Free Sulfhydryl Content Research Articles

Deacetylation enhances the structure and gelation properties of konjac glucomannan/soy protein isolate cold-set gels

This study aimed to investigate the effect of the deacetylated konjac glucomannan (DKGM), with varying degree of deacetylation (DD), on the physicochemical and structural properties of transglutaminase-induced soy protein isolate (SPI) cold-set gels. Compared with native konjac glucomannan (KGM), DKGM significantly enhanced the gel strength, water-holding capacity, and thermal stability of the composite gels, with DK3 (DKGM with 65.85 % deacetylation) showing the most significant improvement. The secondary and tertiary structures of SPI in the DK3 group were the most stable. Compared with the KGM group, the DK3 group showed a 58.32 % increase in hydrophobic interaction and a 37.98 % decrease in free sulfhydryl content. The microstructure results demonstrated that DK3 was uniformly dispersed within the SPI network, promoting the formation of a continuous and dense network structure. This was mainly due to DK3 having a moderate particle size and low viscosity. Therefore, DKGM with a moderate DD is conducive to forming a more ordered and dense gel network structure, imparting optimal gel performance to the SPI cold-set gel.

Effects of interaction between wheat bran dietary fiber and gluten protein on gluten protein aggregation behavior.

Effects of wheat bran dietary fiber (WBDF) as a nutritional additive on flour products quality mainly depends on the interaction between WBDF and gluten protein. In this study, the effects and mechanisms of WBDF with different particle sizes and additive amounts on gluten protein aggregation behavior were investigated. The results showed that the addition of WBDF led to a decrease in free sulfhydryl content, particle size, molecular weight and gluten macromer (GMP) content, an increase in zeta potential and SDS-extractable protein content, and a deterioration in the gluten network morphology compared to the control group, suggesting that the aggregation behavior of gluten protein was inhibited. When WBDF was added at 3 % and 6 %, dilution effect, mechanical shear, steric hindrance, and non-covalent binding were the main mechanisms leading to depolymerization. Further addition of WBDF (9 %, 12 %) inhibited the depolymerization of gluten protein due to competitive hydration and non-covalent binding. However, when WBDF was added at 15 %, the dilution effect, mechanical shear and steric hindrance of WBDF (88 μm < particle size<150 μm) dominated, and their inhibitory of aggregation induced the formation of a loose gluten network structure. In contrast, the weaker mechanical shear and steric hindrance effects of WBDF (particle size<88 μm) mitigated the degradation of gluten network structures by WBDF.

Revealing the influence mechanism of pre-fermentation degree and storage temperature fluctuations on frozen steamed bread dough quality

This study investigated the effects of pre-fermentation degree and storage temperature fluctuations on the gas cells, gluten protein, rheological properties of frozen dough, and quality of steamed bread. Three pre-fermentation degrees and four fluctuating temperatures (−10 °C, 0 °C, 10 °C, and 25 °C) were used. The gas cell size increased with the pre-fermentation degree; however, the gas cells merged and ruptured during temperature fluctuations. Sodium dodecyl sulfate extraction protein content and free sulfhydryl content increased by 3.07 % and 33.62 %, respectively, in the medium pre-fermentation group at 25 °C compared with those at −10 °C. The maximum strain of dough increased as pre-fermentation degree and fluctuating temperatures increased. The specific volumes of steamed bread with medium pre-fermentation degree were 1.87 mL/g at −10 °C and 1.47 mL/g at 25 °C. In conclusion, higher temperature fluctuations exceeding the freezing point exacerbated the dough and steamed bread quality, particularly in high pre-fermentation degree dough.

Dual modification of the aggregation behavior and in vitro digestion of oxidized pine kernel protein via a combination of homogenization and succinylation

Protein oxidation affects the high-value utilization of nuts as oxidative attack causes protein aggregation, thereby challenging their technological functionality. Herein, a strategy using homogenization-assisted octenyl succinic anhydride (OSA) modification was proposed to tailor the structure, aggregation behavior, and digestive characteristics of oxidized pine kernel proteins. Results indicated that the ratio of α-helices to β-turns ranged from as low as 0.43 up to 0.67 after homogenization, suggesting greater molecular flexibility. With increasing protein oxidation, the acylation degree exhibited an inverted V-shaped trend, peaking at 67.22 %. OSA treatment reduced the aggregation rate and prolonged the lag time of proteins by stabilizing the α-helices and β-turns, increasing hydrogen bonding, and decreasing hydrophobicity. This increased the solubility of oxidized pine kernel proteins by ~30 % and improved their fluidity and thermal stability. A lower degree of succinylation was associated with higher free sulfhydryl content and surface hydrophobicity, which facilitated the thermal aggregation and the formation of elastomeric gels. Furthermore, the in vitro dynamic digestion and morphological observations of hydrolysis products indicated that cotreated proteins exhibited higher digestibility and formed small spherical particles ranging from 405.50 to 676.50 nm. These findings provide a promising approach to mitigate the adverse effects of oxidation on nut proteins.

Functionality enhancement of pea protein isolate through cold plasma modification for 3D printing application

Pea protein isolate (PPI) is a valued sustainable protein source, but its relatively poor functional properties limit its applications. This study reports on the effects of cold argon plasma (CP) treatment of a 15 % (w/w) PPI solution on the functionality, structure, and oxidative characteristics of PPI, as well as its application in 3D-printed plant-based meat. Results indicate that hydroxyl radicals and high-energy excited-state argon atoms are the primary active substances. A decrease in free sulfhydryl content and an increase in carbonyl content were observed in treated PPI, indicating oxidative modification. Compared to the control group, the gel strength of PPI was increased by 62.5 % and the storage modulus was significantly improved after 6 min treatment, forming a more ordered and highly cross-linked 3D gel network. Additionally, CP significantly improved the water-holding capacity, oil-holding capacity, emulsifying activity, and emulsion stability of PPI. The α-helix and random coil content in PPI decreased, while the β-sheet content increased, resulting in a more ordered secondary structure after CP treatment. Compared to untreated PPI, the consistency coefficient (K) increased from 36.00 to 47.68 Pa·sn. The treated PPI exhibited higher apparent viscosity and storage modulus and demonstrated better 3D printing performance and self-supporting ability. This study demonstrates that CP can significantly enhance the functional properties of PPI, providing great potential and prospects for improving the printability of 3D printing materials and developing plant protein foods with low-allergenicity.

Effects of eggshell powder emulsion gel on the oxidative stability and sustained-release effect of lavender essential oil

This study aimed to develop a new type of eggshell powder (EP) emulsion gels for improving the antioxidant ability and sustained release effect of lavender essential oil (LEO). The effects of EP addition on the physicochemical, structural properties, oxidative stability, and sustained-release performance of the emulsion gels were investigated. The results showed that with the increase of EP addition (0–1 %), the gel strength initially increased and then decreased. The emulsion gel with 1 % EP had better freeze-thaw stability (36.77 %), thermal stability (78.63 °C), and water holding capacity (96.57 %). Moreover, the micromorphology results indicated that the EP-ovalbumin (OVA)-konjac glucomannan (KGM) complex showed a connected filamentous network structure, and the emulsion gel with 1 % EP addition had the most uniform and densest network structure. Furthermore, the EP emulsion gel had the highest free sulfhydryl content and hydrophobic interaction, and LEO exhibited the best antioxidant and sustained-release properties at this time. In conclusion, the findings demonstrated the potential of eggshell powder to enhance emulsion gel stability, which could improve the high-value utilization of egg by-products.

Interfacial and foaming properties of plant and microbial proteins: Comparison of structure-function behavior of different proteins

Many plant proteins are amphiphilic molecules that can adsorb to air-water interfaces and form protective coatings around gas bubbles. In this study, the composition, structure, physicochemical properties, air-water interfacial properties, and foaming properties of 16 plant and microbial proteins were characterized. We found a correlation between the composition, structure, physicochemical properties, and foaming properties of the proteins. The foaming capacity of them showed a highly significant positive correlation (p ≤ 0.01) with their foaming stability, α-helix content, surface hydrophobicity, and free sulfhydryl content. The foaming capacity and foaming stability showed highly significant negative correlations with disulfide bond content (p ≤ 0.01). We found wheat gluten protein (WGP) and mung bean protein (MBP) had higher foaming capacity (102.67 ± 8.08 % and 89.33 ± 4.72 %), which could be attributed to higher surface hydrophobicity (179.68 ± 1.40 and 130.28 ± 1.41) and larger contact angle (82.369 ± 0.016° and 82.949 ± 0.228°).

Covalent interaction of ovalbumin with proanthocyanidins improves its thermal stability and antioxidant and emulsifying activity.

The structure of proanthocyanidins (PC) contains a large number of active phenolic hydroxyl groups, which makes it have strong antioxidant capacity. This study investigated the structural and functional properties of ovalbumin (OVA) modified by its interaction with PC. It was found that on increasing the concentration ratio of PC to OVA from 10:1 to 40:1, the free amino and total sulfhydryl contents of OVA decreased from 470.59 ± 38.77 and 29.81 ± 0.31 nmol mg-1 to 96.61 ± 4.55 and 21.22 ± 0.78 nmol mg-1, respectively, and the free sulfhydryl content increased from 7.65 ± 0.41 to 9.48 ± 0.58 nmol mg-1. These results indicated that CN and CS bonds were formed and PC was covalently linked with OVA. The PC content in the OVA-PC conjugates increased from 281.93 ± 12.92 to 828.81 ± 46.09 nmol mg-1 on increasing the concentration ratio of PC to OVA from 10:1 to 40:1. The contents of α-helix and β-turn of OVA decreased, and the contents of β-sheet and random coil increased, confirmed by circular dichroism. The tertiary structure of OVA was also altered according to the results of fluorescence and ultraviolet absorption spectra. The surface hydrophobicity of OVA-PC conjugates decreased with increasing bound polyphenol content. The conjugation of OVA to PC significantly improved its emulsification and antioxidant activity and denaturation temperature. This study may provide valuable information for improving OVA's functional properties and its PC conjugates for applications in the food industry. © 2024 Society of Chemical Industry.

Fabrication and characterization of whey protein isolate-tryptophan nanoparticles by pH-shifting combined with heat treatment

L-Tryptophan (Trp) is an essential amino acid with numerous health benefits. However, incorporating Trp into food products is limited due to its pronounced bitter taste. Encapsulating Trp in nanoparticles by using other natural biopolymers is a potential strategy to mask the bitter taste of Trp in the final products. Whey protein isolate (WPI), composed of alpha-lactalbumin (α-LA), bovine serum albumin (BSA), and beta-lactoglobulin (β-LG), has played a crucial role in delivering bioactive compounds. In order to incorporate Trp within WPI, the present study used a combination of pH-shifting andthermal treatment to fabricatewhey protein isolate-tryptophan nanoparticles (WPI-Trp-NPs). During the pH-shifting technique, WPI unfolds at high pH, such as pH 11, and the dissociated WPI molecules are refolded when pH is shifted back to neutral, creating particles with uniform dispersion and encapsulating smaller particles surrounding them in solution. Further, the well-distributed nanoparticles formed by pH-shifting might encourage the formation of more uniform nanoparticles during subsequent thermal treatment. TheWPI-Trp particles have an average particle size of 110.1 nm and a low average PDI of 0.20. Fluorescence spectroscopy confirmed the encapsulation of Trp by WPI, which shows higher fluorescence when the Trp is encapsulated by the WPI. Surface hydrophobicity, circular dichroism, particle size, free sulfhydryl, and antioxidant activity were used to characterize the WPI-Trp-NPs. WPI-Trp-NPs formed by pH-shifting combined with heating showed a higher surface hydrophobicity and free sulfhydryl content than the untreated WPI-Trp mixture. The conversion of α-helix into random coil in the WPI secondary structure indicated a more disordered structure of the modified whey protein. Molecular docking results indicate the interactions between Trp and WPI, including alpha-lactalbumin (α-LA), bovine serum albumin, and beta-lactoglobulin (β-LG), were mainly driven by hydrophobic interactions and hydrogen bonding. The binding affinity between Trp and these proteins was ranked as α-LA>BSA>β-LG. The combination of pH-shifting and heating improved the functionalityof WPI and was an effective way to fabricate WPI-Trp nanoparticles.

Changes in whey protein produced by different sterilization processes and lactose content: Effects on glycosylation degree and whey protein structure

In this study, the interaction patterns between whey protein and lactose were investigated after different ratios of whey protein and lactose (1:2.5; 1:3.0; 1:3.5; 1:4.0; 1:4.5) were treated with two typical sterilization process parameters in powdered products (68 °C, 20 min; 72 °C, 15 min) and two typical sterilization process parameters in liquid products (121 °C, 10 min and 121 °C, 15 min). It was found that the degree of the Maillard reaction of whey protein-lactose solution increased with increasing lactose content, increasing sterilization temperature, or extending sterilization time, which was accompanied by changes in the protein structure of whey protein. In addition, glycosylation accelerates the decrease in free sulfhydryl content, decreasing surface hydrophobicity and decreasing fluorescence intensity. These findings highlight the advantages of designing protein-carbohydrate formulations with a high ratio of whey protein-lactose (1:2.5) to meet the requirements of the product standards for preterm/low-birth-weight infant formulas. When comparing only the sterilization processes of powder and liquid products, the pasteurization process of powder products significantly reduced the degree of the Maillard reaction caused by heat treatment and reduced protein denaturation.

Heat-induced interactions between microfluidized hemp protein particles and caseins or whey proteins

The rising demand for sustainable proteins leads to increased interest in plant proteins like hemp protein (HP). However, commercial HP's poor functionality, including heat aggregation, limit its use. This study explored the heat-induced interactions of hemp protein particles (HPPs) with milk proteins, specifically whey proteins and caseins. Using various analysis techniques—static light scattering, TEM, SDS electrophoresis, surface hydrophobicity, and free sulfhydryl content—results showed that co-heating HPPs with whey protein isolate (WPI) or sodium caseinate (NaCN) at 95 °C for 20 min reduced HPPs aggregation. HPPs/WPI particles had a d4,3 of ∼3.8 μm, while HPPs/NaCN were ∼1.9 μm, compared to ∼27.5 μm for HPPs alone. SDS-PAGE indicated that whey proteins irreversibly bound to HPPs, through disulfide bonds, whereas casein bound reversibly, possibly involving the chaperone-like property of casein. This study proposes possible mechanisms by which HPPs interact with milk proteins and impact protein aggregation. This may provide opportunities for developing hybrid protein microparticles.

Effects of rosmarinic acid covalent conjugation on the allergenicity and functional properties of egg white protein

Polyphenols can form complexes with proteins, potentially enhancing the properties of egg white protein (EWP) by altering its structure. This study aimed to explore the effect of covalent conjugating with rosmarinic acid (RA), a bioactive polyphenol found in various edible Lamiaceae herbs, on the structure, allergenicity, and functional properties of EWP. The successful preparation of EWP-RA conjugates was confirmed through RA binding equivalent analysis. Fluorescence spectroscopy, Fourier transform infrared (FTIR) spectroscopy, circular dichroism (CD), and ultraviolet (UV) absorption spectroscopy collectively indicated that the covalent conjugation with RA led to significant structural alterations in EWP. Furthermore, the conjugation of RA markedly enhanced the antioxidant capacity of EWP, as evidenced by its improved ability to scavenge DPPH and ABTS+ radicals. Enzyme-linked immunosorbent assay (ELISA) results indicated a substantial reduction in the binding capacity of EWP-RA conjugates to IgG and IgE, indicating a decrease in the allergenic potential of EWP. Moreover, the incorporation of RA was associated with an increase in the absolute zeta potential, protein flexibility, and free sulfhydryl content of EWP, alongside a reduction in surface hydrophobicity. The findings also revealed that RA enhanced the emulsifying activity, emulsion stability, foaming ability and foaming stability of EWP. Furthermore, the storage performance of EWP improved after conjugation with RA. In conclusion, the covalent conjugation of EWP with RA not only diminished its allergenic potential but also improved its functional properties through structural modification. This study posits that such an approach could be an effective strategy for enhancing the functional properties of EWP while concurrently mitigating its allergenic potential, thereby offering promising applications in the formulation of future food products.

Effects of mixing ratio on physicochemical, structural properties and application in lycopene-loaded emulsions of blends of whey protein and pea protein

Physicochemical, structural properties and application in lycopene-loaded emulsions of blends of whey protein isolate (WPI) and pea protein isolate (PPI) at varying mass ratios (100/0, 75/25, 50/50, 25/75, 0/100) were investigated. Data indicated that the mass ratios affected the physical, chemical and storage stability of the emulsion by influencing the particle size, zeta-potential, surface hydrophobicity, free sulfhydryl content, and secondary structure of the blends. Particularly, emulsion with a mixing ratio of 75/25 exhibited superior physical stability against salt concentrations (200 and 500 mM), better chemical stability against UV light and heat, and maintained stability over a 30-day storage period. Emulsions stabilized by blends of different ratios exhibited similar digestion behavior, with no significant differences observed in lycopene's transformation stability and bio-accessibility. Data indicated that substitution of whey protein by pea protein is effective in term of emulsifier application and replacement ratio is an important factor need to be considered.

Insight into konjac glucomannan-retarding deterioration of steamed bread during frozen storage: Quality characteristics, water status, multi-scale structure, and flavor compounds

Konjac glucomannan (KGM), a water-soluble hydrocolloid, holds considerable potential in the food industry, especially for improving the quality and nutritional properties of frozen products. This study explored the alleviative effect of KGM on the quality characteristics, water status, multi-scale structure, and flavor compounds of steamed bread throughout frozen storage. KGM significantly improved the quality of steamed bread by slowing down the decrease in water content and the increase in water migration while maintaining softness and taste during frozen storage. Notably, KGM also delayed amylopectin retrogradation and starch recrystallization, thus preserving the texture and structure of the steamed bread. At week 3, the microstructure of the steamed bread with 1.0 % KGM remained intact, with the lowest free sulfhydryl content. Additionally, heat map analysis revealed that KGM contributed to flavor retention in steamed bread frozen for 3 weeks. These results indicate that KGM holds promise as an effective cryoprotectant for improving the quality of frozen steamed bread.

Modification of soybean protein isolate by pH-shifting combined with ultrasonic treatment: Structural, viscosity, and functional properties

In order to reduce the viscosity of soybean protein isolate (SPI) and improve its processing suitability, this study investigated the impact of pH-shifting and ultrasonic treatments on the structure, viscosity and functional properties of SPI. The results indicated that both without and with ultrasonication, the pH-shifting, especially the treatment of alkaline pH-shifting decreased α-helix and β-sheet contents and particle size of SPI, while increased its β-turn and random coil contents, fluorescence intensity, surface hydrophobicity and free sulfhydryl content. The alkaline pH-shifting combined with ultrasonic treatments reduced the viscosity of SPI from 98.97 mPa.s to 22.83 mPa.s. These structural changes endowed SPI with higher solubility (from 81.13 % to 91.53 %), and better emulsifying and foaming properties. Moreover, principal component analysis (PCA) was employed to visualise the influences of pH-shifting and ultrasonic treatments on SPI, confirmed that the structural changes of SPI were correlated with its viscosity and functional properties. These results have important implications for promoting the application of SPI in fluid food.

Effect of ultrasound-assisted pH-shifting treatment on the physicochemical properties of melon seed protein

Melon seeds have received considerable attention in recent years because of their high protein content, but they have not yet been fully used. The modification of melon seed protein (MSP) using ultrasound-assisted pH-shifting treatment was investigated in this study by analyzing structural characteristics and functional properties. The particle size, free sulfhydryl content, surface hydrophobicity, solubility, secondary structure, water-holding capacity, oil-holding capacity, emulsification activity index, and emulsification stability index of MSP were determined. MSP treated with ultrasound-assisted, pH-shifting had a smaller particle size, lower free sulfhydryl content, higher surface hydrophobicity, and solubility increased from 43.67 % to 89.12 %. The secondary structure of MSP was affected by ultrasonic treatment, manifesting as an α-helix increase and β-helix, β-turn, and random coil content decrease, which may be the reason why the protein structure became more compact after treatment. The water and oil holding capacities of MSP increased from 2.74 g/g and 3.14 g/g in untreated samples to 3.19 g/g and 3.97 g/g for ultrasound-treated samples, and further increased to 3.97 g/g and 5.02 g/g for ultrasound-assisted, pH-shifting treatment at pH 9.0, respectively. The emulsification activity index of MSP was 21.11 m2/g before treatment and reached a maximum of 32.34 m2/g after ultrasound-assisted, pH-shifting treatment at pH 9.0. The emulsification stability of MSP was maximized by ultrasonic treatment at pH 7.0. Ultrasound-assisted, pH-shifting treatment can effectively improve the functional properties of MSP by modifying the protein structure, which improves the potential application of melon seed protein in the food industry.

The role of β‐glucanase in modifying dough characteristics, texture and in vitro starch digestibility of highland barley‐enriched bread

SummaryThis study aims to evaluate how β‐glucanase impacts dough characteristics, and the in vitro starch digestibility and quality of breads from mixed wheat and highland barley flour at different wheat/highland barley flour weight ratios (70/30 and 50/50). The results showed that β‐glucanase reduced the dough's viscoelasticity and enhanced its extensibility, softness, α‐helix (2.52%–16.12%), β‐sheet (11.10%–31.66%) and free sulfhydryl content (22.70%–34.49%). This helped to mitigate the negative effects of a high β‐glucan content on the wheat/highland barley dough (P &lt; 0.05). Moreover, β‐glucanase improved the specific volume (44.67%–56.56%) and springiness (5.56%–40.41%) as well as reduced the hardness of wheat/highland barley bread (7.50%–71.32%). Furthermore, as the higher content of slowly digestible starch (20.81%–30.84%) reduced the enzymatic rate (k value), β‐glucanase‐treated wheat/highland barley bread exhibited lower starch digestibility (66.17%–71.16%) than white bread (75.37%). Therefore, this study indicated that β‐glucanase played an offsetting role on highland barley bread while maintaining relatively low starch digestibility.

Study on the physicochemical and functional properties of glutinous rice protein modified by frozen ball milling

This study explored the influence of frozen ball milling on the physicochemical properties and functional characteristics of glutinous rice protein. After grinding glutinous rice protein at 0 min, 10 min, 20 min, 30 min and 40 min, physicochemical indexes showed that with the extension of milling time, the particle size of glutinous rice protein decreased significantly, the free sulfhydryl content increased first and then decreased, the surface hydrophobicity increased gradually, the α-helix content decreased first and then increased, the β-sheet content decreased gradually, and the secondary structure was transformed. However, the electrophoresis bands did not change obviously before and after frozen ball milling. Functional indexes showed that the solubility of glutinous rice protein increased first and then decreased after frozen ball milling. With the increase of the frozen ball milling time, the emulsification activity of glutinous rice protein tended to increase first and then decrease. The emulsifying stability of glutinous rice protein decreased after undergoing freezing and ball milling, showing a notable decrease from 21.25% before frozen ball milling to 8.42% after 40 min of ball milling. This indicates that frozen ball milling is an effective method for producing modified glutinous rice protein products with new structure and characteristics.

Effect of Dry Processing of Coconut Oil on the Structure and Physicochemical Properties of Coconut Isolate Proteins.

The effects of the dry processing of coconut oil on the amino acid composition, molecular weight, secondary structure, solubility, surface hydrophobicity, microstructure, total sulfhydryl and free sulfhydryl content, free amino acid content, thermal properties, and water-holding, oil-holding, foaming, and emulsifying properties of coconut isolate protein were investigated. The results showed that the dry processing altered the amino acid composition of coconut isolate proteins as well as resulted in fewer irregular structural regions and more homogeneous particle sizes, leading to an improvement in the thermal stability of the proteins. SDS-PAGE analysis showed that globular proteins located at ~34 kDa in coconut isolate proteins underwent slight degradation during the dry processing of coconut oil. The dry processing reduced the surface hydrophobicity, total and free sulfhydryl groups, solubility, and free amino acid content of coconut isolate proteins. In addition, the water-holding capacity, oil-holding capacity, and foam stability of coconut isolate proteins were improved to different degrees after the dry processing. Therefore, the development and utilization of copra meal protein is of great significance to increase its added value.

Peptide incorporation in frozen dough and steamed bread: Characteristics and structure-function relationship

Antarctic krill peptide (AKP), a bioactive compound, has garnered significant attention in recent years. This study aimed to explore the effects of varying levels of AKP addition (ranging from 0% to 2.0%, based on the flour, w/w) and different freezing time (0, 1, 2, 4, and 6 weeks) on the rheological properties, rheo-fermentation properties, water distribution, and microstructure of dough. The results revealed that the addition of AKP led to a reduction in the freezable water content, T2 relaxation time, and free sulfhydryl content of frozen dough. After 6 weeks of freezing, the viscoelastic properties of the dough with AKP were higher than those of the control. Additionally, the fermentation height of dough containing 1.5% AKP increased by 25.85% compared with the control, resulting in increased springiness and specific volume, and decreased hardness in the resulting steamed bread. Pearson correlation analysis showed a positive correlation between freezable water content and free sulfhydryl groups, while a negative correlation was observed with springiness. Furthermore, springiness showed a positive correlation with the DPPH free radical scavenging rate. These findings highlight the potential of AKP as a novel food cryoprotectant capable of significantly enhancing the quality and nutritional value of frozen wheat products.