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1.
In the present study emulsions were made with various potato protein preparations, which varied in protease inhibitor and patatin content. These emulsions were characterized with respect to average droplet size, plateau surface excess, and the occurrence of droplet aggregation. Droplet aggregation occurred only with potato protein preparations that contained a substantial amount of protease inhibitors and could be prevented only at pH 3. The average droplet size of the emulsions made with potato proteins appeared to be related to the patatin content of the preparation used. Average droplet size was found to be dominated by the patatin-catalyzed lipolytic release of surface active fatty acids and monoglycerides from the tricaprylin oil phase during the emulsification process. Addition of monoglycerides and especially fatty acids, at concentrations representative of those during emulsification, was shown to cause a stronger and much faster decrease of the interfacial tension than that with protein alone and to result in a drastic decrease in droplet size. The patatin used was shown to have a lipolytic activity of 820 units/g with emulsified tricaprylin as the substrate. Because of the droplet aggregating properties of the protease inhibitors, the patatin-rich potato preparations seem to be the most promising for food emulsion applications over a broad pH range, provided the lipolytic activity can be diminished or circumvented.  相似文献   

2.
The soluble potato proteins are mainly composed of patatin and protease inhibitors. Using DSC and both far-UV and near-UV CD spectroscopy, it was shown that potato proteins unfold between 55 and 75 degrees C. Increasing the ionic strength from 15 to 200 mM generally caused an increase in denaturation temperature. It was concluded that either the dimeric protein patatin unfolds in its monomeric state or its monomers are loosely associated and unfold independently. Thermal unfolding of the protease inhibitors was correlated with a decrease in protease inhibitor activities and resulted in an ionic strength dependent loss of protein solubility. Potato proteins were soluble at neutral and strongly acidic pH values. The tertiary structure of patatin was irreversibly altered by precipitation at pH 5. At mildly acidic pH the overall potato protein solubility was dependent on ionic strength and the presence of unfolded patatin.  相似文献   

3.
The potato (Solanum tuberosum L.) tuber storage protein, patatin, was purified to homogeneity with a molecular mass of 45 kDa. The purified patatin showed antioxidant or antiradical activity by a series of in vitro tests, including 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical (half-inhibition concentration, IC(50), was 0.582 mg/mL) scavenging activity assays, anti-human low-density lipoprotein peroxidation tests, and protections against hydroxyl radical-mediated DNA damages and peroxynitrite-mediated dihydrorhodamine 123 oxidations. Using electron paramagnetic resonance (EPR) spectrometry for hydroxyl radical detections, it was found that the intensities of the EPR signal were decreased by the increased amounts of patatin added (IC(50) was 0.775 mg/mL). Through modifications of patatin by iodoacetamide or N-bromosuccinimide, it was found that the antiradical activities of modified patatin against DPPH or hydroxyl radicals were decreased. It was suggested that cysteine and tryptophan residues in patatin might contribute to its antioxidant activities against radicals.  相似文献   

4.
Autolysis of protein isolates from vascular bundle and inner tuber tissues of potato (Solanum tuberosum) enhanced the inhibition of the angiotensin converting enzyme I (ACE), a biochemical factor affecting blood pressure (hypertension). The physiological age of the tuber affected the strength of ACE inhibition, the rate of its increase during autolysis, and the tuber tissue where ACE inhibition was most pronounced. The highest inhibitory activities (50% reduction in ACE activity achieved following autolysis at a protein concentration of 0.36 mg mL (-1)) were measured in tubers after 5-6 months of storage prior to sprouting. The rate of ACE inhibition was positively correlated with protease activity in tuber tissues. Amendment of the autolysis reaction with protein substrates from which bioactive ACE-inhibitory peptides may be released, for example, a purified recombinant protein or a concentrate of total tuber proteins, also enhanced ACE inhibition. Many tuber proteins including aspartic protease inhibitors were degraded during autolysis. The data provide indications of differences in the enzymatic activities confined to different parts of the potato tuber at different physiological stages. Results suggest that native enzymes and substrate proteins of potato tubers can be utilized in search of dietary tools to manage elevated blood pressure.  相似文献   

5.
Biochemical characteristics of patatin proteins purified by ion-exchange and affinity chromatography from tubers of 20 potato cultivars were studied to evaluate their genotype differences with respect to utility groups, table potato cultivars (TPCs) and processing potato cultivars (PPCs). Both groups of cultivars showed similar values of protein content in dry matter (3.98-7.39%) and of patatin relative abundance (5.40-35.40%). Three mass levels (～40.6, 41.8, and 42.9 kDa) of purified patatins were found by MALDI-TOF MS within all cultivars. Differences among mass levels corresponding with the mass of sugar antenna (～1.2 kDa) confirmed the previous concept of different glycosylation extentsin patatin proteins. It was showed that the individual types of patatin varying in their masses occur in the patatin family in a ratio specific for each of the cultivars, with the lowest mass type being the major one. Electrophoretic analyses demonstrated wide cultivar variability in number of patatin forms. Especially 2D-PAGE showed 17-23 detected protein spots independently on the utility group. Specific lipid acyl hydrolase (LAH) activity of purified patatins from the individual tested cultivars varied between 0.92 and 5.46 μmol/(min mg). Patatin samples within most of the TPCs exhibited higher values of specific LAH activity than samples of PPCs. It may be supposed that individual patatin forms do not have similar physiological roles.  相似文献   

6.
摘要：将马铃薯(Solanum tuberosum )块茎特异蛋白patatin classⅠ基因cDNA与CaMV 35S启动子融合，构建了植物表达载体pBSSP。用电激法将表达载体导入根癌农杆菌（Agrobacterium tumefaciens）LBA4404，然后转化烟草(Nicotiana tabacum )叶片获得再生植株。经PCR、PCR-Southern、Northern杂交和蛋白质检测，证明patatin classⅠ基因cDNA已整合到烟草基因组中并在转基因植株中转录和表达。酯酰水解酶（lipid acylhydrolase, LAH）活性分析显示，转基因烟草植株的叶片中LAH活性明显提高。  相似文献   

7.
Potato starch production leaves behind a huge amount of juice. This juice is rich in protein, which might be exploited for food, biotechnological, and pharmaceutical applications. In northern Europe cv. Kuras is dominant for industrial starch production, and juice protein of freshly harvested mature tubers was fractionated by Superdex 200 gel filtration. The fractions were subjected to selected activity assays (patatin, peroxidase, glyoxalases I and II, alpha-mannosidase, inhibition of trypsin, Fusarium protease, and alcalase) and protein subunit size determination by SDS-PAGE and mass spectrometry. Proteins present in SDS-PAGE bands were identified by tryptic peptide mass fingerprinting. Protein complexes such as ribosomes and proteasomes eluted with the void volume of the gel filtration. Large proteins were enzymes of starch synthesis dominated by starch phosphorylase L-1 (ca. 4% of total protein). Five identified dimeric patatin variants (25%) coeluted with four monomeric lipoxygenase variants (10%) at 97 kDa. Protease inhibitor I variants (4%) at 46 kDa (hexamer) inhibited alcalase. Fourteen Kunitz protease inhibitor variants (30%) at 19 kDa inhibited trypsin and Fusarium protease. Carboxypeptidase inhibitor variants (5%) and defensins (5%) coeluted with phenolics. The native sizes and molecular properties were determined for 43 different potato tuber proteins, several for the first time.  相似文献   

8.
The interaction of the major potato allergen patatin, Sol t 1, with IgE was investigated on a quantitative level as a function of heat treatment at different temperatures. On the basis of a number of publications, potato is considered to be a heat-labile allergen, but the molecular explanation for this behavior was not given. In this work, heat treatment of patatin in the absence and presence of other potato proteins mimicking the proteinaceous environment of the potato was studied. Using far-UV circular dichrosim spectroscopy, tryptophan fluorescence spectroscopy, and differential scanning calorimetry, the molecular transitions during heating of patatin were investigated. It was found that as long as patatin is not aggregated, denaturation of patatin on a secondary or tertiairy folding level is reversible with only a minor effect on the IgE affinity. Aggregation of patatin results in a nonreversible unfolding and a concomitant important decrease in affinity for IgE (25-fold). Aggregation of patatin in the presence of other potato proteins results in a less condensed aggregate compared to the situation of isolated patatin, resulting in a more pronounced decrease of affinity for IgE (110-fold). It is concluded that the heat lability of patatin-IgE interaction is explained by aggregation of patatin with other potato proteins rather than by denaturation of patatin itself.  相似文献   

9.
Whey protein and casein were hydrolyzed with 11 commercially available enzymes. Foam properties of 44 samples were measured and were related to biochemical properties of the hydrolysates using statistical data analysis. All casein hydrolysates formed high initial foam levels, whereas whey hydrolysates differed in their foam-forming abilities. Regression analysis using the molecular weight distribution of whey hydrolysates as predictors showed that the hydrolysate fraction containing peptides of 3-5 kDa was most strongly related to foam formation. Foam stability of whey hydrolysates and of most casein hydrolysates was inferior to that of the intact proteins. The foam stability of casein hydrolysate foams was correlated to the molecular weight distribution of the hydrolysates; a high proportion of peptides >7 kDa, composed of both intact casein and high molecular weight peptides, was positively related to foam stability.  相似文献   

10.
In this study, a protein isolate with a high solubility at neutral pH was prepared from industrial potato juice by precipitation at pH 5 in the presence of ethanol. The effects of ethanol itself and the effects of its presence during precipitation on the properties of various potato protein fractions were examined. The presence of ethanol significantly reduced the denaturation temperature of potato proteins, indicating that the preparation of this potato protein isolate should be performed at low temperature in order to retain a high solubility. In the presence of ethanol, the thermal unfolding of the tertiary and the secondary structure of patatin was shown to be almost completely independent. Even at 4 degrees C, precipitation of potato proteins in the presence of ethanol induced significant conformational changes. These changes did, however, only result in minor changes in the solubility of the potato protein fractions as a function of pH and heat treatment temperature.  相似文献   

11.
Protease inhibitors from potato juice of cv. Elkana were purified and quantified. The protease inhibitors represent ca. 50% of the total soluble proteins in potato juice. The protease inhibitors were classified into seven different families: potato inhibitor I (PI-1), potato inhibitor II (PI-2), potato cysteine protease inhibitor (PCPI), potato aspartate protease inhibitor (PAPI), potato Kunitz-type protease inhibitor (PKPI), potato carboxypeptidase inhibitor (PCI), and "other serine protease inhibitors". The most abundant families were the PI-2 and PCPI families, representing 22 and 12% of all proteins in potato juice, respectively. Potato protease inhibitors show a broad spectrum of enzyme inhibition. All the families (except PCI) inhibited trypsin and/or chymotrypsin. PI-2 isoforms exhibit 82 and 50% of the total trypsin and chymotrypsin inhibiting activity, respectively. A strong variation within the latter activities was shown within one family and between protease inhibitor families.  相似文献   

12.
Foam properties of a sunflower isolate (SI), as well as those of helianthinin and sunflower albumins (SFAs), were studied at various pH values and ionic strengths and after heat treatment. Less foam could be formed from helianthinin than from SFAs, but foam prepared with helianthinin was more stable against Ostwald ripening and drainage than foam prepared with SFAs. Foams made with SFAs suffered from extensive coalescence. The formation and stability of foams made from reconstituted mixtures of both proteins and from SI showed the deteriorating effect of SFAs on foam stability. Foam stability against Ostwald ripening increased after acid and heat treatment of helianthinin. Partial unfolding of sunflower proteins, resulting in increased structural flexibility, improved protein performance at the air/water interface. Furthermore, it was observed that the protein available is used inefficiently and that typically only approximately 20% of the protein present is incorporated in the foam.  相似文献   

13.
The gene of the most abundant protease inhibitor in potato cv. Elkana was isolated and sequenced. The deduced amino acid sequence of this gene showed 98% identity with potato serine protease inhibitor (PSPI), a member of the Kunitz family. Therefore, the most abundant protease inhibitor was considered to be one of the isoforms of PSPI. The PSPI group represents approximately 22% of the total amount of proteins in potato cv. Elkana and is composed of seven different isoforms that slightly differ in isoelectric point. Antibodies were raised against the two most abundant isoforms of PSPI. The binding of these antibodies to PSPI isoforms and protease inhibitors from different groups of protease inhibitor in potato showed that approximately 70% of the protease inhibitors present in potato juice belong to the Kunitz family.  相似文献   

14.
The sponge cake baking test is accepted and routinely used as a standard quality evaluation tool of soft white wheat for Asian markets, but its lengthy and laborious procedure makes it unsuitable for the routine evaluation of a large number of wheat breeding lines. We simplified the sponge cake baking procedure in the egg‐whipping step and improved its consistency by replacement of the hand mixing of cake batter with mechanical mixing, using a wire whisk or a BeaterBlade paddle. Egg whipping and mechanical batter mixing conditions were optimized by comparing foam density, sponge cake volume, and crumb grain to those obtained by the conventional procedure. Foam density, sponge cake volume, and crumb grain comparable to the conventional 100 g flour procedure were obtained with modifications, including extension of whipping time without heat input using a 5 L KitchenAid mixer, one‐time water addition at 3 min before the completion of egg whipping instead of twice, as in the conventional procedure, and cake batter mixing with a KitchenAid wire whisk or a BeaterBlade paddle. For baking a 50 g flour cake, egg foam of appropriate density was obtained with increased whipping speed and shortened egg‐whipping time (8 min). The modified sponge cake baking procedure yielded egg‐foam density, cake volume, and crumb grain similar to the conventional procedure and effectively differentiated soft wheat flours of different quality. Sponge cake volume of 14 soft white wheat flours ranged from 1,134 to 1,426 mL with the conventional procedure, from 1,113 to 1,333 mL with the modified procedure of batter mixing with a wire whisk, from 1,108 to 1,360 mL with the modified procedure of batter mixing with a BeaterBlade paddle, and from 577 to 719 mL with the modified method of 50 g of flour and batter mixing with a wire whisk. The modified methods with the BeaterBlade paddle and wire whisk exhibited significant correlation in cake volume with a conventional procedure (r = 0.931, P < 0.001 and r = 0.925, P < 0.001, respectively).  相似文献   

15.
Botrytis cinerea is an important fungal pathogen particularly dreaded in the cool climate vineyard. It is responsible for important damage, especially the decrease in foamability of sparkling wines, such as Champagne. Different studies have shown that proteins are largely involved in the stabilization of Champagne foam despite their low concentration. Other works demonstrated changes in the electrophoretic characteristics of must proteins originating from botrytized grapes, although the cause of such alterations was never explained. In the first part of this study, results showed the release by B. cinerea of 3.5 mg/L total proteins in a synthetic liquid medium. Among these proteins, the presence of a protease activity on bovine serum albumin (BSA) and must proteins was demonstrated by using a colorimetric method and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. In the model wine, the Bradford method showed a BSA loss of 66% after 24 h and a loss of 96% after 120 h. In the same model wine, the soluble must protein concentration decreased by 35% after 1 week and by 53% after 2 weeks while the control showed no protein loss. B. cinerea proteases were then able to degrade BSA and must proteins and were above all active at must and wine pH and in the presence of ethanol and SO(2). The second part of this work was dedicated to the relationship between the presence of B. cinerea proteases and its effects on the synthetic wine foaming properties. The addition of a B. cinerea culture medium (1/33 v/v) to the synthetic wine containing 21 mg/L soluble grape proteins induced a decrease in foamability by 60% after 1 week. For BSA in the model wine, the foamability decreased by 32% after 24 h and by 95% after 120 h, as shown by the colorimetric method. These experiments demonstrate for the first time the relationship between B. cinerea protease activity and the decrease in wine foaming properties.  相似文献   

16.
Proteins have proven to play a major role in the stabilization of foam in Champagne wines despite their low concentration that ranges from 4 to 20 mg/L. The aim of this study was to evaluate the effect of fining on total protein and grape invertase contents of champenois base wines and their foaming properties. Data showed that fining and especially the use of bentonite at doses ranging from 10 to 50 g/hL leads to a significant decrease in the total protein content of wines together with that of the grape invertase content, with such a decrease being very detrimental to the foaming properties of the treated wines in terms of foam height (HM) and foam stability (HS). Only a slight decrease in the total protein content, in the grape invertase concentration, and in the foam quality of wines was observed when using casein (10 and 20 g/hL) or bentonite combined with casein (both at 20 g/hL). Our study thus clearly establishes the good correlation existing between the wine protein concentration and its foaming properties. A remarkable correlation was observed between the decrease in the grape invertase content and the total protein content of wines, following bentonite treatments, suggesting that the grape invertase (which represents at least 10-20% of the wine proteins) follows a similar behavior upon fining to other proteins of Champagne wines, despite the high molecular mass and the highly glycosylated structure of this particular protein. Moreover, the decrease in total protein and grape invertase contents of wine after fining with bentonite was found to be correlated with a decrease in the foaming properties of the corresponding wines (with respectively R(2) = 0.89 and 0.95).  相似文献   

17.
Brewers' spent grain (BSG) is the insoluble residue of barley malt resulting from the manufacture of wort. Although it is the main byproduct of the brewing industry, it has received little attention as a marketable commodity and is mainly used as animal feed. Our work focuses on one of the main constituents of BSG, i.e., the proteins. The lack of solubility of BSG proteins is one of the limitations for their more extensive use in food processing. We therefore aimed to generate BSG protein hydrolysates with improved technofunctional properties. BSG protein concentrate (BPC) was prepared by alkaline extraction of BSG and subsequent acid precipitation. BPC was enzymatically hydrolyzed in a pH-stat setup by several commercially available proteases (Alcalase, Flavourzyme, and Pepsin) for different times and/or with different enzyme concentrations in order to obtain hydrolysates with different degrees of hydrolysis (DH). Physicochemical properties, such as molecular weight (MW) distribution and hydrophobicity, as well as technofunctional properties, such as solubility, color, and emulsifying and foaming properties, were determined. Enzymatic hydrolysis of BPC improved emulsion and/or foam-forming properties. However, for the hydrolysates prepared with Alcalase and Pepsin, an increasing DH generally decreased emulsifying and foam-forming capacities. Moreover, the type of enzyme impacted the resulting technofunctional properties. Hydrolysates prepared with Flavourzyme showed good technofunctional properties, independent of the DH. Physicochemical characterization of the hydrolysates indicated the importance of protein fragments with relatively high MW (exceeding 14.5 k) and high surface hydrophobicity for favorable technofunctional properties.  相似文献   

18.
The foam stability properties of a defined mixed solution of Tween 20 and bovine serum albumin was evaluated as a function of arabinoxylan concentration. A marked increase in the foam stability was observed with low concentrations of arabinoxylan. Maximum improvement in the foam stability was obtained with 0.2–0.3 mg/mL of arabinoxylan. Enhancement of foam stability due to a combination of bulk viscosity changes and surface effects was identified. The relative contribution of arabinoxylan to bulk viscosity and adsorbed layer structure was studied by examination of the properties of thin liquid films and the macroscopic air-water interface. Arabinoxylan reduced the rate of thin film drainage, increased the equilibrium thickness of the films, slowed the lateral diffusion of a fluorescent probe molecule located in the adsorbed layer, and increased the surface elasticity. These data are congruent with arabinoxylan-mediated crosslinking of adsorbed protein. These observations may be of significance in gas retention during breadmaking. In addition, this naturally occurring polysaccharide offers potential for use in the control of protein foam stability.  相似文献   

19.
beta-Lactoglobulin (betaLg) was subjected to limited hydrolysis by trypsin, plasmin, and endoproteinase from Staphylococcus aureus V8 (S.aur.V8) to degrees of hydrolysis (DH) of 1, 2, and 4%. The several hydrolysates had different peptide compositions (determined by reversed-phase HPLC and gel-permeation chromatography [GPC]). GPC under nondenaturing, denaturing, and denaturing plus reducing conditions showed that the peptides formed were linked by hydrophobic interactions or by disulfide bonds or were not linked at all. At very low protein concentration, some differences in emulsion-forming properties were observed: only the plasmin hydrolysates could form emulsions with a uniform particle-size distribution. The emulsions formed with S.aur.V8 hydrolysates had poor emulsion-stabilizing properties. Some hydrolysates showed increased foam-forming properties in comparison with the intact protein. All foams formed were stable. Overall, the plasmin hydrolysate (DH4) contained relatively much larger molecules and/or hydrophobic molecules. Many molecules were disulfide-linked peptides. This hydrolysate also had the best functional properties.  相似文献   

20.
In this work dynamic light scattering was used to study the thermal aggregation of patatin in situ, to elucidate the physical aggregation mechanism of the protein and to be able to relate the aggregation behavior to its structural properties. The dependence of the aggregation rates on the temperature and the ionic strength suggested a mechanism of slow coagulation, being both diffusion and chemically limited. The aggregation rate dependence on the protein concentration was in accordance with the mechanism proposed. The aggregation rates as obtained at temperatures ranging from 40 to 65 degrees C correlated well with unfolding of the protein at a secondary level. Small-angle neutron scattering and dynamic light scattering results were in good accordance; they revealed that native patatin has a cylindrical shape with a diameter and length of 5 and 9.8 nm, respectively.  相似文献   

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