大豆蛋白水解产物中巯基的热稳定性和抗氧化作用的研究

研究了大豆蛋白水解产物中巯基的热稳定性及抗氧化作用。结果表明,SPI水解不影响巯基含量;加热时大豆蛋白溶液中巯基含量下降近52%,而大豆蛋白水解产物中巯基的含量只下降4%,说明大豆蛋白水解产物中巯基的热稳定性明显提高。当巯基被封闭时,大豆蛋白水解产物的抗氧化性明显减弱,说明巯基是大豆蛋白中很重要的抗氧化成分,但较其他一些抗氧化基团更易于氧化。     

抗坏血酸对大豆分离蛋白酶解产物功能特性影响研究

采用木瓜蛋白酶水解不同浓度的大豆分离蛋白,研究了抗坏血酸对较低水解度（DH为3.7%）和较高水解度（DH为8.9%）酶解产物黏度、发泡性、发泡稳定性、乳化性和乳化稳定性的影响.结果表明：在水解度为3.7%的、浓度为7%的大豆分离蛋白酶解液中添加0.3%抗坏血酸,体系的黏度最大、乳化性最强、乳化稳定性最高;在水解度为8.9%的、浓度为3%的大豆分离蛋白酶解液中添加0.3%抗坏血酸,体系的发泡性最大;在水解度为3.7%的、浓度为7%的大豆分离蛋白酶解液中添加0.5%抗坏血酸,体系的泡沫体积比最大.     

Gel-forming Ability and Radical-scavenging Activity of Soy Protein Hydrolysate Treated with Transglutaminase

ABSTRACT: Gel-forming ability and 1,1-diphenyl-2-picrydrazyl (DPPH) radical-scavenging activity of the peptic hydrolysate from soy protein isolate (SPI) were investigated. The gel-forming ability of mixtures consisted of SPI and its hydrolysate decreased as the percentage of hydrolysate increased. The inferior gel-forming ability of the hydrolysate was shown to be related to both the low surface hydrophobicity of the hydrolysate and the drop in sulfhydryl exchange reactions during gelation. Although antioxidants in the SPI-hydrolysate mixture (SHM) could be helpful in enhancing the radical-scavenging activity of the peptide-based gel, they suppressed the oxidization of sulfhydryls in sulfhydryl group/disulfide bond interaction. As a result of this, antioxidants present reduced the gel-forming ability of the SHM. The addition of transglutaminase (TGase) improved the gel-forming ability of SHM. A mixture of 70% SPI and 30% hydrolysate in the presence of TGase resulted in a gel with good gelling property and high radical-scavenging activity.     

葡聚糖接枝对大豆蛋白功能特性及结构的影响

采用干热糖基化对大豆分离蛋白进行改性,研究其功能特质及结构特性。以葡聚糖和大豆分离蛋白(soy protein isolate,SPI)为原料,考察底物质量比和反应时间两个因素。结果表明:蛋白质与糖质量比2∶1,反应温度60℃时,产物接枝比较高,褐变程度中等;与SPI相比,糖基化之后大豆蛋白的溶解度提高了72.72%,乳化活性(emulsifying activity,EAI)和乳化稳定性(emulsion stability,ESI)分别提高了117.53%和134.20%。十二烷基硫酸钠聚丙烯酰胺凝胶电泳(sodium dodecyl sulfate-polyacrylamide gel electrophoresis,SDS-PAGE)表明SPI与葡聚糖发生了糖基化反应;傅里叶红外光谱(Fourier transform infrared spectroscopy,FT-IR)和荧光光谱分析表明,糖链的引入导致了大豆蛋白空间结构的变化;模拟体外消化特性结果表明,葡聚糖糖基化修饰对SPI体外消化性的改善效果不明显。     

大豆分离蛋白美拉德反应研究进展

本文首先综述了美拉德反应对大豆分离蛋白的溶解性、乳化性以及凝胶性等一系列功能特性的影响,进而阐述了美拉德反应对大豆分离蛋白生物活性的影响,如抗氧化性和抗菌性。最后对大豆分离蛋白的美拉德反应在食品领域的研究进行了展望,以期对大豆分离蛋白的美拉德反应在食品领域的研究提供参考。     

酶解大豆分离蛋白乳化特性的研究

利用枯草芽孢杆菌AS1．398中性蛋白酶对大豆分离蛋白进行水解，并利用浊度法测定了不同水解度、不同pH条件下酶解大豆分离蛋白的乳化特性，结果表明：AS1．398蛋白酶对大豆分离蛋白的最大水解度为36％，水解度为9％时乳化活性最大，水解度为3％是乳化稳定性最好。同一水解度时，pH越高，蛋白质的乳化特性越好。水解度为3％、9％、15％的大豆分离蛋白在pH等于或高于5．0时的乳化活性明显地高于原蛋白质，且水解度为3％时乳化稳定性也明显地高于原蛋白质。     

大豆分离蛋白及其不同酶法水解产物对植脂末乳化稳定性的影响

为研究大豆分离蛋白(SPI)及其不同酶法水解产物对植脂末乳化稳定性的影响,本文对蛋白电泳亚基组成、分子量分布、乳化活性和乳化稳定性、植脂末粉末以及乳液的微观结构、平均粒径、ζ-电位以及咖啡稳定性进行了测定。结果显示,采用胃蛋白酶水解保留了较多的7S和碱性亚基,产物的乳化性质最好,相比于SPI的乳化活性和乳化稳定性分别提高了22.7%和14.1%;而木瓜蛋白酶水解产物主要为小部分碱性亚基条带和大量的小分子肽,尽管产物乳化活性较SPI有所增加,但乳化稳定性相比于SPI下降了17.6%。植脂末粉末的扫描电子显微镜图和植脂末溶解后乳状液的共聚焦激光扫描显微镜图进一步证实了SPI胃蛋白酶水解产物制备的产品具有最好的乳化效果,咖啡稳定性结果显示,两种酶解物均可用于咖啡伴侣。三种蛋白的组成、乳化性、植脂末以及植脂末复溶后乳状液的微观结构说明酶解物中存在过多的小分子肽,则不利于乳化稳定性;酶解物中存在相对较多的7S蛋白和碱性亚基,则有助于形成更稳定的乳状液。     

湿热条件下大豆分离蛋白与葡萄糖、麦芽糖的美拉德反应

研究湿热条件下反应温度、反应时间及混合质量比对大豆分离蛋白（soybean protein isolate,SPI）与葡萄糖、麦芽糖之间美拉德反应的影响,并对所得美拉德反应产物的溶解性、乳化性、溶液pH值、电势、热性能、结构和分子质量的变化进行表征。结果表明,SPI与2?种还原糖发生美拉德反应的最适条件为按质量比4∶1混合后在80?℃条件下反应6?h。美拉德反应明显改善了SPI的溶解度,并且麦芽糖比葡萄糖对SPI的改性效果更佳;美拉德反应降低了SPI的乳化性,并对其ζ电势有一定影响,随着美拉德反应程度的增加,SPI的负电荷明显减少;美拉德反应会使SPI溶液的pH值降低;热稳定性分析表明美拉德反应降低了SPI的热稳定性;傅里叶变换红外光谱分析表明美拉德反应在SPI中引入了新的化学键;荧光分析表明美拉德反应增强了SPI的荧光强度;十二烷基硫酸钠-聚丙烯酰胺凝胶电泳测定表明美拉德反应导致了大分子物质的形成。     

Interaction and Functionality of Mixed Myofibrillar and Enzyme-hydrolyzed Soy Proteins

ABSTRACT Native and briefly heated (85 °C for 3 min) soy protein isolates (SPI) were partially hydrolyzed (4% DH) by Alcalase® and Flavourzyme™ before incorporation into a pork myofibril isolate (MPI) system. The hydrolysis of soy protein enhanced its interaction with MPI, leading to a decreased thermal stability of both soy and muscle proteins. Alcalase SPI hydrolysates, when compared with nonhydrolyzed SPI, improved viscoelastic properties and hardness of MPI gels, while Flavourzyme SPI hydrolysates had an adverse effect. Hydrolyzed SPI augmented emulsifying properties of MPI; the specific efficacy depended upon the type of enzymes used, the SPI:MPI ratio, and whether SPI was heated before hydrolysis.     

Improvement of functional properties of acid-precipitated soy protein by the attachment of dextran through Maillard reaction

The functional acid-precipitated soy protein (SAPP)–dextran conjugate was prepared by dry-heated storage at 60 °C under 79% relative humidity (RH) for 5 days through Maillard reaction between the ε-amino of lysine in soy proteins and the reducing-end carbonyl residue in the dextran. The covalent attachment of dextran to SAPP was confirmed by SDS-polyacrylamide gel electrophoresis and gel filtration chromatography. Functional properties of soy protein depend on the structural and aggregation characteristics of their major components (storage globulins 7S and 11S). The conjugate seemed to be predominantly formed by 7S, and the acidic subunits of 11S in soy protein. The emulsifying properties of the SAPP–dextran conjugate were about four times higher than those of SAPP. The solubility of the protein was not enhanced as a result of preheating, but rather it was not decreased when the conjugated protein was heated at 90 °C for 20 min due to the presence of the polysaccharide. The excellent emulsifying properties of SAPP–dextran conjugate were maintained even at pH 3.0 and were further improved at pH 10.0. The object of Maillard reaction is to guarantee the suitable reaction degree, and the resulting soluble conjugate can have excellent emulsifying properties.     

干法糖基化改性提高大豆分离蛋白的乳化性

在干热条件下,大豆分离蛋白与葡聚糖两种大分子通过Maillard反应进行共价键合,以共价物的乳化活性为指标,确定影响糖基化蛋白乳化活性的因素依次为:反应温度＞反应时间＞pH＞底物配比,最佳工艺条件为:反应温度70℃,反应时间24 h,糖-蛋白(2:1),pH 8.0.以共价物的乳化稳定性为指标,确定了影响糖基化蛋白乳化稳定性的因素依次为:底物配比＞反应时间＞反应温度＞pH.最佳工艺条件为:糖-蛋白(3:1),反应时间24 h,反应温度70℃,pH8.0.通过聚丙烯酰胺凝胶电泳验证了大豆分离蛋白与葡聚糖发生了接枝反应.     

Comparative studies on the physicochemical properties of soy protein isolate-maltodextrin and soy protein isolate-gum acacia conjugate prepared through Maillard reaction

Dry-heated Maillard reaction was applied in the preparation of protein–polysaccharide conjugates. Reaction mixtures containing soy protein isolate (SPI) and maltodextrin (1:1 weight ratio) were dry-heated at 60 °C and 79% relative humidity for three days. The mixtures of SPI and gum acacia (GA) were dry-heated at the same condition for one week. The conjugate of SPI–MD showed lower levels of free amino groups and higher degree of graft, which indicated that reaction between SPI and MD developed much faster than reaction between SPI and GA. The solubility of SPI at isoelectric point was improved remarkably after grafting with MD or GA. The grafted SPI showed significantly higher levels of emulsifying properties than SPI and the emulsifying properties of SPI–GA conjugate were much better than SPI–MD. Decreases of lysine and arginine contents after the graft reaction indicated that these two amino acid residues attended the covalent linkage between SPI and MD or GA. The graft reaction reduced surface hydrophobicity and fluorescence emission maximum value because of a shielding effect of the polysaccharide chain bound to proteins. The results of secondary structure suggested that grafted SPI had decreased the levels of α-helix, β-sheet and β-turn and increased unordered coils level.     

大豆糖蛋白的抗氧化特性

大豆分离蛋白（soy protein isolate,SPI）与葡萄糖按质量比1∶1混合后通过美拉德反应生成大豆糖蛋白, 通过测定不同反应温度（70、80、90 ℃）、反应时间（0、1、2、3、4、5、6 h）大豆糖蛋白的还原能力、羟自由 基清除能力、1,1-二苯基-2-三硝基苯肼（1,1-diphenyl-2-picrylhydrazyl,DPPH）自由基清除能力、游离氨基含量、 褐变程度、紫外光谱扫描分析和十二烷基硫酸钠-聚丙烯酰氨凝胶电泳（sodium dodecyl sulfate-polyacrylamide gel electrophoresis,SDS-PAGE）等指标,探讨大豆糖蛋白的抗氧化性及其作用机理。结果表明：随着反应时间的延 长、反应温度的升高,大豆糖蛋白的抗氧化性越高、游离氨基含量下降越多、反应褐变程度越大,90 ℃、6 h制 得的大豆糖蛋白还原能力达到最高,比SPI还原能力高4.6 倍;90 ℃、5 h的大豆糖蛋白羟自由基清除能力最高,为 5.87%,是SPI羟自由基清除率的1.69 倍;同时在90 ℃、5 h制得的大豆糖蛋白还具有最高的DPPH自由基清除率,比 SPI提高了2.68 倍。由大豆糖蛋白的紫外光谱二阶导数分析可知,经过美拉德反应后蛋白中色氨酸发生偏移,而从 SDS-PAGE的分析中也看出蛋白质与糖发生聚合。因此,大豆蛋白葡萄糖反应生成的大豆糖蛋白具有很强的抗氧化 性,并且抗氧化性与蛋白结构的变化密切相关。     

Preparation,characterisation and selected functional properties of hydrolysed sodium caseinate–maltodextrin conjugate

Sodium caseinate was hydrolysed to a limited, moderate or extensive degree. The hydrolysates were conjugated with maltodextrin by a Maillard‐type reaction by dry‐heat treatment at 60 °C and 79% relative humidity for 2 or 4 days. Conjugates were characterised by SDS–PAGE and gel permeation chromatography. In comparison with the hydrolysates themselves, the conjugated hydrolysates had improved solubility, particularly around the isoelectric pH of the protein. The emulsifying properties of these conjugates were assessed in oil‐in‐water (o/w) emulsions; on emulsion formation, each conjugate‐stabilised emulsion had lower mean fat globule size than the corresponding hydrolysate‐stabilised emulsion. After storage for 7 days under accelerated shelf life testing conditions, the limited and moderate hydrolysate conjugate–stabilised emulsions had improved storage stability compared with hydrolysate‐stabilised emulsions; however, further research is required to optimise the hydrolysate fraction prior to conjugation for the production of novel low molecular weight emulsifiers.     

Modifications of soy protein isolates using combined extrusion pre-treatment and controlled enzymatic hydrolysis for improved emulsifying properties

Effects of combined extrusion pre-treatment and controlled enzymatic hydrolysis on the physico-chemical properties and emulsifying properties of soy protein isolates (SPI) have been investigated. Results showed that extrusion pre-treatment caused a marked improvement in the accessibility of SPI to enzymatic hydrolysis, resulting in changes in degree of hydrolysis (DH), protein solubility (PS), surface hydrophobicity (H₀) and molecular weight distributions (MWD) for ESPIH (extrusion pre-treated SPI hydrolysates). It was observed that emulsion systems formed by control SPI or SPIH (SPI hydrolysates) (20% v/v oil, 1.6% w/v emulsifier, and pH 7.0) were unstable over a quiescent storage period of 21 days, due to bridging flocculation and creaming. However, ESPIH (9.1% DH) was capable of producing a very fine emulsion (d₃₂ = 0.42 μm, d₄₃ = 2.01 μm) which remained stable over a long term quiescent storage. Various surface properties of ESPIH products have also been studied in relation to DH and emulsifying functionalities. It was suggested that significantly increased protein solubility and decreased molecular weight could be the main reasons for the greatly improved emulsifying capability of ESPIH. This study demonstrated that modified soy protein could be an excellent emulsifying agent for food and other applications. It also demonstrated that combined extrusion pre-treatment and enzymatic hydrolysis could be a highly effective method for functionality modification of globular proteins.     

高温短时干热法制备SPI-麦芽糊精糖基化产物及其乳化性的研究

采用高温(90,115和140℃)短时(2 h)干热法制备了大豆分离蛋白(SPI)-麦芽糊精(MD)糖基化产物。利用接枝度和SDS-PAGE研究了SPI与MD发生糖基化反应的程度。同时考察了SPI-MD糖基化产物稳定水包油乳液的性质,并探讨了盐离子和热处理对SPI-MD糖基化产物稳定乳液的储藏稳定性的影响。试验发现,提高反应温度能增大糖基化反应的接枝度,且pH 3.0时,与添加盐离子或经过热处理的SPI,SPI-MD糖基化产物(90℃)和SPI-MD糖基化产物(115℃)稳定乳液相比,添加盐离子或经过热处理的SPI-MD糖基化产物(140℃)的稳定的乳液具有较高的乳化稳定性和储藏稳定性。     

酸枣仁蛋白的不同蛋白酶酶解产物功能特性及抗氧化活性分析

以酸枣仁为原料,采用碱提酸沉法对酸枣仁蛋白进行提取,用三种不同蛋白酶(碱性蛋白酶、中性蛋白酶和木瓜蛋白酶)对酸枣仁蛋白进行酶解,得到三种酶解物,研究不同酸枣仁蛋白酶解物的功能特性和抗氧化活性.结果表明,与酸枣仁蛋白相比,不同酸枣仁蛋白酶解物的溶解性、持油性、起泡性及其稳定性、乳化性及其稳定性均具有不同程度地提高,其中,...     

超高压条件下大豆分离蛋白美拉德反应及乳化性质

本文研究超高压（High Hydrostatic Pressure,HHP）条件下,不同压力（0.1、100、200、300 MPa）在60 ℃时,对大豆分离蛋白（Soybean Protein Islates,SPI）与果糖（Fructose,Fru）美拉德反应产物的影响。以接枝度及乳化活性为指标,并分析最佳条件下所得产物以及产物乳状液的结构性质。结果表明在压力200 MPa、质量比0.8:1、反应时间24 h、溶液pH 8.0条件下,产物的乳化活性及乳化稳定性均有提升,乳化活性为(85.36±0.04) m2/g,是SPI与Fru混合物的1.71倍,是SPI的2.17倍,乳化稳定性为(27.66±0.03) min,是SPI与Fru混合物的1.15倍,是SPI的1.40倍。凝胶电泳图分析表明糖分子以共价键的形式接入到SPI分子中。圆二色谱图分析得知在200 MPa的条件下改性SPI二级结构发生改变,内源荧光光谱分析表明在200 MPa的压力可以使SPI的空间结构发生改变。粒径、电位和激光共聚焦显微镜微观图均可表明200 MPa的压力对蛋白乳状液稳定性的提升。     

大豆分离蛋白与麦芽糊精的Maillard反应性及产物乳化性质研究

以SDS-聚丙烯酰胺凝胶电泳和毛细管电泳研究了大豆分离蛋白-麦芽糊精的Maillard反应形成的共聚物。电泳分析表明:7S亚基与麦芽糊精的反应性较高,而且在文中所研究的蛋白质与多糖质量比的范围内,7S亚基都能与麦芽糊精发生定量的共聚合反应,形成分子特性高度一致的共聚物;而11S亚基与麦芽糊精间的反应性较低,共聚物的分子特性受蛋白质与多糖质量比的影响。共聚物在pH7.0和pH4.5时的乳化性能优于酪朊酸钠,尤其是在pH4.5时具有优良的乳化稳定性。但在较高NaCl浓度时的乳化活性与大豆分离蛋白相比没有明显的改善,其乳化稳定性则明显优于酪朊酸钠。     

大豆分离蛋白超声处理对其与木糖美拉德反应及产物乳化能力的影响

将大豆分离蛋白（soybean protein isolate,SPI）经过超声波预处理不同时间,然后与木糖（xylose,XYL）以质量比4∶1在湿热条件（90?℃、6?h）下发生美拉德反应制备美拉德产物（Maillard reaction products,MRPs）,并以此产物为乳化剂、大豆油为分散相制备乳状液,研究SPI超声处理对其与XYL美拉德反应及所得MRPs乳化能力的影响。结果表明：对SPI进行超声处理可以显著促进其与XYL之间的美拉德反应,并提高相应MRPs的Zeta电位、荧光强度及乳化能力。粒径分析和分层指数分析表明,与天然SPI相比,其经超声处理后再与XYL发生美拉德反应降低了相应MRPs稳定乳液在环境离子强度、加热及pH值发生变化时的聚集程度,但是对乳液的分层情况没有明显的改善作用。