紫苏籽中不同蛋白组分的功能性质研究

以紫苏籽为原料,经粉碎过60目筛后石油醚脱脂得到紫苏籽脱脂粉,然后采用不同方法提取得到紫苏籽分离蛋白、清蛋白和球蛋白,研究了3种蛋白的氨基酸组成及持水性、溶解性、乳化性等功能特性。结果表明:紫苏籽脱脂粉中蛋白质含量丰富,不同紫苏籽蛋白的氨基酸组成相近,其中谷氨酸含量最高,且均含有8种必需氨基酸;分离蛋白的热变性温度稍高于其他两种蛋白;清蛋白的持水性、持油性较好;在pH 1～10范围内,3种蛋白的溶解性均呈现出U型变化趋势,其中球蛋白的溶解性最好;在不同pH下,球蛋白的乳化活性和乳化稳定性高于其他两种蛋白。     

Structure,physicochemical, and functional properties of protein isolates and major fractions from cumin (Cuminum cyminum) seeds

In this study, cumin protein isolates (CPI) and major protein fractions were extracted and separated from cumin seeds, their structure, physicochemical, and functional properties were investigated. Albumin (62.29%) and glutelin (25.16%) were the predominant protein fractions of cumin seeds. Glutamic acid (Glu) and aspartic acid (Asp) were the major amino acids of cumin proteins, whereas more hydrophobic and aromatic amino acids were predominantly found in chickpea protein isolates. Electrophoresis profiles indicated that CPI have more disulphide bonds than major protein fractions. The intrinsic fluorescence data revealed that glutelin displayed greater exposure of tyrosine (Tyr) and tryptophan (Trp) residues compared to albumin and CPI. Circular dichroism (CD) data showed CPI presented more α-helix (14.4%) and less β-strand (30.7%) than albumin and glutelin. The atomic force microscope (AFM) profile and hydrodynamic diameter (D_h) determination showed the presence of low particle size in albumin fractions. Differences in the hydrophobicity (H_o) and the zeta-potential (ζ) of CPI, albumin, and glutelin were also observed due to their difference in structure and amino acid composition. Compared with CPI and glutelin, albumin exhibited the highest emulsifying activity (103.67 m²/g) and stability (42.84 min) and the smallest emulsion particle size (4.29 μm). The CPI, albumin and glutelin presented typical U-shaped protein solubility–pH curves, with the lowest solubility at pH 4.0. Rheological investigation demonstrated that CPIs were efficient in forming a gel at 80.6°C, whereas glutelin could form the hardest gel at 92.6°C. The overall results suggested that the cumin proteins can be a promising protein source for the food industry.     

Functional properties of hydrolysates from Phaseolus lunatus seeds

Use of low degree of hydrolysis (DH < 10%) with enzymatic treatment can produce protein hydrolysates with functional properties superior to the raw material. Suspensions of Phaseolus lunatus protein isolate (PPI) were treated with one of two commercial enzymes (Alcalase or Flavourzyme) at 50 °C and pH 8.0. DH with Alcalase was greater than Flavourzyme at 5 or 15 min of reaction. Alcalase-prepared hydrolysates had more peptides than those prepared with Flavourzyme. All the hydrolysates had higher solubility than the PPI, the highest being for the Alcalase-prepared hydrolysate at 15 min reaction time. Overall, the Alcalase-prepared hydrolysates had better solubility characteristics, whereas the Flavourzyme-prepared hydrolysates had better film properties (maximum emulsifying capacity and the highest foam formation values). This is probably because of the greater ease of movement toward the interface as shown by their high surface hydrophobicity values. The Alcalase-prepared hydrolysates had generally low or nonexistent film properties.     

Antioxidant properties of extracts from Ginkgo biloba leaves in meatballs

The aim was to determine the effect of Ginkgo leaf extracts on the stability of lipids and cholesterol in pork meatballs over 21 days of refrigerated storage. The antioxidants used were characterized by their antioxidant activity towards lipids and cholesterol. Extracts were prepared from green and yellow leaves from Ginkgo biloba L. trees. Water, acetone and ethanol were used as extractants. The extracts showed stabilizing effects on both lipid and cholesterol oxidation processes. The lipid oxidation process of pork meatballs was mostly inhibited by the aqueous and ethanolic extracts of the yellow leaves. Their antioxidant activity was higher than that of BHT. All the extracts had a stabilizing effect on cholesterol and most of them inhibited the formation of oxidized derivatives. The acetone and ethanol extracts of green leaves and the ethanol extract of yellow leaves inhibited the formation of cholesterol oxidation products formation most effectively.     

Functional properties of protein hydrolysates from pea (Pisum sativum,L) seeds

The aim of this study was to investigate the effects of partial enzymatic hydrolysis on functional properties of two different pea protein isolates obtained from two pea genotypes, Maja and L1. Papain and commercial protease (Streptomyces griseus protease) were used for protein modification. Solubility, emulsifying and foaming properties were estimated at four different pH values (3.0, 5.0, 7.0 and 8.0). Papain increased solubility of L1 pea protein isolate at pH 3.0, 5.0 and 8.0, emulsifying properties and foaming capacity at all pH values. Otherwise, papain increased solubility of Maja pea protein isolate only at pH 8.0. This pea protein isolate modified with both enzymes formed emulsions with improved stability at lower pH (3.0, 5.0). The commercial protease‐prepared pea protein isolates showed generally low solubility and different emulsifying and foaming properties. Proper selection of enzyme, conditions of hydrolysis and genotypes could result in production of pea protein isolates with desirable functional properties.     

白木通籽分离蛋白的理化与功能性质研究

以白木通籽为原料,采用碱提酸沉法,制备白木通籽分离蛋白（API）,并对其理化性质与功能性质进行了分析。结果表明:白木通籽分离蛋白含17种氨基酸,其中谷氨酸和天门冬氨酸的含量相对较高,有贮藏蛋白的共性。苏氨酸为白木通籽分离蛋白的第一限制性氨基酸。通过SDS-PAGE分析,白木通籽分离蛋白的亚基分子量范围为25～35ku。圆二色性光谱分析表明,白木通籽分离蛋白的二级结构主要由β-折叠和无规则卷曲组成,含量分别为31.2%和36.6%。白木通籽分离蛋白的等电点在pH4～5之间,在此pH范围内,蛋白的溶解性和起泡能力均最低。      

Characterization of hyacinth bean (Lablab purpureus (L.) sweet) seeds from Indonesia and their protein isolate

Hyacinth bean (Lablab purpureus (L.) sweet) seeds from Indonesia were characterized for the purposes of usage as a protein source. Protein isolate was prepared from the seeds using an isoelectric method, which was also used to characterize the physicochemical and functional properties. Hyacinth bean seeds have a moderate concentration of protein (17.1 ± 1.5%), and low concentration of HCN (1.1 ± 0.1 mg/100 g). However, before using the seeds as food, some treatments are needed to reduce their anti-nutritional factors, since the contents of trypsin inhibitor and phytate are 0.15 ± 0.02 TIU/mg and 18.9 ± 0.2 mg/g, respectively. Using the isoelectric preparation, the yield of protein isolate was low (7.38 ± 0.2 g per 100 g of the seeds), but the protein isolate had good colour, neutral odour, high protein content (89.8 ± 0.82%), and low ash (2.97 ± 0.36%). The protein isolate also had good functional properties, such as solubility, foaming capacity, and emulsifying activity. However, the foaming and emulsifying stabilities were low.     

Comparative study of functional properties of commercial and membrane processed yellow pea protein isolates

Functional properties of commercial and membrane processed pea protein isolates (PPI) prepared from yellow peas were investigated. Four protein isolates were prepared from yellow pea flour using water and KCl extractions at 25 °C followed by ultrafiltration and diafiltration (UF and DF) at pHs of 7.5 and 7.5 or 6 respectively. Following assessment of compositional attributes; solubility, foaming, flow and dynamic rheology, emulsification ability and heat-induced textural and rheological properties of prepared PPIs and a commercially available PPI were tested and compared. Membrane purification of proteins resulted in 28% to 68% reduction in phytic acid and enhanced, comparatively, the tested functional properties. Solubility of membrane processed PPIs, at all tested pHs, was superior and the lowest foaming stability and apparent viscosity were associated with commercial PPI. Gelling temperatures of water and KCl extracted PPIs, DF treated at pH 6, trimmed down to 75.7 ± 0.63 °C and 81.6 ± 0.55 °C in contrast to that of commercial PPI at above 90 °C. Similarly, the formation of firm gels, after 1 h heating at 90 °C, was associated with membrane processed PPIs whereas commercial PPI did not develop any gel.     

Physicochemical and functional properties of albumin,globulin and glutelin fractions of green lentil seed

Defatted lentil seed flour proteins were separated into their constituent albumin (ALB), globulin (GLB) and glutelin (GLT) fractions followed by determination of their structural and functional properties. The GLB fraction demonstrated superior solubility (84%–100%) at acidic and alkaline pH values when compared to the lower values for ALB and GLT. Amino acid composition analysis showed lower contents of hydrophobic and sulphur-containing residues for GLB. However, GLB had the highest in vitro protein digestibility, which may be due to lower contents of rigid secondary structure fractions like the β-sheet and β-turns. In contrast, water and oil holding capacities as well as gelling ability were better for GLT and ALB than GLB. The GLT fraction formed very poor emulsions at pH 3 and 5 but emulsification was significantly (p < 0.05) improved (smaller oil droplets) at pH 7 and 9. Foaming capacity was strongest for GLB, especially at pH 5, 7 and 9 where increase in protein concentration had a negative effect on foam formation. Overall, the protein type and pH of the environment had stronger effects on emulsion and foaming properties than the protein concentration.     

Functional properties of pH-shifted protein isolates from bigeye snapper (Priacanthus tayenus) head by-product

The functional properties of pH-shifted protein isolates from bigeye snapper head were evaluated. Alkaline isolate showed a superior salt-solubility and gel forming ability to acid counterpart as indicated by a regular gel structure (i.e., imaged by scanning electron microscope) with higher gel strength and lower expressible drip (p < 0.05). Acid isolate exhibited higher surface hydrophobicity (p < 0.05) and thereby improved interfacial properties. Emulsifying activity index of acid isolate was lower than commercial whey protein and egg-white (p < 0.05) but its emulsion stability was better (p < 0.05). Both protein isolates had lower foamability than commercial proteins but their foam stability was not different (p > 0.05).     

Physicochemical and structural characterisation of protein isolate,globulin and albumin from soapnut seeds (Sapindus mukorossi Gaertn.)

The amino acid (AA) composition and physicochemical and conformational properties of protein isolate (SNPI), globulin (SNG) and albumin (SNA) fractions from soapnut seeds were evaluated. The essential AA of SNG, SNA and SNPI (except sulfur-containing AA) are sufficient for the FAO/WHO suggested requirements for 2–5 year old infants. SNG and SNPI showed similar electrophoresis patterns and AA compositions, the subunit of those proteins consisted of two polypeptides linked by disulfide bonds. In contrast, SNA showed a different AA compositions and SDS–PAGE pattern. Both SNG and SNPI presented a typical U-shape protein solubility (PS)–pH profile, SNA showed a completely different PS–pH profile, especially at pH 2.0–4.0. The near-UV circular dichroism (CD), differential scanning calorimetry (DSC) and tryptophan fluorescence spectra analyses indicated that the flexibility in tertiary conformations decreased in the order: SNA > SNPI > SNG, while soapnut proteins had a similar secondary conformation, with a highly ordered structure (the β-types), as evidenced by far-UV CD spectra.     

Functional properties of sonicated and non-sonicated extracted leaf protein concentrate from Diplazium esculentum

Leaf protein concentrate of edible fern Diplazium esculentum was extracted using sonication and non-sonication methods and its functional properties were evaluated. The leaf protein concentrate contained 34.28 and 9.89% protein for sonicated and non-sonicated extractions, respectively. Sonication yielded (36.36%) better emulsion activity over non-sonication (31.10%). Foaming capacity was also found better in sonication (7.27%) over non-sonication (6.99%), and oil absorption capacity also improved in sonication (7.55 g of oil/g) over its counterpart (7.41 g of oil/g). Contact angle experiments with the leaf protein concentrate evidenced the enhancement of more hydrophilicity of the sonicated sample. Thermal properties of the leaf protein concentrate with sonication evidenced more stability (55.58 and 95.95°C) over the non-sonicated (46.75 and 75.60°C). Fourier transform infrared spectral analysis with the leaf protein concentrate of Diplazium esculentum was used to assess the secondary structural data such as α-helix and β-sheets. The various percentages of secondary structures of protein in sonicated and non-sonicated samples were 49.06 and 69.16% for α-helix, 33.59% and 17.02% for β-sheet and 42.02 and 35.68% for turn, respectively. The results of the present investigation showed credible evidence to support that sonication method of extraction of leaf protein concentrate was better in terms of protein yield and functional properties as compared to the non-sonication. The sonicated extracted leaf protein concentrate has the potential for developing value added products.     

Functional properties of protein fractions obtained from commercial yellow field pea (Pisum sativum L.) seed protein isolate

Commercial pea protein isolate was separated into water-soluble (WS), salt-soluble (SS), alkaline-soluble (AS) and ethanol-soluble (ES) fractions. AS fraction was the most abundant, constituting about 87% of the proteins in PPI followed by WS, SS and ES fractions in decreasing order. ES fraction consistently formed emulsions with a narrow range of smaller oil droplet sizes (0.6–19 μm) at pH 4.0, 7.0 or 9.0 compared to a wider range of sizes for emulsions stabilised by WS, SS and AS fractions. Emulsions formed with ES fraction were also the most stable (p < 0.05) over the 3 h test period at all the pH values used in this work. The WS fraction had significantly highest (p < 0.05) protein solubility and foaming capacity at all the pH values when compared to solubility of PPI, SS, and ES. Except for AS and ES fractions, foaming capacities of the protein fractions were higher at pH 9.0 than at pH 4.0 or 7.0.     

长白山榛仁分离蛋白及其主要组分的功能性质研究

本文以长白山榛仁为原料,采用Osborne蛋白分级提取法得到纯度为72.32%、68.72%、40.60%的清蛋白(PAP),球蛋白(PGP)和谷蛋白(PLP),采用碱溶酸沉法得到纯度为90.31%的分离蛋白,对比分析四种蛋白的功能性质,结果显示:分离蛋白总巯基含量最高为6.71μmol/g,清蛋白暴露巯基和二硫键含量最高分别为2.28μmol/g和60.40μmol/g。四种蛋白起泡性和泡沫稳定性随p H增大趋势相反,在p H 5时,起泡性最低而泡沫稳定性最高,在偏酸或偏碱条件下,起泡性较好而泡沫稳定性皆较差。谷蛋白吸水性和吸油性均最高分别为3.40 m L/g和2.52 m L/g,清蛋白吸水性和吸油性最低分别为0.63 m L/g和1.79 m L/g。四种蛋白质的溶解性,乳化性以及乳化稳定性随p H变化趋势相似,在等电点时最低。清蛋白、球蛋白、谷蛋白和分离蛋白中必需氨基酸含量占总氨基酸含量的29.83%、32.14%、35.23%和30.32%,除蛋氨酸外均能满足FAO/WHO规定成人需要摄入量。     

Functional properties of protein concentrates and isolates produced from cashew (Anacardium occidentale L.) nut

Protein isolates and concentrates were obtained from defatted cashew nut powder by two methods: alkaline extraction-isoelectric precipitation (IP) and alkaline extraction-methanol precipitation (MP). The functional properties of cashew nut protein isolates, concentrates and powder were significantly different (p < 0.05). Cashew nut protein isolate (CNPI) had higher water and oil absorption capacities (2.20 ml/g and 4.42 ml/g, respectively), emulsifying stability index (447%), foam capacity and stability (45% and 55%, respectively), and least gelation capacity (13.5%) than cashew nut protein concentrate (CNPC), which was also higher than that of defatted cashew nut powder (DCNP). However, emulsifying activity index (12.45%) and bulk density (0.31) of CNPI were lower than that of CNPC, which were also lower than that of DCNP. The water solubility of CNPI (95%) and CNPC (95%) was not significantly different (p > 0.05) among the samples, but was significantly different (p < 0.05) from that of DCNP (75%). The CNPI, CNPC and DCNP showed decreasing solubility with decreasing pH, with the minimum solubility being observed at a pH range of 4.0–4.5, confirming the isoelectric point of cashew proteins. However, higher water solubility, emulsifying activity, and foaming property were observed at an alkaline pH than at an acidic pH in all samples.     

Microencapsulation properties of protein isolates from three selected Phaseolus legumes in comparison with soy protein isolate

The spray-drying microencapsulation properties of protein isolates from three selected Phaseolus legumes (kidney, red and mung beans; KPI, RPI and MPI), at a specific concentration (6 g/100 mL) and oil/protein ratio (1:1, w/w) were compared with soy protein isolate (SPI). The oil retention efficiency (RE), redispersion and dissolution behavior, as well as microstructure of the spray-dried powders were characterized. The influence of storage at 75% relative humidity for 7 days on these characteristics was also evaluated. The results indicated that the microencapsulation properties (except RE in the KPI case) of the three protein isolates were considerably poorer than SPI, though their emulsifying ability was even superior. The microencapsulating properties of these protein isolates were largely associated with their interfacial properties, especially the interfacial protein concentration. Among the three protein isolates, the spray-dried powders with KPI exhibited highest RE but least redispersion and/or dissolution behavior. The storage resulted in a severe loss of RE and ability to be redispersed and/or dissoluted, with much higher extent observed for the KPI powder. These results suggest that appropriate modifications, especially in interfacial properties, should be conducted on these proteins to warrant their application as wall materials in spray-drying microencapsulation.     

Extraction and characterization of chickpea (Cicer arietinum) albumin and globulin

ABSTRACT:  Albumin and globulin fractions of 1 Desi and 2 Kabuli varieties of chickpeas ( Cicer arietinum ) were extracted with water and salt solutions (K₂SO₄ and NaCl). The extractable yields and particularly the albumin-globulin ratio varied greatly with the extraction medium and chickpea variety. Depending on the procedure employed, albumin could be extracted as a major fraction of chickpea proteins. Higher levels of essential amino acids and sulfur containing amino acids were found in albumins than in globulins of all chickpeas investigated. The common structural characteristics of both Kabuli and Desi chickpea albumins and globulins were clearly identified by densitometric profiles of their sodium dodecyl sulfate polyacrylamide gel patterns. Albumins contained subunits with higher molecular weights than those of globulins. The in vitro digestibility of the chickpea proteins by papain, pepsin, chymotrypsin, and trypsin indicated that globulins were more susceptible to proteolytic hydrolysis.     

Characterization of protein isolates from different Indian chickpea (Cicer arietinum L.) cultivars

Protein isolates prepared by alkaline solubilization followed by isoelectric precipitation and freeze drying from desi (PBG-1, PDG-4, PDG-3, GL-769, and GPF-2) and kabuli (L-550) chickpea cultivars were evaluated for functional (water and oil absorption capacities, least gelation concentration, foaming capacity and stability) and thermal properties. Significant difference (P ? 0.05) in properties of kabuli and desi chickpea protein isolates was observed. Kabuli chickpea protein isolate showed significantly (P ? 0.05) higher ash (1.14%), protein (94.4%), L^∗, ΔE value, oil absorption capacity (OAC) and lower water absorption capacity (WAC) than their corresponding desi chickpea protein isolates. The solubility-pH profile of different protein isolates showed minimum solubility in the pH between 4.0 and 5.0 and two regions of maximum solubility at pH 2.5 and 7.0. Foaming capacity of all protein isolates increased with the increase in concentration. Kabuli chickpea protein isolate showed the highest foam stability (94.7%) after 120 min of storage. The thermal properties of protein isolates from different chickpea cultivars were studied by differential scanning calorimetry (DSC). Protein isolates from both the chickpea types differed significantly (P ? 0.05) in peak denaturation temperature (T_d) and heat of transition (ΔH). Kabuli type protein isolate exhibited lower T_d and ΔH value as compared to those from desi types. The interrelationships between characteristics of protein isolates showed a significant (P ? 0.05) negative correlation of T_d with protein content and OAC. It was also observed that cultivars with high fat content had high ΔH and lower WAC.     

Functional properties of protein isolates from soybeans stored under various conditions

Soybeans were stored under 88% relative humidity at 30 °C (adverse condition) for 8 months, under 55% relative humidity at 20 °C (mild condition), cold condition (4 °C), and an uncontrolled ambient garage for 12 months, respectively. Protein isolates were prepared from the soybeans stored under various conditions and periods, and their functional properties were characterized. The protein subunits of the isolates prepared under the adverse conditions were degraded slightly after 3 months, degraded significantly after 6 months, and almost all subunits were degraded completely after 8 months; the relative contents of the protein subunits markedly decreased at the 7th or 8th month and some even approached zero. The relative contents of the 7S and 11S fractions began to decrease markedly at the 5th or 6th month, and the 11S/7S ratios seemed to decrease after the initial 6 months, and then increased at the 7th and 8th month. The nitrogen solubility index (NSI), protein disperse index (PDI), emulsifying activity, emulsifying stability, texture index and thermal stability of soybean protein isolates decreased following the degradation of subunits. The functional properties of protein isolates prepared from the other three conditions (mild, cold and ambient) showed almost no significant changes for 12 months of storage when compared with those of the control.