Cross-Linking and Glucosamine Conjugation of Casein by Transglutaminase and the Emulsifying Property and Digestibility In Vitro of the Modified Product

Microbial transglutaminase was applied as a biocatalyst and glucosamine as an acyl acceptor to modify casein by cross-linking and glucosamine conjugation. Electrophoretic analysis revealed that transglutaminase-induced cross-linking and glucosamine conjugation occurred simultaneously during reaction, and some polymers of glycoproteins with higher molecular weights were formed in the modified casein product prepared. HPLC analysis demonstrated that about 1.2 mol of glucosamine was conjugated to 1 mol of casein, under the preparation conditions as follows: casein concentration of 3% (w/v), molar ratio of acyl donor in casein to glucosamine acceptor of 1:3, transglutaminase addition level of 10 U/g casein, reaction temperature of 37°C, and reaction time of 4 h. The evaluation results also showed that the surface hydrophobicity of the modified casein product decreased. The emulsifying activity index and emulsifying stability index of the modified casein product were 100.9 m²/g and 84.3%, about 12 and 20% higher than that of original casein. The digestibility in vitro of the modified casein product was the same as that of original casein or had an increase of 9.8%. Meanwhile, cross-linking of casein by transglutaminase in the absence of glucosamine showed adverse impact on the emulsifying properties of the cross-linked casein prepared. The new modification method developed might have the potential as an effective approach to improve the functional properties of food proteins.     

酪蛋白的转谷氨酰胺酶酶促糖基化交联条件及产物性质

在氨基葡萄糖存在的条件下,利用转谷氨酰胺酶(EC2.3.2.13)对酪蛋白进行糖基化交联修饰。以修饰酪蛋白产物中氨基葡萄糖的导入量为指标,采用单因素试验分别考察反应体系pH值、酶添加量、反应温度和时间对修饰反应的影响。优化后的适宜修饰条件为:酪蛋白底物质量浓度为30g/L,氨基葡萄糖添加量为3mol(每kg酪蛋白中)、pH值为7.5、酶添加量为10kU(每kg酪蛋白中)、反应温度为37℃、时间4h。与酪蛋白和转谷氨酰胺酶促交联的酪蛋白相比,修饰酪蛋白产物的乳化性质和胶凝性质得到显著改善,并且体外消化性能未受到影响,表明转谷氨酰胺酶催化的糖基化交联修饰可以用于改善酪蛋白的这些功能性质。     

Rheological,gelling and emulsifying properties of a glycosylated and cross‐linked caseinate generated by transglutaminase

The impacts of oligochitosan glycosylation and cross‐linking on some properties of a commercial caseinate were investigated in this study. The glycosylated and cross‐linked caseinate with glucosamine content of 4.74 g kg^?1 protein was generated by transglutaminase (TGase) and oligochitosan at pH 7.5 and 37 °C, with fixed substrate molar ratio of 1:3 (acyl donor to glucosamine acceptor), caseinate content of 50 g L^?1, TGase of 10 kU kg^?1 protein and reaction time of 3 h, respectively. In comparison with the caseinate, the glycosylated and cross‐linked caseinate had decreased reactable amino groups (0.58 vs. 0.51 mol kg^?1 protein), higher apparent viscosity, decreased emulsifying activity index (about 14.5%) and statistically unchanged emulsion stability index (92.6 vs. 90.5%). Based on the mechanical spectra of the acid‐induced gels, the glycosylated and cross‐linked caseinate showed shorter gelation time (95 vs. 200 or 220 min) than the caseinate or cross‐linked caseinate. The gels prepared from the glycosylated and cross‐linked caseinate also had enhanced hardness, springiness and cohesiveness. The results indicated that TGase‐mediated oligochitosan glycosylation and cross‐linking has the potential to obtain new protein ingredients.     

The preparation of an oligochitosan‐glycosylated and cross‐linked caseinate obtained by a microbial transglutaminase and its functional properties

A glycosylated and cross‐linked caseinate (GCC) with glucosamine amount of 4.74 g/kg protein was generated from caseinate and oligochitosan by a microbial transglutaminase. The applied temperature, pH and molar ratio of acyl donor/acceptor were 37 °C, 7.5 and 1:3, respectively; while caseinate concentration, transglutaminase addition and reaction time selected from single‐factor trials were 50 g/L, 10 kU/kg protein and 3 h, respectively. Electrophoretic analysis revealed the cross‐linking and glycosylation of caseinate. Compared with caseinate, GCC showed improved solubility in pH 4–11, higher digestibility in vitro and water binding capacity, about 3‐fold, but lower surface hydrophobicity and oil binding capacity (34%).     

Functional properties of milk proteins as affected by enzymatic oligomerisation

Milk proteins were enzymatically modified by transglutaminase, lactoperoxidase, laccase as well as glucose oxidase and analysed for changes in molar mass distribution, techno- and tropho-functional properties.The study revealed that high degrees of protein cross-linking were not only detected upon enzymatic modification of milk proteins by transglutaminase, but also upon incubation with oxidoreductases like lactoperoxidase, laccase as well as glucose oxidase. Due to different reaction mechanisms, oligomeric (20,000–200,000 g/mol) and polymeric (>200,000 g/mol) reaction products with different functional property profiles were synthesised. In contrast to transglutaminase-treated milk proteins, e.g., lactoperoxidase-treated milk proteins performed outstanding interfacial properties and glucose oxidase-treated milk proteins higher in vitro digestibility. Oxidoreductase-treated proteins were shown to exhibit increased antioxidative capacity. Laccase was demonstrated to generate oligomeric as well as polymeric protein/protein and protein/phenolic acid reaction products.The study characterises enzymatically cross-linked proteins and makes it possible to specifically select modified proteins for industrial applications according to the requirements towards food proteins, weighing changes in techno- and tropho-functional protein properties.     

Evaluation of microbial transglutaminase and ribose cross-linked soy protein isolate-based microcapsules containing fish oil

Soy protein isolate (SPI)-based microcapsules containing fish oil were prepared using a modified coacervation method followed by cross-linking treatments. The procedure yielded 95–98% microcapsules containing 0.5–0.6 g fish oil/g capsule with a volume mean diameter ranged from ~ 260 to ~ 280 μm. Four types of microcapsules produced were SPI with sucrose (MC-C/S), SPI with ribose (MC-C/R), SPI with sucrose and microbial transglutaminase (MC-MTG/S) and SPI with ribose and MTGase (MC-MTG/R). Protein cross-linking due to ε-(γ-glutamyl)lysine bonds and “Maillard cross-linking” were evidenced in the SDS-PAGE profiles of MC-C/R, MC-MTG/S and MC-MTG/R. Even though the microcapsules prepared with cross-linking treatments had significantly (P < 0.05) lower protein solubility as compared to that of the control, the results of fish oil release in pepsin solution at 37 °C indicated that the core release of all microcapsules prepared with ribose (MC-C/R and MC-MTG/R) was significantly (P < 0.05) lower than other microcapsules. During storage, microcapsules prepared with ribose had longer shelf life as compared to other microcapsules. This may be due to the release of antioxidative Maillard reaction products during heating and storage and a slower rate of gas permeability through the capsules.

Industrial relevance

The use of protein-based wall materials in the food industry for sensitive ingredients is limited because proteins are generally unstable with heating and damaged by organic solvents and the cross-linking agent is usually harmful. Therefore a novel method of combining two familiar cross-linking agents such as the microbial transglutaminase and ribose can convert SPI microcapsules into a stable form. The application of SPI in industry would be increased.     

TGase催化玉米醇溶蛋白糖基化改性

利用转谷氨酰胺酶（transglutaminase,TGase）催化玉米醇溶蛋白与氨基葡萄糖盐酸盐（glucosamine hydrochloride,GAH）发生交联反应。通过SDS-聚丙烯酰胺凝胶电泳确认玉米醇溶蛋白与GAH发生交联反应。以玉米醇溶蛋白糖基化修饰产物中GAH导入量为指标,优化糖基化反应条件,并对玉米醇溶蛋白糖基化修饰样品的溶解性进行了表征。结果表明,最适的糖基化反应条件为底物质量浓度5 g/100 mL、TGase添加量50 U/g（以玉米醇溶蛋白计）、玉米醇溶蛋白中酰基供体与GAH中的酰基受体物质的量比1∶6、初始pH 8.0、反应温度44 ℃、反应时间7 h;此反应条件下,玉米醇溶蛋白中GAH的最大导入量为（11.34±0.21） mg/g（以玉米醇溶蛋白计）。与玉米醇溶蛋白相比,玉米醇溶蛋白交联样品与糖基化修饰样品的溶解性均得到提高,玉米醇溶蛋白糖基化修饰样品的溶解性最高。     

Application and sensory evaluation of enzymatically texturised vegetable proteins in food models

Using simplified model systems, the effects of salts and oil on enzymatic texturisation of protein isolates from soy (Glycine max (L.) Merr.; SPI), pea (Pisum sativum L.; PPI) and sweet lupine (Lupinus albus L.; LPI) were evaluated. In aqueous systems, protein cross-linking by microbial transglutaminase (MTG) was significantly improved when NaCl (1–2 g hg⁻¹) was added, but respective doses of CaCl₂ reduced gel strengths. As shown by emulsion model systems of PPI and SPI with oil/protein ratios of 1 and 2 g g⁻¹, emulsification of corn oil into aqueous protein suspensions prior to enzymatic cross-linking enhanced gel formation depending on the emulsification technique. The impact of NaCl and oil varied among the protein isolates as to obtainable maximum gel strengths and optimum doses of these ingredients. The applicability of MTG to leguminous proteins in complex plant foodstuffs was finally deduced from their performance in complex food models of the liquid (thickened soup), foamed (mousse) and solid (sausage-like substitute) type, respectively. The sensory characteristics of the latter were evaluated by trained panellists relative to their milk-, gelatin- and meat-based counterparts. Texture was appealing in the foamed and solid food models, but the liquid soup model suffered from unfavourable grittiness. Without masking their beany off-flavour, the food models containing leguminous proteins deviated from the reference products. On the whole, MTG-catalysed cross-linking rendered the leguminous proteins suitable for the food applications in terms of visual appearance, texture and colour. Especially, the gels representing mousse-type foams and cuttable sausage-like vegetarian substitutes were very promising.     

Effect of processing parameters on the properties of transglutaminase-treated soy protein isolate films

The effects of processing parameters, including the applied amount of microbial transglutaminase (MTGase), the pH of film-forming solution, air-drying temperature, as well as the additional pre-incubation, on the properties of MTGase-treated soy protein isolate (SPI) films were investigated. The treatment with low concentration of MTGase (4–10 units per gram of SPI, U g^− 1) significantly increased the tensile strength (TS) values of SPI films, while high concentration of MTGase (over 20 U g^− 1) resulted in significant decrease in the TS values (P ≤ 0.05). The elongation at break (EB) values of corresponding films gradually decreased, and the contact angle values persistently increased with the enzyme concentration. At alkaline pH range, the TS and EB values of MTGase-treated SPI films were significantly higher than that at pH 7.0 (P ≤ 0.05). Meanwhile, the contact angle values significantly decreased with increasing pH from 7.0 to 10.0 (P ≤ 0.05). The TS, EB and contact angle values of MTGase-treated films gradually but insignificantly decreased with increasing the air-drying temperature from 18 to 50 °C (P > 0.05). The properties of MTGase-treated films were also affected by the additional pre-incubation of film-forming solutions with MTGase before casting. Furthermore, the aggregation of SPI or its components induced by MTGase has been proved to mainly account for the influence of processing parameters on the properties of SPI films (MTGase-treated). Thus, low concentration of enzyme, alkaline pH range and low air-drying temperature, at which conditions the MTGase-induced aggregation of SPI in film-forming solutions could be in some extent inhibited or delayed, might facilitate the improvement of the properties of SPI films by MTGase, especially the mechanical and surface hydrophobic properties.Industrial relevanceThe development of biodegradable protein film has attracted a lot of attention worldwide. The enzymatic cross-linking induced by transglutaminase has been confirmed to improve mechanical and surface hydrophobic properties of cast films from most of food proteins, including soy proteins. Results of this study show that, the improvement of properties of cast films of soy proteins by transglutaminase treatment is largely dependent upon many processing parameters, e.g., enzyme concentration, the pH of film-forming solution and temperature.     

Gelation Properties of Transglutaminase-Induced Soy Protein Isolate and Wheat Gluten Mixture with Ultrahigh Pressure Pretreatment

In this study, we elucidated the microbial transglutaminase-induced gelation properties and thermal gelling ability of soy protein isolate (SPI) and wheat gluten (WG) mixture following ultrahigh pressure (UHP, 100–400 MPa) pretreatment. UHP treatment induced unfolding and aggregation within SPI/WG protein molecules, which led to increases in free sulfhydryl group content and surface hydrophobicity. However, the transglutaminase cross-linking reaction facilitated the formation of hydrophobic interactions and disulfide bonds and thus resulted in higher gel strength, water holding capacity, and denser and more homogeneous gel networks of transglutaminase cross-linked SPI/WG gels. Rheological measurements revealed that the addition of UHP steps might generate a higher storage modulus (G′) value of MTGase-induced SPI/WG gelation during the heating-cooling cycle (25 °C → 95 °C → 25 °C). Our results indicated that various chemical interactions including covalent interactions (i.e., ε-(γ-glutamyl)lysine bonds and disulfide bonds) and non-covalent interactions (i.e., electrostatic forces and hydrophobic interactions) were involved in SPI/WG gel network structures. Hydrophobic interactions and disulfide bonds are significantly increased with the pressure level (100–400 MPa) compared with that of the unpressurized control. Furthermore, UHP treatment reduced the α-helix and β-turn content but increased the β-sheet and random coil structures. Thus, UHP treatment may be considered as a novel technique to expand the utilization of SPI/WG mixture in the food protein gelation industry.     

谷氨酰胺转移酶对大豆分离蛋白膜性能的影响

研究注模前酶作用时间对谷氨酰胺转移酶(TGase)改性大豆分离蛋白(SPI)膜性能的影响。在注模之前,将TGase(8U/g SPI)加入到成膜溶液中,分别在磁力搅拌下作用0、30、60、120min,然后注模成膜。利用质构仪检测蛋白膜的机械性能,结合哈克流变仪的动态黏弹实验及SDS-PAGE 实验进一步分析。注模前适度的酶作用(≤60min)在一定程度上有利于TGase 改性的SPI 膜机械强度的提高,特别是抗拉强度(TS)值;但是,时间不宜过长,因为注模前的酶作用也会诱导SPI 蛋白组分的聚沉反应,从而降低成膜溶液中可溶解蛋白的含量。结果表明,TGase改性SPI 膜时,一方面会诱导蛋白交联;另一方面,交联过多又会导致沉淀;在利用TGase 提高SPI 膜的机械性能时如何把握两者之间的关系,在交联的同时抑制酶促聚沉非常重要。     

转谷氨酰胺酶途径的酶法糖基化修饰在蛋白质/多肽改性中的研究进展

为了拓展蛋白质的应用范围,常对蛋白质进行改性,其中转谷氨酰胺酶(TGase)催化的酶法糖基化反应已应用于多种蛋白质/多肽的改性中。为了对蛋白质/多肽的酶法糖基化技术的广泛应用提供参考,简述了TGase的来源、催化的反应类型和底物类型,重点阐述了糖基化蛋白/多肽糖基化程度的评价方法以及修饰产物功能性质的变化。目前,TGase主要来源于微生物,其可催化底物的交联、酰基转移(酶法糖基化)和脱酰基3种类型的反应。在TGase催化的酶法糖基化反应中,常用RP-HPLC、邻苯二甲醛(OPA)法和3,5-二硝基水杨酸(DNS)法评价糖基化程度。通过酶法糖基化反应,可以不同程度地改善底物的溶解性、乳化性、热稳定性等功能性质。TGase催化的酶法糖基化反应还存在反应体系复杂、糖基化效率低等问题,需要进一步研究解决。     

酶法修饰对大豆分离蛋白凝胶性质影响的研究进展

大豆分离蛋白（soybean protein isolate,SPI）具有高营养性和良好的功能特性,但是,采用“碱溶酸沉”的传统方法所获得SPI往往会发生部分变性,最终常会以热力学稳定的水不溶性大聚集体和/或沉淀形式出现,对其凝胶性能产生不利影响。在实际生产中为改善SPI的凝胶性质,可进行物理、化学改性或酶法修饰,其中物理和化学改性反应特异性低,难以控制蛋白变性程度;而酶法修饰手段因具有反应条件温和、产品得率高、生产过程安全等特点得到广泛关注。本文综述了不同酶法修饰手段对SPI凝胶形成及性能的影响,通过描述SPI热凝胶和冷凝胶的形成机制,讨论限制性酶解、酶诱导的侧链接枝反应以及酶诱导的交联反应对SPI凝胶形成的影响,并对酶法修饰SPI凝胶的开发应用进行展望。     

酶法制备玉米七肽糖基化产物及其对促酒精代谢活性的影响

目的 对玉米七肽(Ser-Ser-Asn-Cys-Gln-Pro-Phe,SSNCQPF)进行糖基化制备和分离纯化,并对其进行乙醇脱氢酶(alcohol dehydrogenase,ADH)激活活性验证。方法 通过谷氨酰胺转氨酶(transglutaminase,TGase)介导,以玉米七肽作为酰基供体,D-氨基葡萄糖(D-glucosamine,GlcN)为酰基受体的糖基化反应,并分离纯化玉米糖肽单体——SSNCQ(GlcN)PF。使用超高效液相色谱-静电场轨道阱质谱仪(ultra performance liquid chromatography-quadrupole-exactive orbitrap mass spectrometry,UPLC-QE Orbitrap MS)进行面积归一化法测定糖肽纯度,采用核磁共振波谱仪(nuclear magnetic resonance,NMR)测定糖肽的氢谱(₁^{H NMR)}和碳谱(₁₃^{C NMR)},并结合二级质谱进行结构定性分析。最后用酶标仪(microplate reader spectrometry,MRS)对比测定玉米七肽及其糖肽的ADH激活活性,以验证玉米七肽糖基化修饰对其ADH激活活性的影响。结果 玉米糖肽经过分离、纯化和冻干后,使用液质联用仪测定其纯度达到99.11%,并且通过二级质谱、核磁氢谱和碳谱的分析,确定氨基葡萄糖连接在玉米七肽谷氨酰胺残基的氨基上。在摩尔浓度为2.5 mM时,糖肽的ADH激活率比玉米七肽高9.89%。结论 与玉米肽相比,采用TGase酶介导玉米七肽和氨基葡萄糖合成的糖肽,具有更高的促酒精代谢生物活性,为玉米肽糖基化在食品工业中的应用提供参考。     

Transglutaminase and tyrosinase as potential cross-linking tools for the improvement of rheological properties of gluten-free amadumbe dough

Gluten-free bread remains of poor quality despite efforts to amend gluten-free flours with ingredients such as hydrocolloids and proteins. Enzymatic modification of the proteins in dough may result in polymers that mimic gluten. This research investigated the effects of transglutaminase and tyrosinase on the rheological properties of amadumbe dough. Tyrosinase oxidation resulted in a 7.7–39.4% decrease in dough-free amine, and a 16.8–46.3% decrease in the dough thiol content as activity was increased from 0 to 80 U g⁻¹ flour. Transglutaminase treatment decreased the dough-free amino groups by 10–38.1% as activity was increased from 0 to 2 U g⁻¹ flour. Evidence of tyrosinase and transglutaminase-mediated cross-linking was provided by relevant model reactions monitored by mass spectrometry. An increase in dough G′ and G″ showed that both transglutaminase and tyrosinase improved dough viscoelasticity. The increase in the viscoelasticity of the dough potentially improves carbon dioxide retention during proofing.     

Gelling of microbial transglutaminase cross-linked soy protein in the presence of ribose and sucrose

Soy protein isolate (SPI) was incubated with microbial transglutaminase (MTGase) enzyme for 5 (SPI/MTG(5)) or 24 (SPI/MTG(24)) h at 40 °C and the cross-linked SPI obtained was freeze-dried, and heated with 2% (w/v) ribose (R) for 2 h at 95 °C to produce combined-treated gels. Longer incubation period resulted in more compact and less swollen SPI particle shape when reconstituted with sugar solution. Thus, this MTGase treatment affected samples in terms of flow behaviour and gelling capacity. Rheological study showed different gelling profiles with the cross-linking treatments and combined cross-linked SPI gave a higher G′ value compared to single treated samples. These are due to the formation of additional ε-(γ-glutamyl)lysine bonds and “Maillard cross-links” within the SPI protein network during the MTGase incubation and heating in the presence of ribose (i.e. reducing sugar). Network/non-network protein analysis found that network protein increased with cross-linking treatment, which also resulted in different SDS–PAGE profiles. As in non-network protein fraction, A₄ subunit was suggested to become part of the network protein as a result of combined cross-linking.     

乳铁蛋白-乳清分离蛋白乳状液微聚集体构建与酶交联对其流变学特性的影响

以乳清分离蛋白（whey protein isolate,WPI）与乳铁蛋白（lactoferrin,LF）乳状液形成微聚集体与转谷氨酰胺酶酶促交联微聚集体,以期提高体系流变特性。通过微射流分别制备WPI和LF乳状液,二者混合后,乳状液微滴之间发生异型聚集效应,通过转谷氨酰胺酶交联结合形成具有特定三维空间网络结构的微聚集体。研究结果表明：WPI与LF乳状液发生异型聚集,最大程度的聚集和最高物理稳定性体系发生在50% LF-50% WPI微滴形成的微聚集体。异型聚集效应改变了乳状液的流变特性,与单一WPI和LF乳状液相比,50% LF-50% WPI微聚集体流变学特性黏度值分别为单一乳状液的3.72?倍和2.2?倍,通过转谷氨酰胺酶交联,乳状液微聚集体的黏度值为原来的11.4?倍。因此,基于异型聚集效应结合酶促交联,可提高食品体系的流变特性,为开发食品脂质替代物提供了一定的理论支持。     

Susceptibility of an industrial α-lactalbumin concentrate to cross-linking by microbial transglutaminase

The susceptibility of an industrial α-lactalbumin concentrate to cross-linking with a microbial transglutaminase from Streptoverticillium mobaraense was investigated. At a protein concentration of 0.5% w v⁻¹, the maximum cross-linking was observed at 50°C, pH 5 and at 5 h of incubation time. Results from sodium dodecyl sulphate (SDS)-polyacrylamide gel electrophoresis showed that most of the monomeric form of α-lactalbumin was converted to polymers too large to move into the gel matrix. Addition of ethylenediamine tetraacetic acid or SDS prior to the incubation of protein–enzyme mixture, further enhanced the transglutaminase reaction with the industrial α-lactalbumin. Results from reverse phase chromatography indicated that cross-linking caused a broadening of the α-lactalbumin peak with little change in the average hydrophobicity of the protein. In contrast to the reported results on pure α-lactalbumin, the industrial α-lactalbumin concentrate showed considerable cross-linking with transglutaminase even without the reduction of the disulphide bonds. This difference was attributed to the partially unfolded secondary structures in the industrial α-lactalbumin concentrate.     

Effects of transglutaminase treatment on the thermal properties of soy protein isolates

The effects of covalent cross-linking of microbial transglutaminase (MTGase) on the thermal properties of soy protein isolates (SPI), including the thermal denaturation and glass transition were investigated by conventional and modulated differential scanning calorimetry (DSC). The MTGase treatment significantly increased the thermal denaturation temperatures (including the on-set temperature of denaturation, T_m and the peak temperature of denaturation, T_d) of glycinin and β-conglycinin components of SPI (P ⩽ 0.05), and the thermal pretreatment of SPI further increased the extent of this improvement. The MTGase treatment also improved the ability of SPI to resist the urea-induced denaturation. Modulated DSC analysis showed that there were two glass transition temperatures (T_g) in the reversible heat flow signals of native SPI (about 5% moisture content), approximately corresponding to 45 and 180 °C, respectively. These T_g values of SPI were significantly decreased by the MTGase treatment (at 37 °C for more than 2 h) (P ⩽ 0.05). The improvement in the hydration ability of protein and the formation of high molecular biopolymers may account for the changes of thermal properties of soy proteins caused by the MTGase cross-linking.     

干热处理下焦磷酸钠改性大豆蛋白乳化和起泡性质研究

研究了在80℃干热条件下焦磷酸钠改性大豆蛋白的乳化和起泡性质。研究发现:改性大豆蛋白的乳化性质和起泡性质得到明显的改善,蛋白质结合磷的量随干热处理时间的延长而增加。在干热处理前对大豆蛋白进行适度的预热处理大大提高了蛋白质结合磷的量,80℃预热处理10min使改性大豆蛋白表现出最好的乳化性质,而预热处理20min的改性蛋白质却表现出最好的起泡性质。红外光谱分析发现,焦磷酸钠以磷酸根的形式与蛋白质分子的游离羟基缩合。SDS-凝胶电泳表明,焦磷酸钠能抑制干热处理时大豆蛋白各亚基之间的聚合作用,从而提高其功能性质。该研究为大豆蛋白的改性提供了新的思路。