to study the interaction mechanism between cereal phenolic acids and gluten protein. The results showed that adding GA significantly (P < 0.05) decreased the content of free sulfhydryl in gluten proteins by 70-87.26% compared with the control group. The aggregates' behavior of gluten protein induced by adding the phenolic acids would produce oversized particles (>5000 nm). Adding the selected phenolic acids changed the hydrogen-bond linkage of protein secondary structure. Zeta potential values of gluten protein increased significantly (P < 0.05) by 14.41%, 26.49%, 30.77%, and 57.93% for CA, p-CA, GA, and SA respectively added at 0.03 g kg-1 . Moreover, the gluten protein surface hydrophobicity increased when the phenolic acids were added at 0.03 g kg-1 , displaying the effect of the phenolic acid on the hydrophobic interaction of protein. Molecular docking results showed that the selected phenolic acids could interact with glutenin and gliadin using hydrogen-bond formation, and SA had the strongest binding with glutenin and gliadin. The results demonstrated that the selected phenolic acids could interact with gluten protein via covalent cross-linking as well as by hydrogen bonding, thereby changing the structure of the gluten protein. This exploration is expected to provide theoretical support for the development and utilization of whole-grain foods. © 2022 Society of Chemical Industry.

Selective removal effect of subcritical fluid extraction on egg yolk lipids and characterization and enzymatic improvement of defatted egg yolk powder

This study investigated the effects of subcritical fluid extraction on lipid removal and the physicochemical properties of egg yolk powder. In addition, two-step enzymatic hydrolysis was used to improve the physicochemical properties. The content of total lipids and cholesterol decreased to 30.2% and 10.5 mg/g after subcritical propane-butane extraction, respectively, while phospholipids were retained. Protein solubility, surface hydrophobicity and total sulfhydryl results showed that this partial defatting avoided further quality deterioration of egg yolk powder. Scanning electron microscopy and confocal microscopy showed that the surface morphology and distribution of proteins and lipids changed with defatting degree. After two-step enzymatic hydrolysis, protein solubility of subcritical propane-butane extraction egg yolk powder significantly increased to 31.4% and soluble peptides with an average molecular weight lower than 1000 Da accounted for 70.0%. The improved defatted egg yolk powder is rich in protein, peptides and phospholipids and has great potential as a nutritional supplement.

Evaluation of protein degradation and flavor compounds during the processing of Xuan'en ham.

Protein degradation occurs during the processing of dry-cured ham, which has important influences on the flavor and quality of products. The aim of this work was to study the degradation kinetics of myofibrillar proteins (MPs) and sarcoplasmic proteins (SPs) extracted from the biceps femoris muscle during the processing of Xuan'en ham. A relationship between protein degradation and the flavor formation was found. During the processing of Xuan'en ham, MPs and SPs were mainly degraded in the salting stage and incipient fermentation. Accompanied by protein degradation, the content of carbonyl group in SPs increased gradually, but in MPs, it first increased and then decreased. Interconversion between sulfhydryl and disulfide bonds was investigated during this processing. Oxidation, degradation, and thermal effects significantly affected the surface hydrophobicity of proteins. More than one hundred volatile compounds have been identified at each stage of ham preparation. Among them, organic acids were the predominant group, followed by hydrocarbons, aldehydes, alcohols, ketones, and esters.

Development of a rapid, high-sensitivity, low-cost fluorescence method for protein surface hydrophobicity determination using a Nanodrop fluorospectrometer

A microvolumetric method for surface hydrophobicity (H0) determination of proteins using a Nanodrop fluorospectrometer was developed. This method reduces the protein and fluorophore quantities that are necessary for sample preparations and readings by two and three orders of magnitude, respectively, compared to conventional methods. In addition, readings can be obtained in just 2–6 s. Bovine serum albumin (BSA) and 1-anilino 8-naphthalene sulfonic acid (ANS) were used for the first optimization of appropriate fluorophore-protein conditions for H0 determination (20 μM ANS, 0.5–4 μM BSA, pH 5). Based on validation guidelines, the novel method shows linear behavior, good intraday precision, accuracy, and sensitivity. This method was robust against several factors, as determined by a Youden-Steiner test. Additional surface hydrophobicity determinations using several proteins demonstrate suitable method applicability. The present microvolumetric method provides a reliable technique to determine the H0 of proteins for pharmaceutical, biotechnological, and food applications.

Interaction and binding mechanism of lipid oxidation products to sturgeon myofibrillar protein in low temperature vacuum heating conditions: Multispectroscopic and molecular docking approaches.

In this work, the binding mechanism of myofibrillar protein (MP) with malondialdehyde and 4-hydroxy-2-nonenal under low temperature vacuum heating was investigated via multispectroscopic and molecular docking. The results showed that binding interaction and increasing temperature caused significant changes in the conformations as well as a decrease in the value of protein intrinsic fluorescence, surface hydrophobicity, and fluorescence excitation-emission matrix spectra. Furthermore, the decrease in α-helix and β-turn, increase in β-sheet and a random coil of MP, imply the MP molecules to be more unfolded. Isothermal titration calorimetry and molecular docking results showed that main driving force for binding with MP was hydrogen bond, and the binding ability of malondialdehyde was superior to that of 4-hydroxy-2-nonenal. Moreover, increasing the heating temperature was beneficial to the binding reaction and intensified the conformational transition of MP. These results will provide a reference for further studies on the lipid and protein interaction of sturgeon.

Engineered Design of the E-Helix Structure on Ferritin Nanoparticles.

Insertion of an immunogenic epitope at the C-terminus of ferritin has shown the potential to produce a stable and efficacious vaccine. There is however limited understanding of how C-terminus insertion affects ferritin protein stability. The E-helix at the C-terminus has attracted interest because there are contradictory reports as to whether it has a role in protein stabilization. Here, we report, for the first time, combining molecular dynamics simulation (MDS) with experiment to engineer the design of the E-helix at the C-terminus of engineered human ferritin heavy chain (F1) inserted with Epstein-Barr nuclear antigen 1 (EBNA1, E1) and flexible linker (L3) residues (to afford F1L3E1). Hot spots on the E-helix of the C-terminus were predicted by MDS at aa 167 (Glu) and aa 171 (Asp). Five (5) variants of F1L3E1 were constructed by considering hot spots and alteration of electrostatic or hydrophobic interfaces, namely, (1) C1, hot spots substituted with noncharged residue Gln; (2) C2, hot spots substituted with positively charged residue Arg; (3) C3, hydrophobic residues substituted with the most hydrophobic residues Val and Ile; (4) C4, hydrophobic residues substituted with the most hydrophilic residues Gln and Asn; and (5) C5, a heptad repeat structure in the E-helix disrupted by substituting "a" and "d" heptad residues with noncharged polar residue Gln. It was found that the E-helix is essential to maintain integrated protein stability and that changing the hydrophobic interface (C3 and C4) had more significant effects on protein folding and stability than changing the electrostatic interface (C1 and C2). It was confirmed by both MDS and experiment that variants C1, C2, and C5 were able to fold to form stable conformational structures with protein surface hydrophobicity similar to that of F1L3E1. However, they are less thermally stable than F1L3E1. Significant changes in hydrophobicity drove significant protein aggregation for variants C3 and C4. It is concluded that the molecular design of the C-terminus in engineered ferritin, especially the E-helix, is important to ensure the epitope-based chimeric vaccine is safe (aggregate free) and efficacious.

Modification of grass pea protein isolate (Lathyrus sativus L.) using high intensity ultrasound treatment: Structure and functional properties

In this study the effect of different high intensity ultrasound (HIU) amplitudes (25, 50 and 75%) and sonication times (5, 10 and 20 min) on the structure and functional properties of grass pea protein isolate (GPPI) was investigated. A higher sonication amplitude and longer time improved the protein solubility and surface hydrophobicity and reduced the particle size of GPPI. These physicochemical alterations in GPPI enhanced the protein adsorption at the oil–water interface, reduced the interfacial tension and increased the EAI and ESI values. SDS-page demonstrated that sonication did not change the primary structure of the protein. However, CD spectroscopy indicated a reduction in α-helix and an increase in the content of β-sheet and random coil structures in the sonicated GPPI. The free SH groups content and UV–vis absorbance intensity increased after the sonication. However, prolonged sonication up to 20 min reduced the free SH content in GPPI due to the oxidation of susceptible SH groups. HIU increased the thermal degradation of GPPI and lowered the least concentration needed for gelatinization of GPPI (LGC). Therefore, less protein powder was needed to form a strong gel compared to the non-sonicated GPPI. Sonicated GPPIs showed higher gel strength especially when 75% amplitude used for 10 min. These results showed that the HIU is a promising approach for modification of the functional properties of GPPI for food applications.

Ultrasound and effect on the surface hydrophobicity of proteins: a meta‐analysis

SummaryThis review aims to investigate and evaluate the effect of ultrasound process parameters on the interfacial properties (surface hydrophobicity) of food proteins. The data obtained from English published papers accessed on Web of Science, PubMed and Wiley published from 2013 to 2021 allowed a table overview construction and a meta‐analysis. Study selection was conducted based on the Preferred Reporting Items for Systematic Reviews and Meta‐Analyses method. A total of 40 relevant reports and 185 data used for meta‐analysis were considered. In general, the results revealed that the use of the ultrasound process increased the surface hydrophobicity of proteins. Processing time, power, amplitude and ultrasound frequency were significant in protein modification. The findings showed that the ultrasound process parameters should be considered to assess the effect on the modification and improvement of the interfacial properties of proteins.

Effects of microsize on the biocompatibility of UiO67 from protein-adsorption behavior, hemocompatibility, and histological toxicity

The biocompatibility of metal–organic frameworks (MOFs) is necessary to humans but is far from being sufficiently addressed. This study focused on the effects of microsize on the biocompatibility of MOFs by selecting UiO67 with micron and submicron size as the MOFs models. Under the dose metric of surface area, the binding constant between UiO67 and human serum albumin (HSA) gradually increased with increased UiO67 size. Submicron UiO67 induced stronger conformational transformation and more greatly affected the protein surface hydrophobicity than micron UiO67. Micron UiO67 also inhibited the esterase-like activity of HSA through competitive inhibition mechanism, whereas submicron UiO67 inhibited it through noncompetitive inhibition mechanism. The size of UiO67 had little effect on hemocompatibility. A smaller size of UiO67, corresponded with a higher IC50 value for 293 T and LO2 cells, and the adsorption of HSA can effectively improve cytotoxicity. In vivo toxicity evaluations revealed that all UiO67 did not cause obvious distortion of organs, and they were metabolized primarily in the kidney. These results provided useful information about the toxicity of MOFs and experimental references for the development of MOFs-based engineering materials.

The influence of protease hydrolysis of lactic acid bacteria on the fermentation induced soybean protein gel: Protein molecule, peptides and amino acids

The purpose explored the influence of protease hydrolysis of lactic acid bacteria and its hydrolysates on the fermentation induced soybean protein gel. The changes of protein molecule, peptides and amino acids after hydrolysis were analyzed. With the extension of fermentation time, the molecules (≤30 kDa) of L. paracasei-gel and L. plantarum-gel increased to 68.8% and 63%, the surface hydrophobicity of protein was increased, internal sulfhydryl groups and soluble proteins were reduced. These results indicated physicochemical properties of protein molecules were changed, small molecular proteins produced by hydrolysis were aggregated through intermolecular forces to promote gel formation. Peptide profiles and amino acid profiles showed that the peptides (≤10AA) of L. casei-gel increased by 3.32%, the peptides derived from 7S protein increased by more than 5%, the hydrophobic peptides and hydrophobic amino acids increased, these enzymatic hydrolysates may form insoluble aggregate through intermolecular forces to promote gel formation.

Effects of different curing methods on edible quality and myofibrillar protein characteristics of pork

This study aimed to investigate the effects of standing curing (SC), tumbling curing (TC), vacuum tumbling curing (VTC) and ultrasonic-assisted curing (UAC) on the edible quality of black pork and property of myofibrillar proteins (MPs) extracted from black pork. The results showed that all curing methods could improve the marinating absorptivity and the gel water retention of black pork, the solubility and surface hydrophobicity of myofibrillar proteins, and reduce the cooking loss and shear force of black pork, the hydrogen bond content of myofibrillar proteins and the gel whiteness compared with the control group (SC). The result of sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE) showed that the concentration of protein bands by VTC treatment was decreased obviously. In addition, the result of the scanning electron microscope (SEM) presented that tumbling and ultrasound treatment would destroy the structure of muscle fibers and make them loose and disordered.

Effects of combined high pressure and temperature on solubility, foaming, and rheological properties of soy 11S globulin

AbstractThis study examines the effects of combined high pressure (0.1, 200, and 400 MPa) and temperature (25 and 50°C) on the solubility, aggregation, conformation, foaming, emulsifying capacity, and rheological properties of soy 11S globulin. The foaming stability, particle size, free sulfhydryl groups content, emulsifying activity, emulsifying stability, and shear stress of soy 11S globulin were decreased significantly (p ≤ .05) compared with that of 0.1 MPa‐treated sample, but the solubility, surface hydrophobicity, foaming capacity, and apparent viscosity were increased significantly (p ≤ .05), except the sample treated at 400 MPa and 50 ± 2°C. The solubility, surface hydrophobicity and free sulfhydryl groups content of soy 11S globulin decreased significantly (p ≤ .05) with increasing pressure and temperature, which caused the decrease of the foaming capacity, emulsifying activity, emulsifying stability, shear stress, and apparent viscosity. Overall, the use of high‐pressure and thermal treatments combined could change the foaming, emulsifying, and rheological properties of soy 11S globulin through the increase/decrease of protein solubility, aggregation, surface hydrophobicity, and free sulfhydryl groups content.Practical applicationsThis study provides a method of high‐pressure and thermal treatments combined, which can change the solubility, foaming, and rheological properties soy 11S globulin, and its use should be expanded in food processing.

Influence of ultrasonic treatment on functional properties and structure of tussah pupa protein isolate

Tussah pupa protein is one of the high-quality insect proteins with high nutritional value and has been gradually recognised by the public, which can be used as a substitute for traditional animal-derived food proteins. But in contrast, the processing potential of it is much worse. Given this, this study took tussah silkworm chrysalis as the research object, and the isolated protein was extracted by alkali dissolution and acid precipitation and treated by ultrasonic wave (suspension concentration 9%, ultrasonic time 100 min, ultrasonic amplitude 40%), the effects of ultrasound were evaluated by determining the tussah pupa protein isolate (TPPI) functionalities and its structure changes. The results showed that compared with the untreated TPPI, the ultrasound-treated TPPI solubility significantly increased 4.57 times, water-holding capacity increased 1.06 times, emulsifying activity and emulsifying stability increased 2.10 times and 1.23 times respectively, foaming capacity as well as foaming stability increased 1.83 times and 1.05 times respectively (P&lt;0.05). Besides, the protein surface hydrophobicity and flexibility were also strongly improved (P&lt;0.05). Protein structure analysis showed that the disulphide bonds content reduced 1.21 times, sulfhydryl content increased 0.82 times, α-helices and random coils content in protein secondary structures increased significantly, β-sheets and β-turns content significantly decreased (P&lt;0.05) after ultrasonic treatment, indicating that ultrasound caused the transformation of some ordered structures into irregular structures. According to Fourier transform infrared spectrum, some protein characteristic peaks changed, including O-H stretching vibration intensity increased, and the amide I band moved to the low wavenumber direction, which indicated that the spatial structure of TPPI had been extended. Ultrasonic treatment can expose the internal polar groups and increasing the surface active sites of protein, to improve some functional properties of TPPI to a certain extent, which provided a theoretical foundation for developing new types of tussah pupa protein foods.

The essential role of hydrophobic interaction within extracellular polymeric substances in auto-aggregation of P. stutzeri strain XL-2

To enrich the understanding of bio-aggregates formation, the mechanism of auto-aggregation is one of the concerns in wastewater treatment. The auto-aggregation ability by P. stutzeri strain XL-2 was mainly attributed to the self-secretion of extracellular polymeric substances (EPS). A comprehensive correlation analysis indicates that hydrophobic interaction within EPS played essential roles in auto-aggregation. To give insights into the underlying mechanisms, tightly bound EPS (TB-EPS), loosely bound EPS (LB-EPS) and soluble EPS (S-EPS) were characterized by colorimetry, hydrophobicity, enzymatic hydrolysis, FT-IR spectroscopy and XPS analysis, showing that proteins in TB-EPS comprised a high proportion of hydrophobic carbon-containing (C-containing) functional groups. Further amino acids analysis revealed that these C-containing functional groups might derive from the hydrophobic R groups of amino acids, which significantly affected the surface hydrophobicity of proteins in TB-EPS and thus promoted the auto-aggregation of strain XL-2. This work provides an in-deep understanding of the auto-aggregation mechanism by strain XL-2, which may enrich the understanding of microbial aggregates formation and lead to further application of strain XL-2 in wastewater treatment processes.

The influence of xylanase and thermal treatment on the composition and interfacial rheology properties of whole wheat dough liquor

SummaryThe dough liquor (DL) centrifuged from dough played an important role in determining the gas cell stability during dough making, and the adding of xylanase (XYL) in the dough could efficiently increase the stability of DL foam, especially at 60 °C. In this work, we prepared whole wheat dough added with different dosages of XYL and extract the DL. The components especially proteins in DL and their interaction mechanism and interfacial rheology properties at the air–water interface were studied. The proteins formed protein aggregates (&gt;150 kDa) at 60 °C. After XYL treatment, DL solution exhibited higher protein surface hydrophobicity and surface pressure. And the equilibrium surface pressure of DL varied between 23 and 28 mN m−1. At 25 °C, the interfacial dilatational modulus increased by 26.77% and 14.22% compared with control, respectively. And the XYL can improve the interface shear strength both for the unheated and heated DL solutions. These findings showed that XYL might improve the ability of DL constituents to stabilise the air–water interface to contribute to the stability of gas cells in the dough. The obtained results have provided a theoretical basis for improving the gas cell stability by changing the properties of whole wheat DL with the addition of XYL.