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ABSTRACT: Fusarium head blight, incited by the fungus Fusarium graminearum, primarily affects wheat (Triticum aestivum) and barley (Hordeum vulgarum), while oat (Avena sativa) appears to be more resistant. Although this has generally been attributed to the open panicle of oats, we hypothesized that a chemical component of oats might contribute to this resistance. To test this hypothesis, we created culture media made of wheat, barley, and oat flour gels (6 g of flour in 20 ml of water, gelled by autoclaving) and inoculated these with plugs of F. graminearum from actively growing cultures. Fusarium growth was measured from the diameter of the fungal plaque. Plaque diameter was significantly smaller on oat flour cultures than on wheat or barley cultures after 40 to 80 h of growth. Ergosterol concentration was also significantly lower in oat cultures than in wheat cultures after growth. A hexane extract from oats added to wheat flour also inhibited Fusarium growth, and Fusarium grew better on hexane-defatted oat flour. The growth of Fusarium on oat flour was significantly and negatively affected by the oil concentration in the oat, in a linear relationship. A hexane-soluble chemical in oat flour appears to inhibit Fusarium growth and might contribute to oat's resistance to Fusarium head blight. Oxygenated fatty acids, including hydroxy, dihydroxy, and epoxy fatty acids, were identified in the hexane extracts and are likely candidates for causing the inhibition.
Journal of food protection 12/2011; 74(12):2188-91. · 1.94 Impact Factor
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ABSTRACT: Oat kernels were extracted with methanol, and glycolipid-enriched fractions were prepared using silica solid phase extraction. Using direct infusion electrospray ionization (ESI) tandem mass spectrometry (MS), high performance liquid chromatography (HPLC)-ESI-MS, and HPLC-atmospheric pressure chemical ionization (APCI)-MS, we confirmed previous reports that digalactosyldiacylglycerol (DGDG) was the most abundant glycolipid in oat kernels and confirmed a previous report of the presence of a DGDG mono-estolide in oat kernels. In the current study we also identified several additional natural galactolipid estolides: two new DGDG estolides (di- and tri-estolides), two trigalactosyldiacylglycerol (TriGDG) estolides (mono- and di-estolides), and one tetragalactosyldiacylglycerol (TetraGDG) estolide (mono-estolide). The levels of total galactolipid estolides in oat kernels were estimated to be about 29% of the total glycolipid fraction. To our knowledge, this report is the first evidence of natural di- and tri-estolides of polar lipids.
Lipids 07/2008; 43(6):533-48. · 2.13 Impact Factor
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ABSTRACT: Quality attributes of waxy durum wheat (Triticum turgidum L), milled semolina and cooked spaghetti were examined and compared with those of two non-waxy durum cultivars. With the exception of kernel hardness, wheat quality characteristics were similar for both waxy and non-waxy durum. Compared with average values obtained for durum wheat grown in North Dakota (USA) during the crop year 2000, the values obtained for the wheat used in this study were equal or better for most parameters evaluated. Semolina extraction for all samples was lower than the 2000 average of 62.6%. The waxy lines had higher ash, lower speck count, similar protein quantity, lower wet gluten and stronger mixograph curves than the non-waxy cultivars. Waxy durum semolina had higher lipid content, starch damage, stirring number and flour swelling values. Spaghetti made from waxy durum semolina had shorter cooking time, similar cooking loss and cooked weight and lower firmness values, which would be unacceptable by most standards. Spaghetti made from blends containing 20–80% waxy durum semolina were evaluated. Cooking time and firmness decreased and cooking loss increased as the amount of waxy semolina increased. Acceptable spaghetti was obtained using 20–40% waxy semolina blends, depending on the quality of the non-waxy blending material. Copyright © 2004 Society of Chemical Industry
Journal of the Science of Food and Agriculture 01/2004; 84(2):190 - 196. · 1.44 Impact Factor
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ABSTRACT: Cereal Chem. 78(6):675–679 The determination of groat percentage in experimental oat breeding lines requires the dehulling of oats. Here, we report the results of our efforts to optimize dehulling conditions so that the most accurate and reliable result can be obtained. Hand dehulling was always reliable and accurate, however, it was the most time-consuming and tedious of the methods studied. Two mechanical methods of oat dehulling, compressed-air dehulling and impact dehulling, also frequently provided reliable results, however, results were strongly influenced by dehulling conditions. Opti-mal dehulling conditions represented compromises between unfavorable extremes. Correct aspiration strength was critical to accurate groat per-centage determination. We have found that a secondary aspiration is highly desirable after compressed-air dehulling to remove hulls remaining with the groats after dehulling. Also, increased mechanical stress on oats as exerted either by the number of passes through the impact dehuller, or by the air pressure in the compressed-air dehuller, resulted in higher dehulling efficiency, but increased groat breakage as well. Dehulling efficiency decreased as moisture increased from 7.5 to 15%, but increased as moisture was further increased to 30%. In contrast, groat breakage with impact dehulling decreased as moisture increased from 7.5 to 30%. A new equation for groat percentage calculation has been introduced where the mass of hulled oats remaining after dehulling is subtracted from the mass of the original oat sample, so that poor dehulling efficiency does not influence the groat percentage.
01/2001; 78.
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ABSTRACT: Growth and development of plants are known to be affected by exposure to red and blue light. Mechanisms by which light quality influences gene expression in maize (Zea mays L.) embryos have not been explored. Maize kernels can be cultured in vitro allowing experimental manipulation of environmental factors during seed development. We used the in vitro kernel culture system to investigate the response of developing maize seeds, which normally develop without exposure to light, to controlled light quality. Kernels grown under red light accumulated more dry weight than those grown in darkness, whereas kernels grown under blue light accumulated less. Reciprocal color shift experiments showed that light quality during the first week in culture had more influence on kernel weight than during the subsequent three weeks in culture. Soluble sugars were higher in both light treatments than in darkness. Blue-grown kernels had higher amino acid and lower lipid levels than red-or dark-grown kernels. Embryo morphology was markedly affected by red light, under which the upper shoot axis was longer than under blue light or in darkness. Embryo morphology was influenced by light quality during the later stages of development rather than the first week. We suggest, based on these results, that gene expression in the embryo and endosperm of developing maize seeds is sensitive to light quality, and the mechanism and time dependence of this effect warrant further study. In vitro maize kernel culture affords a convenient system for such light quality experiments.
Plant Cell Tissue and Organ Culture 07/1995; 42(2):147-152. · 3.09 Impact Factor
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ABSTRACT: Fumonisin B1 toxin is produced by the fungusFusarium moniliforme Sheldon, which is systemic to maize (Zea mays L.) and maize seeds. The effects of zero to 100 parts per million fumonisin B1 on the germination process of maize seeds was determined. The presence of fumonisin had no effect on percent seed germination, but fumonisin inhibited radicle elongation by up to 75% after 48 hours of imbibition. An analysis of amylase secretion in the maize endosperm indicated that fumonisins inhibited amylase production in the germinating seed. Isoelectric focusing of endosperm extracts indicated that secretion of the low pI class of amylases was affected more that other amylase isozymes. The results suggested that the presence of high levels of fumonisin in maize seed may have deleterious effects on seedling emergence.
Mycopathologia 07/1994; 127(2):117-121. · 1.65 Impact Factor
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ABSTRACT: To examine the effects of N nutrition upon endosperm development, maize (Zea mays) kernels were grown in vitro with either 0, 3.6, 7.1, 14.3, or 35.7 millimolar N. Kernels were harvested at 20 days after pollination for determination of enzyme activities and again at maturity for quantification of storage products and electrophoretic separation of zeins. Endosperm dry weight, starch, zein-N, and nonzein-N all increased in mature kernels as N supply increased from zero to 14.3 millimolar. The activities of sucrose synthase, aldolase, phosphoglucomutase, glutamate-pyruvate transaminase, glutamate-oxaloacetate transaminase, and acetolactate synthase increased from 1- to 2.5-fold with increasing N supply. Adenosine diphosphate-glucose pyrophosphorylase and both ATP- and PPi-dependent phosphofructokinases increased to lesser extents, while no significant response was detected for hexose kinases and glutamine synthetase. Nitrogen-induced changes in enzyme activities were often highly correlated with changes in final starch and/or zein-N contents. Separation of zeins indicated that these peptides were proportionately enhanced by N supply, with the exception of C-zein, which was relatively insensitive to N. These data indicate that at least a portion of the yield increase in maize produced by N fertilization is induced by a modification of kernel metabolism in response to N supply.
Plant physiology 12/1990; 94(3):858-64. · 6.53 Impact Factor
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ABSTRACT: Characterization of sugar content and enzyme activity in germinating soybean (Glycine max L. Merrell) seeds led to the discovery of sorbitol accumulating in the axes during germination. The identity of sorbitol was confirmed by relative retention times on high-performance liquid chromatography and gas liquid chromatography and by mass spectra identical with authentic sorbitol. Accumulation of sorbitol in the axes started on day 1 of germination as sucrose decreased and glucose and fructose increased. Sucrose also decreased in the cotyledons, but there was no accumulation of sorbitol, glucose, or fructose. Accumulation of sorbitol and hexoses was highly correlated with increased invertase activity in the axes, but not with sucrose synthase and sucrose phosphate synthase activities. Sucrose synthase activity was relatively high in the axes, whereas the activity of sucrose phosphate synthase was relatively high in the cotyledons. Ketose reductase and aldose reductase were detected in germinating soybean axes, but not in cotyledons. Fructokinase and glucokinase were present in both axes and cotyledons. The data suggest a sorbitol pathway functioning in germinating soybean axes, which allows for the interconversion of glucose and fructose with sorbitol as an intermediate.
Plant physiology 09/1990; 93(4):1514-20. · 6.53 Impact Factor
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D C Doehlert
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ABSTRACT: A new form of fructokinase has been identified from developing maize (Zea mays L.) kernels that utilizes CTP, UTP, and GTP from four to eight times more effectively than ATP at nonlimiting concentrations. Ten millimolar dithiothreitol was necessary to stabilize activity. A second form of fructokinase was nonspecific for nucleoside triphosphate whereas a third form was fairly specific for ATP.
Plant physiology 06/1990; 93(1):353-5. · 6.53 Impact Factor
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ABSTRACT: Sugar metabolism in kernels of starch-deficient endosperm mutants of maize (Zea mays L.) was examined to determine how single locus mutations of carbohydrate metabolism affect carbohydrate metabolism as a whole. Activities of 14 enyzmes were measured in extracts from endosperms from isogenic lines of normal, shrunken, shrunken-2, shrunken-4, brittle-1, and brittle-2 maize in an OH43 background. Nearly every enzyme activity examined was affected in some or all of the mutants. Sucrose synthase and aldolase activities were lower in all mutants compared to normal. ADP-Glc pyrophosphorylase activity in immature kernels was much higher in brittle endosperms than in normal, but absent in brittle-2 and shrunken-2 endosperms. The activity in those genotypes exhibiting activity was positively correlated with sucrose concentration in the kernels. Sucrose may be modulating the coarse control of ADP-Glc pyrophosphorylase activity by affecting the genetic transcription of message for this enzyme. Sorbitol dehydrogenase activity was negatively correlated with its substrate, fructose, supporting the hypothesis that sorbitol dehydrogenase converts fructose produced during sucrose degradation into sorbitol. Glucokinase activity was positively correlated with mature kernel dry weight. This supports the hypothesis that glucokinase activity may limit sucrose utilization. Shrunken-4 extracts had lower activities for a number of enzymes, supporting the view that this mutant may have an impediment to protein synthesis. Elevated sucrose levels were evenly distributed throughout 20-day postpollination shrunken-2 kernels, whereas a sucrose concentration gradient existed in normal kernels between the basal region and the upper endosperm. This gradient is apparently generated by the utilization of sugars and may facilitate the movement of sugars into developing corn kernels.
Plant physiology 05/1990; 92(4):990-4. · 6.53 Impact Factor
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D C Doehlert
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ABSTRACT: Four forms of hexose kinase activity from developing maize (Zea mays L.) kernels have been separated by ammonium sulfate precipitation, gel filtration chromatography, blue-agarose chromatography, and ion exchange chromatography. Two of these hexose kinases utilized d-glucose most effectively and are classified as glucokinases (EC 2.7.1.2). The other two hexose kinases utilized only d-fructose and are classified as fructokinases (EC 2.7.1.4). All hexose kinases analyzed had broad pH optima between 7.5 and 9.5 with optimal activity at pH 8.5. The two glucokinases differed in substrate affinities. One form had low K(m) values [K(m)(glucose) = 117 micromolar, K(m)(ATP) = 66 micromolar] whereas the other form had much higher K(m) values [K(m)(glucose) = 750 micromolar, K(m)(ATP) = 182 micromolar]. Both fructokinases had similar substrate saturation responses. The K(m)(fructose) was about 130 micromolar and the K(m)(ATP) was about 700 micromolar. Both exhibited uncompetitive substrate inhibition by fructose [K(i)(fructose) = 1.40 to 2.00 millimolar]. ADP inhibited all four hexose kinase activities, whereas sugar phosphates had little effect on their activities. The data suggest that substrate concentrations are an important factor controlling hexose kinase activity in situ.
Plant physiology 05/1989; 89(4):1042-8. · 6.53 Impact Factor
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ABSTRACT: Tissue distribution and activity of enzymes involved in sucrose and hexose metabolism were examined in kernels of two inbreds of maize (Zea mays L.) at progressive stages of development. Levels of sugars and starch were also quantitated throughout development. Enzyme activities studied were: ATP-linked fructokinase, UTP-linked fructokinase, ATP-linked glucokinase, sucrose synthase, UDP-Glc pyrophosphorylase, UDP-Glc dehydrogenase, PPi-linked phosphofructokinase, ATP-linked phosphofructokinase, NAD-dependent sorbitol dehydrogenase, NADP-dependent 6-P-gluconate dehydrogenase, NADP-dependent Glc-6-P dehydrogenase, aldolase, phosphoglucoisomerase, and phosphoglucomutase. Distribution of invertase activity was examined histochemically. Hexokinase and ATP-linked phosphofructokinase activities were the lowest among these enzymes and it is likely that these enzymes may regulate the utilization of sucrose in developing maize kernels. Most of the hexokinase activity was found in the endosperm, but the embryo had high activity on a dry weight basis. The endosperm, which stores primarily starch, contained high PPi-linked phosphofructokinase and low ATP-linked phosphofructokinase activities, whereas the embryo, which stores primarily lipids, had much higher ATP-linked phosphofructokinase activity than did the endosperm. It is suggested that PPi required by UDP-Glc pyrophosphorylase and PPi-linked phosphofructokinase in the endosperm may be supplied by starch synthesis. Sorbitol dehydrogenase activity was largely restricted to the endosperm, whereas 6-P-gluconate and Glc-6-P dehydrogenase activities were highest in the base and pericarp. A possible metabolic pathway by which sucrose is converted into starch is proposed.
Plant physiology 05/1988; 86(4):1013-9. · 6.53 Impact Factor
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D C Doehlert
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ABSTRACT: Ketose reductase (NAD-dependent polyol dehydrogenase EC 1.1.1.14) activity, which catalyzes the NADH-dependent reduction of fructose to sorbitol (d-glucitol), was detected in developing maize (Zea mays L.) endosperm, purified 104-fold from this tissue, and partially characterized. Product analysis by high performance liquid chromatography confirmed that the enzyme-catalyzed reaction was freely reversible. In maize endosperm, 15 days after pollination, ketose reductase activity was of the same order of magnitude as sucrose synthase activity, which produces fructose during sucrose degradation. Other enzymes of hexose metabolism detected in maize endosperm were present in activities of only 1 to 3% of the sucrose synthase activity. CaCl(2), MgCl(2), and MnCl(2) stimulated ketose reductase activity 7-, 6-, and 2-fold, respectively, but had little effect on NAD-dependent polyol dehydrogenation (the reverse reaction). The pH optimums for ketose reductase and polyol dehydrogenase reactions were 6.0 and 9.0, respectively. K(m) values were 136 millimolar fructose and 8.4 millimolar sorbitol. The molecular mass of ketose reductase was estimated to be 78 kilodaltons by gel filtration. It is postulated that ketose reductase may function to metabolize some of the fructose produced during sucrose degradation in maize endosperm, but the metabolic fate of sorbitol produced by this reaction is not known.
Plant physiology 08/1987; 84(3):830-4. · 6.53 Impact Factor
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ABSTRACT: Invertase (β-fructofuranoside fructohydrolase, EC 3.2.1.26) activity in developing maize (Zea mays L. inbred W64A) was separated into soluble and particulate forms. The particulate form was solubilized by treatment with 1 M NaCl or with other salts. However, CaCl2 inhibited invertase activity, and neither detergents nor 0.5 M methyl mannoside were effective in solubilizing the invertase activity. The soluble and particulate invertases were both glycoproteins, both had pH optima of 5.0 and Km values for sucrose of 2.83 and 1.84 mM, respectively. The apparent molecular weight of salt-solubilized invertase was 40 kDa. Gel filtration of the soluble invertase showed multiple peaks with apparent molecular weights ranging from 750 kDa to over 9 000 kDa. Histochemical staining of cell wall preparations for invertase activity suggested that the particulate invertase is associated with the cell wall. Also, nearly all the invertase activity was localized in the basal endosperm and pedicel tissues, which are sites of sugar transport. No invertase activity was found in the upper endosperm, the embryo or in the placento-chalazal tissue. In contrast, sucrose synthase (EC 2.4.1.13) activity was found primarily in the embryo and the upper endosperm, which are areas of active biosynthesis of storage compounds.
Physiologia Plantarum 04/1987; 70(1):51 - 57. · 3.11 Impact Factor
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ABSTRACT: The inhibition patterns of inorganic phosphate (Pi) on sucrose phosphate synthase activity in the presence and absence of the allosteric activator glucose-6-P was studied, as well as the effects of phosphoglucoisomerase on fructose-6-P saturation kinetics with and without Pi. In the presence of 5 millimolar glucose-6-P, Pi was a partial competitive inhibitor with respect to both substrates, fructose-6-P and uridine diphosphate glucose. In the absence of glucose-6-P, the inhibition patterns were more complex, apparently because of the interaction of Pi at the activation site as well as the catalytic site. In addition, substrate activation by uridine diphosphate glucose was observed in the absence of effectors. The results suggested that Pi antagonizes glucose-6-P activation of sucrose phosphate synthase by competing with the activator for binding to the modifier site.The fructose-6-P saturation kinetics were hyperbolic in the absence of phosphoglucoisomerase activity, but became sigmoidal by the addition of excess phosphoglucoisomerase. The sigmoidicity persisted in the presence of Pi, but sucrose phosphate synthase activity was decreased. The apparent sigmoidal response may represent the physiological response of sucrose phosphate synthase to a change in hexose-P concentration because sucrose phosphate synthase operates in the cytosol in the presence of high activities of phosphoglucoisomerase. Thus, the enzymic production of an activator from a substrate represents a unique mechanism for generating sigmoidal enzyme kinetics.
Plant physiology 10/1984; 76(1):250-3. · 6.53 Impact Factor
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ABSTRACT: Sucrose phosphate synthase was partially purified from spinach leaves and the effects and interactions among glucose-6-P, inorganic phosphate (Pi), and pH were investigated. Glucose-6-P activated sucrose phosphate synthase and the concentration required for 50% of maximal activation increased as the concentration of fructose-6-P was decreased. Inorganic phosphate inhibited sucrose phosphate synthase activity and antagonized the activation by glucose-6-P. Inorganic phosphate caused a progressive increase in the concentration of glucose-6-P required for 50% maximal activation from 0.85 mm (minus Pi) to 9.9 mm (20 mm Pi). In the absence of glucose-6-P, Pi caused partial inhibition of sucrose phosphate synthase activity (about 65%). The concentration of Pi required for 50% maximal inhibition decreased with a change in pH from 6.5 to 7.5. When the effect of pH on Pi ionization was taken into account, it was found that per cent inhibition increased hyperbolically with increasing dibasic phosphate concentration independent of the pH. Sucrose phosphate synthase had a relatively broad pH optimum centered at pH 7.5. Inhibition by Pi was absent at pH 5.5, but became more pronounced at alkaline pH, whereas activation by glucose-6-P was observed over the entire pH range tested. The results suggested that glucose-6-P and Pi bind to sites distinct from the catalytic site, e.g. allosteric sites, and that the interactions of these effectors with pH and concentrations of substrate may be involved in the regulation of sucrose synthesis in vivo.
Plant physiology 01/1984; 73(4):989-94. · 6.53 Impact Factor
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ABSTRACT: The specific measurement of alpha-amylase activity in crude plant extracts is difficult because of the presence of beta-amylases which directly interfere with most assay methods. Methods compared in this study include heat treatment at 70 degrees C for 20 min, HgCl(2) treatment, and the use of the alpha-amylase specific substrate starch azure. In comparing alfalfa (Medicago sativa L.), soybeans (Glycine max [L.] Merr.), and malted barley (Hordeum vulgare L.), the starch azure assay was the only satisfactory method for all tissues. While beta-amylase can liberate no color alone, over 10 International units per milliliter beta-amylase activity has a stimulatory effect on the rate of color release. This stimulation becomes constant (about 4-fold) at beta-amylase activities over 1,000 International units per milliliter. Two starch azure procedures were developed to eliminate beta-amylase interference: (a) the dilution procedure, the serial dilution of samples until beta-amylase levels are below levels that interfere; (b) the beta-amylase saturation procedure, addition of exogenous beta-amylase to increase endogenous beta-amylase activity to saturating levels. Both procedures yield linear calibrations up to 0.3 International units per milliliter. These two procedures produced statistically identical results with most tissues, but not for all tissues. Differences between the two methods with some plant tissues was attributed to inaccuracy with the dilution procedure in tissues high in beta-amylase activity or inhibitory effects of the commercial beta-amylase. The beta-amylase saturation procedure was found to be preferable with most species. The heat treatment was satisfactory only for malted barley, as alpha-amylases in alfalfa and soybeans are heat labile. Whereas HgCl(2) proved to be a potent inhibitor of beta-amylase activity at concentrations of 10 to 100 micromolar, these concentrations also partially inhibited alpha-amylase in barley malt. The reported alpha-amylase activities in crude enzyme extracts from a number of plant species are apparently the first specific measurements reported for any plant tissues other than germinating cereals.
Plant physiology 03/1983; 71(2):229-34. · 6.53 Impact Factor
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ABSTRACT: Amylase was found in high activity (193 international units per milligram protein) in the tap root of alfalfa (Medicago sativa L. cv. Sonora). The activity was separated by gel filtration chromatography into two fractions with molecular weights of 65,700 (heavy amylase) and 41,700 (light amylase). Activity staining of electrophoretic gels indicated the presence of one isozyme in the heavy amylase fraction and two in the light amylase fraction. Three amylase isozymes with electrophoretic mobilities identical to those in the heavy and the light amylase fractions were the only amylases identified in crude root preparations. Both heavy and light amylases hydrolyzed amylopectin, soluble starch, and amylose but did not hydrolyze pullulan or beta-limit dextrin. The ratio of viscosity change to reducing power production during starch hydrolysis was identical for both alfalfa amylase fractions and sweet potato beta-amylase, while that of bacterial alpha-amylase was considerably higher. The identification of maltose and beta-limit dextrin as hydrolytic end-products confirmed that these alfalfa root amylases are all beta-amylases.The pH optimum for both beta-amylase fractions was 6.0. Both light and heavy beta-amylases showed normal Michaelis-Menten kinetics, with soluble starch as substrate, and had respectively K(m) values of 5.9 and 6.8 milligrams starch per milliliter and V(max) of 640 and 130 international units per milligram protein. Arrhenius plots indicated that the energy of activation for the heavy beta-amylase remained relatively unchanged (12.7 to 13.0 kilocalories per mole) from 0 to 30 degrees C, whereas the energy of activation for the light amylase increased from 12.0 to about 28.0 kilocalories per mole at 8.7 degrees C as temperature was lowered. The light amylase was shown to be inhibited by maltose.
Plant physiology 06/1982; 69(5):1096-102. · 6.53 Impact Factor
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ABSTRACT: The activation of spinach leaf sucrose phosphate synthase by glucose 6-phosphate (Glc6 P) was labile in the absence of dithiothreitol, whereas enzyme activity in the absence of activator remained stable. The loss of regulation by Glc6P proceeded more rapidly by treatment with 24 mM H2O2 and was reversible by 2.5 mM dithiothreitol. Titration of the enzyme with the sulfhydryl reagents N-ethylmaleimide or p-chloromercuribenzenesulfonic acid (0–50 μM) also resulted in elimination of Glc6P activation and most of the inorganic phosphate inhibition without eliminating catalytic activity. The results suggested that Glc6P and phosphate bind to a modifier site that is distinct from the catalytic site. The modifier site apparently contains essential and accessible sulfhydryl groups, while the catalytic site does not. Even though sulfhydryl reagents did not eliminate catalysis, changes in substrate affinities occurred. Treatment with 50 μM p-chloromercuribenzenesulfonic acid lowered the Km (fructose 6-phosphate) from 3.0 to 1.0 mM and increased the Km (uridine diphosphate glucose) from 3.0 to 8.9 mM without affecting the Vmax. Spinach leaf sucrose phosphate synthase extracted in the absence of reductant from leaves in the light (at 15:00 h) or in the dark (at 03:00 h) exhibited similar Glc6P activation, suggesting that the light/dark status of leaves does not affect the redox status of essential sulfhydryl groups of the modifier site.
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology.
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ABSTRACT: Test weight or bulk density of oats (Avena sativa L.) has a major influence on the monetary value of oat grain. We hypothesize that test weight can be attributed to grain density and packing efficiency. We have measured oat grain volume and density by a sand-displacement method and derived the packing factor for six oat cultivars grown in three environments. Volumes of individual grains were 31-38 mm3 and were highly correlated with grain mass. Grain densities were 0.96-1.03 g/cm3. Packing efficiency, defined as the space proportion occupied by the grains, was 53-55%. Regression analysis suggested that 78% of the variation in test weight could be attributed to grain density. Size fractionation of grain by sieving and analysis by digital image analysis indicated that smaller grains within an oat sample packed more efficiently than larger grains and larger grains in a sample were less dense than the smaller grains. Analysis of oat grain components indicated groat densities were approximately equal to 1.29 g/cm3 and hull densities were approximately equal to 0.69 g/cm3. The difference in densities between groat and hull provide a physical basis for the recognized relationship between groat percentage and test weight.
