木瓜蛋白酶控制水解蚕豆水溶性蛋白及水解度对蚕豆蛋白功能性质的影响

针对蚕豆蛋白在pH较低的体系中溶解性差、乳化能力低,制约其在食品工业中应用等问题,应用808Titrando瑞士万通全自动滴定仪控制木瓜蛋白酶水解蚕豆蛋白,实现蚕豆蛋白的有限水解,探讨水解度对蚕豆蛋白水解物的溶解性、乳化能力及持水性等功能性质的影响。通过木瓜蛋白酶的控制水解获得水解度为2%～4%的蚕豆蛋白水解物;与蚕豆蛋白相比,在pH4.0～6.0体系、水解度为4%的蚕豆蛋白水解物的溶解度提高2～3倍;pH6.0、水解度为2%的蚕豆蛋白水解物的乳化能力是蚕豆蛋白的2.3倍,持水力是蚕豆蛋白的1.6倍。     

Functional properties of bovine blood plasma intended for use as a functional ingredient in human food

With the aim of using bovine blood as functional ingredient in food processing, as an emulsifier or fat replacer, a study of some functional properties of blood plasma was made. The effect of pH (3.0–8.0), tryptic hydrolysis and NaCl addition (0.034 mol/L) on the solubility, hydrophobicity and emulsifying properties of bovine blood plasma were studied. The results showed that the hydrophobicity and emulsifying activity index (EAI) of bovine blood plasma reached a maximum at pH 3.0 and 7.0, respectively, while the other parameters stayed nearly constant with pH change. Tryptic hydrolysis improved hydrophobicity at certain hydrolysis times, reduced solubility and emulsifying capacity (EC) and showed no effect on EAI and emulsion stability (ES). The influence of NaCl tested at pH 5.0 and 6.0 was only positive for plasma EAI at pH 5.0 and significantly reduced solubility, hydrophobicity and EC at pH 5.0 and 6.0. For ES, NaCl addition did not produce any modification.     

碱性蛋白酶限制性酶解对蓝圆鲹分离蛋白功能特性的影响

以蓝圆鲹(Decapterus maruadsi)分离蛋白为原料,采用碱性蛋白酶对其进行限制性酶解,研究水解度(degree of hydrolysis,DH)对分离蛋白酶解产物溶解性、持油力、乳化性与起泡性等功能特性的影响.结果表明,碱性蛋白酶酶解产物的相对分子质量显著下降.酶解可有效提高分离蛋白的溶解性,其溶解度随...     

Functional properties of raw and heat processed cashew nut (Anacardium occidentale, L.) kernel protein isolates

The functional properties viz. solubility, water and oil absorption, emulsifying and foaming capacities of the protein isolates prepared from raw and heat processed cashew nut kernels were evaluated. Protein solubility vs. pH profile showed the isoelectric point at pH 5 for both isolates. The isolate prepared from raw cashew nuts showed superior solubility at and above isoelectric point pH. The water and oil absorption capacities of the proteins were slightly improved by heat treatment of cashew nut kernels. The emulsifying capacity of the isolates showed solubility dependent behavior and was better for raw cashew nut protein isolate at pH 5 and above. However, heat treated cashew nut protein isolate presented better foaming capacity at pH 7 and 8 but both isolates showed extremely low foam stability as compared to that of egg albumin.     

Effect of enzymatic hydrolysis on molecular weight distribution,techno-functional properties and sensory perception of pea protein isolates

Pea protein isolate (Pisum sativum “Navarro”) was hydrolyzed with 11 proteolytic enzymes at different hydrolysis times (15, 30, 60, and 120 min) to improve techno-functional and sensory properties. The degree of hydrolysis and changes within the molecular weight distribution were used as indicators for a reduced allergenic potential. The highest degree of hydrolysis was reached by Esperase hydrolysates (9.77%) after 120 min of hydrolysis, whereas Chymotrypsin hydrolysates showed the lowest (1.81%). Hydrolysis with Papain, Trypsin, Bromelain, Esperase, Savinase, and Alcalase suggested an effective degradation of the 72 kDa-convicilin fraction. Papain and Trypsin hydrolysates showed a degradation of the 50 kDa-mature vicilin after 15 min of hydrolysis. Most hydrolysates showed a significant increase in protein solubility at pH 4.5 at all times of hydrolysis. Trypsin hydrolysates showed the highest foaming (2271%) and emulsifying (719 mL/g) capacities. The bitterness of the hydrolysates was strongly correlated (P < 0.05) with the degree of hydrolysis. In general, enzymatic hydrolysis improved techno-functional properties indicating their potential usage as food ingredients.Industrial relevanceDue to their high protein content, peas are becoming an attractive ingredient for the food industry. However, pea protein isolates are often characterized by poor techno-functional and sensory properties. Enzymatic hydrolysis is known to change the molecular weight distribution of proteins. Consequently, the techno-functional and immunogenic properties might be altered selectively. In this study, enzymatic hydrolysis was applied, resulting in highly functional pea protein hydrolysates with a hypothesized reduction of main allergens. The lower bitter perception highlights their high potential as valuable functional food ingredients.     

Solubility and Foaming Properties of Phytate-Reduced Soy Protein Isolate

A pilot scale ion exchange process was developed to produce a 75 - 77% phytate-reduced soy protein isolate. The solubility and foaming properties of this isolate were compared to those of control and commercial soy protein isolates as a function of protein concentration (5 and 10%, w/v), pH (3, 6 and 9) and preheat temperature (25, 60 and 80°C). Phytate-reduced soy protein extract exhibited minimum solubility at pH 4.8 - 5.0, compared to 4.2 - 4.5 for control soy extract. Phytate-reduced soy protein isolate was most soluble and functional at pH values below its isoelectric point (pH 3), whereas control and commercial soy isolates were generally most soluble and functional at pH values above their isoelectric point (pH 6 and 9).     

Comparative study of potato protein concentrates extracted using ammonium sulfate and isoelectric precipitation

In this study, effects of NaCl concentrations (0.0, 0.2, 0.4, 0.6, 0.8, and 1.0 M) and pH (3.0, 5.0, 7.0, and 8.0) on the physico-chemical and functional properties of potato protein concentrates extracted from potato fruit juice (PFJ) using ammonium sulfate precipitation (ASP) and isoelectric precipitation (IEP) were investigated. The total polyphenol content of potato protein concentrates extracted by IEP (IEPP) was 2.5 times of that of potato protein concentrates extracted by ASP (ASPP), which resulted in the color of IEPP darker than that of ASPP. More protein fractions (74, 62, and 35 kDa) were found in IEPP compared to ASPP. ASPP exhibited higher solubility than IEPP. The emulsifying properties of ASPP and IEPP increased along with the increasing NaCl concentration. ASPP and IEPP showed the lowest emulsifying properties and foaming ability at pH 5.0. While the foaming stability of ASPP and IEPP achieved the maximum and minimum at pH 5.0, respectively. Two endothermic peaks were observed in ASPP at pH 3.0, 8.0, and higher NaCl concentration (≥0.6 M), while more than two endothermic peaks were observed in IEPP at all NaCl concentrations (0.2–1.0 M) and pH values (3.0, 5.0, 7.0, and 8.0). The glutamic acid concentration of ASPP and aspartic acid concentration of IEPP were the highest, while histidine was the lowest according to the amino acid profile of both ASPP and IEPP. In terms of an essential amino acid index with respect to a reference protein of FAO/WHO, the nutritional values of IEPP were higher than those of ASPP.     

Isolation and study of the functional properties of pea proteins

Proteins of pea seeds were isolated after defatting with hexane using alkaline (0.1 M sodium hydroxide) extraction and acid (HCl) precipitation. Concentrates were also prepared by hexane extraction and ethanolic extraction (pH = 5). Gross chemical composition amino acid content and functional properties (solubility profile, emulsifying – and foaming properties, water – and oil absorption) were studied. The results were compared with the same parameters of soy and lupin protein products. Although the majority of functional characteristics of isolates were lower in comparison to soy isolates, pea protein concentrate and isolate could be successfully used in bakery products for enrichment in protein and improvement of biological value. Their utilization as meat protein substitute in some Frankfurter type sausages is also possibly.     

Functional Properties of Hydrolysates from Proteolysis of Heat-denatured Whey Protein Isolate

Heat-denatured whey protein isolate was hydrolyzed with trypsin, α-chymotrypsin, Alcalase or Neutrase to 2.8, 4.3, 6.0 or 8.0% degree of hydrolysis. Hydrolysates were fractionated by ultrafiltration and freeze-dried. Protein content of retentates showed little variation but permeates differed with enzyme. Surface hydrophobicity increased with hydrolysis but was not linear except for α-chymotrypsin. Ultrafiltration increased solubility and the permeates and retentates had better solubility than hydrolysates. Retentates had higher emulsifying activity index than hydrolysates while permeates did not form stable emulsions. Permeates formed stable foams but hydrolysates and retentates showed poor foaming characteristics. Specificity of the enzyme, and degree of hydrolysis influenced the functional properties of the peptides. Fractions generated by trypsin, at all levels of hydrolysis generally had higher solubility, emulsifying properties and foaming properties. Permeates from Alcalase hydrolysis had the best foam capacity but low foam stability.     

Isolation and characterization of proteins from soymilk residue (okara)

Protein was extracted from okara at pH 9.0 and 80 °C for 30 min, giving a recovery of 53% protein. The extracted protein was isolated by isoelectric precipitation at pH 4.5, and the dried, defatted protein isolates (prepared at 25 and 80 °C) had over 80% protein.

The okara protein isolates have essential amino acid profiles similar to the FAO scoring pattern, and high in vitro protein digestibility, with methionine and cysteine as the limiting amino acids. Polyacrylamide gel electrophoresis in sodium dodecyl sulfate showed that okara protein isolates had a large quantity of high molecular weight components suggesting protein aggregation. Differential scanning calorimetry and hydrophobicity data suggested extensive protein unfolding in the okara products.

Okara protein isolates had lower solubility than a commercial soy protein isolate at both acidic and alkaline pH, probably due to protein aggregation. Other functional properties, including emulsifying, water and fat binding, and foaming properties, were found to be comparable to the commercial soy isolate.     

Effect of Partial Proteolysis and Succinylation on Functionality of Corn Germ Protein Isolate

Corn germ protein isolate (CGPI) was partially hydrolyzed with trypsin and pepsin and succinylated at three levels. Various functional and electrophoretic properties of the native and modified protein were determined. Water absorption and foaming properties of CGPI were Improved by partial hydrolysis with trypsin; emulsifying capacity and nitrogen solubility were reduced; oil absorption was increased only slightly. CGPI pepsin hydrolyzate has decreased oil absorption, nitrogen solubility and emulsifying capacity but improved foaming properties; water absorption was unchanged. Treatment of CGPI with succinic anhydride improved water and oil absorption, nitrogen solubility and foaming capacity but decreased emulsifying capacity; foam stability was unchanged. Succinylation retarded electropohoretic mobility while hydrolysis altered band intensities.     

A comparative study of the functional properties of amaranth and soybean globulin isolates

The functional properties of the amaranth globulin isolate were determined and compared to those of the well studied soybean globulin isolate. Functional properties investigated included protein solubility, heat coagulation, foaming and emulsifying activity and stabilities, as well as fat binding. Overall, the amaranth globulin isolate was found to have significantly higher solubility (p ⪇ 0.05) i.e., 9 times higher, and higher heat stability (p ⪇ 0.05) in the vicinity of its isoelectric point, pH 5–6, than the corresponding soybean globulin isolate. Between pH 3–9 the amaranth globulin isolate was found to have significantly higher (p ⪇ 0.05) foaming capacities and stabilities than the soybean isolate. Maximum foaming capacity for the amaranth globulin was determined to occur around its isoelectric point. The emulsifying activity of the amaranth globulin isolate was found to be significantly higher (p ⪇ 0.05) between pH 3–9 than the corresponding soybean globulin isolate. The most substantial difference between the two isolates was that the amaranth isolate showed maximal emulsifying activity and stability at pH 7.0. Little difference was observed in the fat absorption capacities between the two prepared isolates. Nutritionally, the amaranth globulin isolate was found to be of superior quality compared to the soybean globulin isolate due to its higher content of essential amino acids. Overall, the functional properties of the amaranth globulin isolate were much better than the soybean isolate especially in the vicinity of its isoelectric point, suggesting a potential advantage if used in various thermally processed food formulations that fall within this pH range; a range where more common isolates perform very poorly.     

Functional Properties of Acylated Pea Protein Isolates

Pea protein isolates were acylated with succinic and acetic anhydride at 1.0, 3.0, and 5.0 mmol anhydride/g protein. The chemically modified isolates showed increased emulsifying capacity, emulsion stability, foam capacity and stability, and water adsorption compared to untreated pea protein isolate. In general, the greater the extent of acylation, the greater the improvement in emulsification properties compared to the untreated protein isolate; however, improvement at greater than 3.0 mmol anhydride/g protein was slight. Acetylation at 3 mmol/g increased foam capacity to the greatest extent. Water adsorption was enhanced to the greatest extent in protein isolates acetylated at 5 mmol/g. Acylation lowered the isoelectric point of protein isolates compared to untreated isolate. In vitro enzyme hydrolysis of the protein isolates, as determined by a multienzyme system of trypsin, chymotrypsin and peptidase, was not impaired by acylation.     

Effects of limited enzymatic hydrolysis with trypsin on the functional properties of hemp (Cannabis sativa L.) protein isolate

Effects of limited enzymatic hydrolysis induced by trypsin on the physicochemical and functional properties of hemp (Cannabis sativa L.) protein isolate (HPI) were investigated. The enzymatic hydrolysis was confirmed by sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and size exclusion chromatography (SEC). SEC and differential scanning calorimetry (DSC) analyses confirmed the presence of aggregates in the corresponding hydrolysates (with the degree of hydrolysis of 2.3–6.7%). Functional properties, including protein solubility (PS), thermal properties, emulsifying and foaming properties, and water holding and fat adsorption capacities (WHC and FAC) were evaluated. The PS was remarkably improved by the limited enzymatic hydrolysis at all tested pH values. However, the enzymatic hydrolysis led to the marked decreases in emulsifying activity index, foaming capacity and foam stability, WHC and FAC. These decreases were to a great extent related to the presence of aggregates in the hydrolysates.     

鳙鱼鱼肉蛋白的酶解及其对功能性质的影响

为了改善鳙鱼鱼肉蛋白(BCMP)的功能性质以扩大其在食品工业中的应用,以鳙鱼为原料制备了鳙鱼鱼肉蛋白,并利用碱性蛋白酶Alcalase2.4L对其进行水解,得到了3种不同水解度(DH4.5%、DH9.0%、DH13.5%)的酶解物。研究了BCMP及其酶解物的功能性质,包括溶解性、持水性、持油性、乳化性、起泡性。结果表明,与原鳙鱼鱼肉蛋白相比,酶解物的功能性质除持油性以外均有不同程度的提高。此外,DH4.5%的酶解物乳化性和起泡性最高,过度水解(DH9.0%、DH13.5%)反而造成乳化性和起泡性下降。     

Effect of pH on phosphorylation of potato protein isolate

Potato protein isolate (PPI) was phosphorylated with sodium trimetaphosphate (STMP) at ambient temperature and various reaction pH (5.2, 6.2, 8.0 and 10.5) to improve the functional properties without impairing the nutritional availability. Changes in chemical composition (total and coagulable protein content, ash and minerals content and amino acid composition), functional properties (protein solubility index, emulsifying activity and foaming capacity, water and oil absorption capacity) and phosphorus were determined. The chemical composition and functional properties of phosphorylated potato protein isolate (PP-PPI) were significantly different (p < 0.05). The PP-PPI at pH 5.2 was characterised by the highest content of all amino acids, whereas, PP-PPI under alkaline conditions (pH 10.5) caused decrease in these compounds. PP-PPI at pH 8.0 had the highest oil absorption capacity, emulsion activity and foam capacity, whereas, PP-PPI at pH 10.5 had the highest WAC.     

Comparison between protein functional properties of two rice cultivars

The functional properties of proteins from a high-protein–content rice cultivar (Nutriar) were analyzed and compared with those from a usual Latin-American cultivar (El Paso 144). Isolates from brown and milled flours were prepared and their emulsifying, foaming, and hydration properties studied. The four isolates displayed a very low solubility within a wide range of moderate pH, but demonstrate a significantly higher solubility at extreme pHs (either high or low). Nutriar isolates had a significantly higher solubility and greater surface properties than El Paso 144 isolates. The Nutriar isolate from brown flour was more soluble at pH 9 than the other isolates and moreover showed the highest capacity for forming and stabilizing foams and emulsions. In contrast, the Nutriar isolate from milled rice exhibited a higher solubility and greater foaming properties at an acid pH. The surface properties and solubility were significantly correlated among the four samples. All four isolates exhibited good water-imbibition and water-holding capacities.     

pH-dependent emulsifying properties of pea [Pisum sativum (L.)] proteins

Emulsifying properties of two partially purified legumin and vicilin (PL and PV) and protein isolate (PPI) from dry pea seeds at various pH values (3.0, 5.0, 7.0 and 9.0) were investigated. The tested emulsion characteristics included droplet size, flocculation and coalescence indices (FI and CI), creaming index, as well as interfacial protein adsorption. Some physicochemical properties of these proteins, e.g., free sulfhydryl and disulfide bond contents, protein solubility (PS), surface hydrophobicity (H_o) and thermal stability (and denaturation), were also characterized. The results indicated that emulsifying ability and emulsion stability of various pea proteins considerably varied with the preparation process, protein composition and pH. Overall, all the pea proteins exhibited least emulsifying ability at pH 5.0 (around isoelectric point), and concomitantly, the resultant emulsions were most unstable against coalescence and creaming. The emulsifying ability of these proteins at pH 3.0 was generally better than that at neutral or alkali pH values, and among all the three proteins, PL exhibited highest emulsifying ability at this pH. The flocculated state and size of droplets in fresh emulsions did not directly affect stability of these emulsions against flocculation and coalescence (upon 24 h of storage), and even creaming (up to 7 days). Interestingly, the PL and PV exhibited much better creaming stability than PPI, at pH deviating from the pI. The emulsifying properties of these proteins were not only related to their PS and H_o, but also associated with the protein adsorption and nature (e.g., viscoelasticity) of interfacial protein films. These results can greatly extend the knowledge for understanding the emulsifying properties of pea proteins, especially the pH dependence of emulsion characteristics.     

Effects of succinylation and deamidation on functional properties of oat protein isolate

The effects of two different modification methods (deamidation and succinylation) on the functional properties (solubility, water- and oil-binding capacity, foaming capacity and stability, emulsion activity and stability) of oat protein isolates were evaluated. Protein isolates extracted from defatted oat flour at alkaline pH were acylated by 0.20 g/g of succinic anhydride. The protein isolate was also modified using a mild acidic treatment (HCl, 0.5 N). Succinylation and deamidation improved solubility and emulsifying activity of the native protein isolate. Foaming capacity of oat protein isolate increased after deamidation, whereas succinylation decreased it. The deamidated and succinylated proteins had lower foam and emulsion stabilities than had their native counterpart. Water- and oil-binding capacity, in both modified oat proteins, was higher than those of the native oat protein isolate.     

Study of Some Functional Properties of Casein: Effect of pH and Tryptic Hydrolysis

The trypsin was used to hydrolyze commercial casein at varied times and pH range. The functional properties studied were the emulsifying capacity (EC), the emulsifying activity index (EAI), and the emulsion stability (ES). The dispersed phase used was corn oil. The tryptic hydrolysis was beneficial to the solubility and EC of casein in practically all pH values and reaction times. In case of EAI, this same effect was less intense and was observed only in acid region (pH 3.0 to 5.0), while for ES the trypsin action was mainly deleterious in almost all pH range and reaction times.