Preparation and characterization of papain-modified sesame (Sesamum indicum L.) protein isolates

Defatted sesame meal ( approximately 40-50% protein content) is very important as a protein source for human consumption due to the presence of sulfur-containing amino acids, mainly methionine. Sesame protein isolate (SPI) is produced from dehulled, defatted sesame meal and used as a starting material to produce protein hydrolysate by papain. Protein solubility at different pH values, emulsifying properties in terms of emulsion activity index (EAI) and emulsion stability index (ESI), foaming properties in terms of foam capacity (FC) and foam stability (FS), and molecular weight distribution of the SPI hydrolysates were investigated. Within 10 min of hydrolysis, the maximum cleavage of peptide bonds occurred as observed from the degree of hydrolysis. Protein hydrolysates have better functional properties than the original SPI. Significant increase in protein solubility, EAI, and ESI were observed. The greatest increase in solubility was observed between pH 5.0 and 7.0. The molecular weight of the hydrolysates was also reduced significantly during hydrolysis. These improved functional properties of different protein hydrolysates would make them useful products, especially in the food, pharmaceutical, and related industries.     

Physicochemical and functional properties of buckwheat protein product

This study was conducted to compare the physicochemical and functional properties of buckwheat protein product (BWP), soy protein isolate (SPI), and casein. BWP was prepared from buckwheat flour by the method including alkaline extraction and isoelectric precipitation. The amino acid composition of BWP was very similar to that of buckwheat flour. The protein solubility (PS) of BWP was much greater than that of SPI at all pH levels (pH 2-10) but lower than that of casein at pH 7-10. The isoelectric point of BWP was around pH 4. The higher aromatic hydrophobicities (ARH) of BWP, SPI, and casein were obtained at lower pH levels (pH 2-3). The emulsifying stability (ES) of BWP was lower than those of SPI and casein at high pH levels (pH 7-10). At all pH levels, BWP formed a thin emulsion. Regression analysis showed that the ARH of BWP was significantly associated with the ES. Although the water holding capacity of BWP was quite lower than that of SPI, its fat absorption capacity was slightly higher than those of SPI and casein. These results indicated that the physicochemical properties of BWP were different from those of SPI or casein. Thus, BWP is a potential source of functional protein for possible food application.     

Properties of cast films from hemp (Cannabis sativa L.) and soy protein isolates. A comparative study

The properties of cast films from hemp protein isolate (HPI) including moisture content (MC) and total soluble mass (TSM), tensile strength (TS) and elongation at the break (EAB), and surface hydrophobicity were investigated and compared to those from soy protein isolate (SPI). The plasticizer (glycerol) level effect on these properties and the interactive force pattern for the film network formation were also evaluated. At some specific glycerol levels, HPI films had similar MC, much less TSM and EAB, and higher TS and surface hydrophobicity (support matrix side), as compared to SPI films. The TS of HPI and SPI films as a function of plasticizer level (in the range of 0.3-0.6 g/g of protein) were well fitted with the exponential equation with coefficient factors of 0.991 and 0.969, respectively. Unexpectedly, the surface hydrophobicity of HPI films (including air and support matrix sides) increased with increasing the glycerol level (from 0.3 to 0.6 g/g of protein). The analyses of protein solubility of film in various solvents and free sulfydryl group content showed that the disulfide bonds are the prominent interactive force in the HPI film network formation, while in the SPI case, besides the disulfide bonds, hydrogen bonds and hydrophobic interactions are also to a similar extent involved. The results suggest that hemp protein isolates have good potential to be applied to prepare protein film with some superior characteristics, e.g., low solubility and high surface hydrophobicity.     

Some nutritional and functional properties of defatted wheat germ protein

Defatted wheat germ protein (DWGP) was isolated by alkaline extraction at pH 9.5 and subsequent isoelectric precipitation at pH 4.0, and its nutritional and functional properties were studied. The results showed that the amino acid content of defatted wheat germ was as high as 26.793 g/100 g, and the contents of eight essential amino acids were all relatively high. The isoelectric point of DWGP was 4.0. When pH >6.0, the DWGP had high solubility with a nitrogen solubility index of 70%. The emulsifying activity and emulsifying stability of DWGP were similar to those of bovine serum albumin and a little higher than those of casein. DWGP had good foaming capacity, but its foaming stability (FS) was not very good. However, the FS of DWGP can be improved through physical, chemical, or enzymatic methods. Moreover, DWGP had excellent water retention (WR); especially at pH 8.0 and a temperature of 70 degrees C, the WR of DWGP was the highest at 229.4%. DWGP offers is a potential source of functional protein isolate for possible food applications.     

Study of some physicochemical and functional properties of quinoa (chenopodium quinoa willd) protein isolates

The amino acid composition and the physicochemical and functional properties of quinoa protein isolates were evaluated. Protein isolates were prepared from quinoa seed by alkaline solubilization (at pH 9, called Q9, and at pH 11, called Q11) followed by isoelectric precipitation and spray drying. Q9 and Q11 had high levels of essential amino acids, with high levels of lysine. Both isolates showed similar patterns in native/SDS-PAGE and SEM. The pH effect on fluorescence measurements showed decreasing fluorescence intensity and a shift in the maximum of emission of both isolates. Q9 showed an endotherm with a denaturation temperature of 98.1 degrees C and a denaturation enthalpy of 12.7 J/g, while Q11 showed no endotherm. The protein solubility of Q11 was lower than that of Q9 at pH above 5.0 but similar at the pH range 3.0-4.0. The water holding capacity (WHC) was similar in both isolates and was not affected by pH. The water imbibing capacity (WIC) was double for Q11 (3.5 mL of water/g isolate). Analysis of DSC, fluorescence, and solubility data suggests that there is apparently denaturation due to pH. Some differences were found that could be attributed to the extreme pH treatments in protein isolates and the nature of quinoa proteins. Q9 and Q11 can be used as a valuable source of nutrition for infants and children. Q9 may be used as an ingredient in nutritive beverages, and Q11 may be used as an ingredient in sauces, sausages, and soups.     

Yeast (Saccharomyces cerevisiae) protein concentrate: preparation, chemical composition, and nutritional and functional properties

The main objective of the present study was to compare the composition and functional and nutritional properties of whole yeast cells (WY) from an ethanol distillery with those of a phosphorylated protein concentrate (PPC) prepared from the same cells. Comparisons were also made of PPC with texturized soy protein (TSP) and soy protein isolate (SPI), both acquired in the local market. Yeast (Saccharomyces cerevisiae) is a rich source of protein, soluble fiber, and some minerals. Saturated fatty acids predominated over monounsaturated and polyunsaturated in both WY and PPC. The functional properties of PPC were similar to those of SPI and TSP. Both soy products and PPC replaced 20 or 40% chuck roll protein without affecting the emulsion properties of the meat products. Amino acid scoring was high for both WY and PPC; digestibility was higher (90%) for PPC and lower (68%) for WY. The protein nutritive value of PPC did not differ from that of casein and was significantly higher than that for WY.     

Porphyran as a functional modifier of a soybean protein isolate through conjugation by the Maillard reaction

Porphyran (Por) prepared from dried nori was applied as a functional modifier of a soybean protein isolate (SPI) to conjugate with SPI from defatted soybean by the Maillard reaction (79% relative humidity and 60 degrees C for 7 days). Two kinds of partially denatured conjugate (Conj 45 and Conj 63) were obtained from the reaction product by sequential extraction at pH 4.5 and pH 6.3, and the respective yield and weight ratios of the SPI and Por moieties were 8.4% and 1:1 for Conj 45 and 11.7% and 1:0.16 for Conj 63. Conj 63 demonstrated improved solubility between pH 5.0 and pH 8.0, while Conj 45 exhibited substantially complete solubility over the pH range of 2.0-8.0. Conj 63 showed more tolerance against digestion with pancreatin than SPI, whereas this was lost after denaturation. Conj 63 and Conj 45 both showed a markedly higher emulsion activity index and emulsion stability than SPI, even at pH 3.0; in particular, Conj 45 exhibited outstanding emulsifying ability. Conj 63 had about a two-fold higher calcium-binding ability than SPI, and Conj 63 and Conj 45 did not aggregate with added Ca2+ and Mg2+. It is believed that Por could be a valuable functional modifier of SPI for providing soybean protein-based liquid foods such as beverages by conjugation through the Maillard reaction.     

亚麻籽分离蛋白结构表征及其性能分析

为实现亚麻籽饼粕中分离蛋白的综合加工利用,该文以冷榨亚麻籽饼粕为原料,对其进行脱胶脱脂处理,采用超声辅助水提法分别提取亚麻籽分离蛋白和脱胶脱脂亚麻籽分离蛋白,并对理化性质、结构及功能特性进行分析比较。结果表明,冷榨亚麻籽饼粕和脱胶脱脂亚麻籽饼粕中蛋白质质量分数分别为37.52%±0.04%、37.47%±0.02%。采用十二烷基硫酸钠-聚丙烯酰胺凝胶电泳测定亚麻籽分离蛋白和脱胶脱脂亚麻籽分离蛋白的分子质量,显示10～55 kDa之间有明显谱带,其中水溶性低分子质量的白蛋白（10、14、15及17 kDa）和盐溶性高分子质量的球蛋白（30、33、35、40、45及55 kDa）谱带最为明显。氨基酸的种类各检测到17种,含有丰富的必需氨基酸和非必需氨基酸。傅里叶变换红外光谱测定的2种蛋白质的二级结构稳定性一般;由扫描电镜和X-射线衍射可知亚麻籽分离蛋白比脱胶脱脂亚麻籽分离蛋白的微观孔隙率低,结构中都较缺乏结晶度或有序排列。2种蛋白的两亲性与大豆分离蛋白相比,亲水/油特性突出,亲油性是大豆分离蛋白的2倍多。通过对不同pH（2～11）和盐离子浓度（0～1.25 mol/L）下溶解度、起泡性、泡沫稳定性、乳化活性及乳化稳定性的测定,显示两者具有良好的碱溶性,脱胶脱脂亚麻籽分离蛋白的起泡性、乳化活性及乳化稳定性均优于亚麻籽分离蛋白,而泡沫稳定性恰好相反,该研究结果有利于拓宽2种分离蛋白在健康食品领域中的应用前景,为食品中的应用提供有益参考和数据支撑。     

Solubilized wheat protein isolate: functional properties and potential food applications

Solubility, foaming capacity/stability, water holding and fat absorption capacities, and emulsifying capacity/stability of a solubilized wheat protein isolate (SWPI) were compared with those of commercial protein, that is, sodium caseinate (NaCAS), dried egg white (DEW), nonfat dry milk (NFDM), and soy protein isolate (SPI). SWPI was highly soluble at pH 6.5-8.5. Foaming capacity of SWPI was superior to those of SPI, NFDM, and DEW, and its foaming stability was similar to those of the commercial proteins. Foaming properties of SWPI were greatly improved in the presence of 0.5% (w/v) CaCl(2). Water holding capacity of SWPI was greater than that of NaCAS, NFDM, and DEW, whereas its fat absorption capacity was comparable to that of SPI, NaCAS, and DEW. SWPI exhibited emulsifying properties similar to those of SPI. SWPI was incorporated at 5, 10, 15, or 20% into ice cream, chocolate chip cookies, banana nut muffins, and hamburger patties. Products containing <5% SWPI were acceptable to consumers.     

Lipid oxidation in corn oil-in-water emulsions stabilized by casein,whey protein isolate,and soy protein isolate

Proteins can be used to produce cationic oil-in-water emulsion droplets at pH 3.0 that have high oxidative stability. This research investigated differences in the physical properties and oxidative stability of corn oil-in-water emulsions stabilized by casein, whey protein isolate (WPI), or soy protein isolate (SPI) at pH 3.0. Emulsions were prepared with 5% corn oil and 0.2-1.5% protein. Physically stable, monomodal emulsions were prepared with 1.5% casein, 1.0 or 1.5% SPI, and > or =0.5% WPI. The oxidative stability of the different protein-stabilized emulsions was in the order of casein > WPI > SPI as determined by monitoring both lipid hydroperoxide and headspace hexanal formation. The degree of positive charge on the protein-stabilized emulsion droplets was not the only factor involved in the inhibition of lipid oxidation because the charge of the emulsion droplets (WPI > casein > or = SPI) did not parallel oxidative stability. Other potential reasons for differences in oxidative stability of the protein-stabilized emulsions include differences in interfacial film thickness, protein chelating properties, and differences in free radical scavenging amino acids. This research shows that differences can be seen in the oxidative stability of protein-stabilized emulsions; however, further research is needed to determine the mechanisms for these differences.     

Flavor-protein binding: disulfide interchange reactions between ovalbumin and volatile disulfides

The irreversible binding of selected sulfur-containing flavor compounds to proteins was investigated in aqueous solutions containing ovalbumin and a mixture of disulfides (diethyl, dipropyl, dibutyl, diallyl, and 2-furfuryl methyl) using solid-phase micro-extraction (SPME). In systems which had not been heated, the recovery of disulfides from the headspace above the protein at the native pH (6.7) was similar to that from an aqueous blank. However, significant losses were observed when the pH of the solution was increased to 8.0. When the protein was denatured by heating, much greater losses were observed and some free thiols were produced. In similar heat-denatured systems at pH 2.0, no losses of disulfides were observed. Disulfides containing allyl or furfuryl groups were more reactive than saturated alkyl disulfides. Interchange reactions between protein sulfhydryl groups and the disulfides are believed to be responsible for the loss of the disulfides.     

Optimization of the enzymatic deamidation of soy protein by protein-glutaminase and its effect on the functional properties of the protein

The effects of enzymatic deamidation by protein-glutaminase (PG) on the functional properties of soy protein isolate (SPI) were studied. Conditions for the deamidation were evaluated by means of response surface methodology (RSM). Optimal conditions based on achieving a high degree of deamidation (DD) with a concurrently low degree of hydrolysis (DH) were 44 °C, enzyme:substrate ratio (E/S) of 40 U/g protein and pH 7.0. Under optimal conditions, both DD and DH increased over time. SDS-PAGE results indicated that lower molecular mass subunits were produced with increasing DD. Far-UV circular dichroism spectra revealed that the α-helix structure decreased with higher DD, while the β-sheet structure increased until 15 min of deamidation (32.9% DD), but then decreased at higher DD. The solubility of deamidated SPI was enhanced under both acidic and neutral conditions. SPI with higher DD showed better emulsifying properties and greater foaming capacity than SPI, while foaming stability was decreased. It is possible to modify and potentially improve the functional properties of SPI by enzymatic deamidation using PG.     

Quantitative analysis of cystine, methionine, lysine, and nine other amino acids by a single oxidation--4 hour hydrolysis method

The sulfur-containing amino acids cystine and methionine play important roles in animal, especially avian, nutrition. Because these sulfur-containing amino acids are destroyed to varying extents by 6N HCl hydrolysis, oxidation and hydrolysis of cystine to cysteic acid and methionine to methionine sulfone have been widely used for determination of cystine and methionine. Lysine is considered the next limiting amino acid after the sulfur amino acids in poultry nutrition; therefore, determination of the amino acid content of rations focuses first on these 3 amino acids. The objective of this investigation was to establish whether lysine and other amino acids could be accurately determined in proteinaceous materials which had undergone performic acid oxidation. To perform this evaluation, lysine was determined in a variety of protein-containing materials both with and without performic acid oxidation. Performic acid oxidation followed by 6N HCl hydrolysis at 145 degrees C for 4 h allows accurate measurement of 3 amino acids especially important to poultry nutrition, cystine, methionine, and lysine, in a single preoxidized hydrolysate; this method can be extended to another 9 protein amino acids.     

高场强超声-加热联用增强大豆分离蛋白冷凝胶凝胶特性

为探究高场强超声技术对大豆分离蛋白葡萄糖酸内酯冷凝胶性的影响,该研究将高场强超声技术与加热处理联用,对大豆蛋白进行预处理后形成冷凝胶。采用质构仪、圆二色谱、荧光色谱、扫描电镜、电泳、粒度仪等多种表征手段,比较了2种高场强超声-加热联用工艺对大豆分离蛋白冷凝胶凝胶性的影响,并推测其作用机理。研究发现:与传统加热预处理相比,2种高场强超声-加热联用预处理都能够显著(P0.05)增强大豆分离蛋白冷凝胶的持水性和凝胶强度。工艺一(20 k Hz,400 W下先超声0、2、4、10 min后加热20 min)制备的冷凝胶的凝胶强度与持水性随超声时间的增加逐步增加(凝胶强度由(5.83±0.31)g增加到(46.37±1.15)g;持水性由42.04%±1.59%增加到81.74%±6.22%),而工艺二(先加热20 min后超声0、2、4、10 min)制备的冷凝胶的凝胶强度与持水性在较短超声时间内(4 min内)迅速增加(凝胶强度由(5.83±0.31)g增加到(37.57±2.57)g;持水性由42.03%±1.85%增加到79.31%±3.00%)。与工艺一相比,工艺二能够在较短超声时间内增强大豆分离蛋白冷凝胶性的机理可能在于:工艺二的处理方式,大豆蛋白经过热处理后充分展开、变性,使超声作用能在较短的时间内对大豆分离蛋白的二级结构和三级结构明显改变,暴露更多疏水基团,增加疏水环境和表面疏水性,增强蛋白在溶液中的溶解性,并增强大豆蛋白分子间的静电相互作用,从而形成致密、均一的微观凝胶结构,增加凝胶的持水性和凝胶强度。研究结果可为高场强超声-加热联用技术在大豆加工领域中的应用提供参考。     

Preparation and functional properties of rice bran protein isolate

Rice bran protein isolate (RBPI) containing approximately 92.0% protein was prepared from unstabilized and defatted rice bran using phytase and xylanase. The yield of RBPI increased from 34% to 74.6% through the use of the enzymatic treatment. Nitrogen solubilities of RBPI were 53, 8, 62, 78, 82, and 80% at pHs 2.0, 4.0, 6.0, 8.0, 10.0, and 12.0, respectively. Differential scanning calorimetry showed that RBPI had denaturation temperature of 83.4 degrees C with low endotherm (0.96 J/g of protein). RBPI had similar foaming properties in comparison to egg white. But emulsifying properties of RBPI were significantly lower than those of bovine serum albumin. The result of amino acid analysis showed that RBPI had a similar profile of essential amino acid requirements for 2-5-year-old children in comparison to that of casein and soy protein isolate.     

Effect of enzymatic treatment of extracted sunflower proteins on solubility, amino acid composition, and surface activity

Industrial proteins from agriculture of either animal or vegetable origin, including their peptide derivatives, are of great importance, from the qualitative and quantitative point of view, in food formulations (emulsions and foams). A fundamental understanding of the physical, chemical, and functional properties of these proteins is essential if the performance of proteins in foods is to be improved and if underutilized proteins, such as plant proteins (and their hydrolysates and peptides derivatives), are to be increasingly used in traditional and new processed food products (safe, high-quality, health foods with good nutritional value). In this contribution we have determined the main physicochemical characteristics (solubility, composition, and analysis of amino acids) of a sunflower protein isolate (SPI) and its hydrolysates with low (5.62%), medium (23.5%), and high (46.3%) degrees of hydrolysis. The hydrolysates were obtained by enzymatic treatment with Alcalase 2.4 L for DH 5.62 and 23.5% and with Alcalase 2.4 L and Flavorzyme 1000 MG sequentially for DH 46.3%. The protein concentration dependence on surface pressure (surface pressure isotherm), a measure of the surface activity of the products (SPI and its hydrolysates), was obtained by tensiometry. We have observed that the degree of hydrolysis has an effect on solubility, composition, and content of the amino acids of the SPI and its hydrolysates. The superficial activity and the adsorption efficiency were also affected by the degree of hydrolysis.     

Effects of high hydrostatic pressure on some functional and nutritional properties of soy protein isolate for infant formula

The effects and mechanism of high hydrostatic pressure (HHP) on some functional and nutritional properties of soy protein isolate (SPI) for infant formula were investigated. Results indicated that solubility, water holding capacity, emulsification activity index, and foaming capacity were improved at lower pressure and time levels, whereas these properties declined at higher levels. However, the emulsification stability index dropped when the pressure increased and the foaming stability decreased with pressure and time levels rising. HHP-treated SPI gave better swallowing properties and in vitro digestibility than control. The hardness, adhesive force, and springiness of SPI gels increased with increaded pressure and elongated time, being lower than those of the control. Near UV circular dichroism spectra confirmed the alteration of tertiary and/or quaternary conformations caused by HHP. Sodiumdoecyl sulfate polyacrylamide gel electrophoresis results indicated that β-conglycinin was more pressure labile than glycinin, and high molecular weight subunits formed via disulfide linkage at higher treatment levels.     

Nonenzymatic browning reaction of essential amino acids: effect of pH on caramelization and Maillard reaction kinetics.

The interaction between glucose and essential amino acids at 100 degrees C at pH values ranging from 4.0 to 12.0 was investigated by monitoring the disappearance of glucose and amino acids as well as the appearance of brown color. Lysine was the most strongly destroyed amino acid, followed by threonine which induced very little additional browning as compared with that undergone by glucose. Around neutrality, the nonenzymatic browning followed pseudo-zero-order kinetics after a lag time, while the glucose and amino acid losses did not follow first-order kinetics at any of the pH values tested. Glucose was more strongly destroyed than all of the essential amino acids, the losses of which are really small at pH values lower than 9.0. However, glucose was less susceptible to thermal degradation in the presence of amino acids, especially at pH 8.0 with threonine and at pH 10.0 with lysine. The contribution of the caramelization reaction to the overall nonenzymatic browning above neutrality should lead to an overestimation of the Maillard reaction in foods.     

适宜含水率保持油茶籽贮藏品质

为了确定油茶籽贮藏适宜的含水率,研究了在4℃,不同含水率(7%、10%、13%、16%、20%)油茶籽贮藏期间的品质变化。结果表明,较低的含水率能较好保持油茶籽的贮藏特性及营养品质。其中,含水率为7%的油茶籽贮藏效果较好,但与10%处理效果差异不明显(P>0.05)。在整个贮藏期,含水率为7%时油茶籽可溶性蛋白下降了13.05 mg/g,油酸含量下降了2.38%,酸值、过氧化值等品质指标上升速率较慢,同时能较好保持β-谷甾醇和角鲨烯等生物活性成分;其次是10%的含水率处理。而含水率为20%的油茶籽贮藏期间可溶性蛋白下降较快,贮藏结束时为25.47 mg/g,油茶籽劣变严重,所提取的油样品质变差,营养物质含量较少,因此含水率20%的油茶籽不适宜长期贮藏。综合考虑油茶籽品质因素和处理成本,认为控制含水率在10%以下能较好保持油茶籽的贮藏品质。该研究可为科学合理地贮藏油茶籽提供参考。     

糖接枝处理改善大豆蛋白纤维聚集体泡沫稳定性

为了探究糖接枝对大豆蛋白纤维聚集行为和泡沫性质的影响,明确蛋白质结构与功能的关系,该研究以大豆蛋白(soy protein isolation,SPI)和乳糖(lactose)为原料,通过干热法制备糖接枝大豆蛋白(SPI-lactose conjugate,SPI-Lac),以及在酸性条件下加热诱导其形成纤维聚集体(p H值2.0),制备了一种糖接枝大豆蛋白纤维聚集体(SPI-lactose conjugate fibillar aggregates),并考察了糖接枝对大豆蛋白的纤维聚集行为及泡沫性质的影响。研究结果表明:大豆蛋白在酸性条件下(p H值2.0)经加热后会发生水解,同时水解产物不断聚集形成大分子的纤维聚集体。糖接枝导致大豆蛋白的水解速度下降,但荧光光强和粒径的结果表明糖接枝能增强纤维聚集能力。SPI-Lac在中性条件下的溶解度(p H值5.0—7.0)显著高于SPI(P0.05),且不同时间处理的SPI-Lac纤维聚集体均能改善SPI在酸性条件下的溶解度(p H值2.0—5.0)。此外,不同时间处理的SPI-Lac纤维聚集体在酸性条件下的起泡能力均高于SPI纤维聚集体。SPI和SPI-Lac纤维聚集体的形成会导致SPI起泡能力的下降,但是短时间酸热处理形成的纤维聚集体泡沫稳定性得到显著改善。因此,糖接枝结合短时间酸热处理制备的糖接枝大豆蛋白纤维聚集体在中性条件下的泡沫稳定性显著提高(P0.05),是合理有效的蛋白质改性方法。