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Site-specific phosphorylation of L-form starch phosphorylase by the protein kinase activity from sweet potato roots.

A 78-amino acid insertion (L78) is found in the low-affinity type (L-form) of starch phosphorylase (L-SP, EC 2.4.1.1). This insertion blocks the starch-binding site on the L-SP molecule, and it decreases the binding affinity of L-SP toward starch. The computational analysis of the amino acid sequence on L78 predicts several phosphorylation sites at its Ser residues. Indeed, from the immunoblotting results using antibodies against phosphoamino acids, we observed that the purified L-SP from mature sweet potato (Ipomoea batatas) roots is phosphorylated. This observation led us to the detection of a protein kinase activity in the protein fraction of the crude extract from the sweet potato roots. The kinase was partially purified by liquid chromatography, and its native molecular mass was estimated as 338 kDa. An expressed peptide (L78P) containing the essential part of L78 was intensively phosphorylated by the kinase. However, H-SP (the high-affinity isomer of SP lacking the L78 insertion) and the proteolytic modified L-SP, which lost its L78 fragment, could not be phosphorylated. Furthermore, using L78P mutants by site-directed mutagenesis at Ser residues on L78, we demonstrate that only one Ser residue on L78 is phosphorylated by the kinase. These results imply that this kinase is specific to L-SP, or more precisely, to the L78 insertion. The in vitro phosphorylated L-SP shows higher sensitivity to proteolytic modification, but has no change in its kinetic parameters.

Amino Acid Sequence↗

Sucrose and starch catabolism in the anther of Lilium during its development: a comparative study among the anther wall, locular fluid and microspore/pollen fractions.

In order to better understand the various pathways of sucrose and starch catabolism in the anther of lily (Lilium hybrida var. "Enchantment"), invertase (EC 3.2.1.26) and amylase (EC 3.2.1.1, EC 3.2.1.2) activities were measured separately in different fractions (anther wall, locular fluid and microspore/pollen) and correlated with the sugar content during anther development. Our findings showed significant differences among the fractions analyzed, suggesting that the regulation of sucrose and starch catabolism could follow distinct pathways in each fraction. Glucose and fructose amounts progressively decreased from anther wall to fluid and from fluid to microspore/pollen. Thus, the developing pollen could act as a sink for the carbohydrates that reach the anther. In this sense, cell wall-bound invertases seem to play a major role in soluble sugar partitioning in the different fractions of the anther. Sucrose concentration was found to be substantially higher in the locular fluid than in the other fractions, indicating a probable site for storage. On the other hand, the anther wall tissues could have a buffering function, storing nutrient surplus in starch grains and thus regulating the availability of soluble sugars in the whole anther. All these results proved the advantages of the experimental model proposed here, as well as its usefulness to investigate sugar metabolism in Lilium anthers.

Amylases↗

Growth of tobacco in short-day conditions leads to high starch, low sugars, altered diurnal changes in the Nia transcript and low nitrate reductase activity, and inhibition of amino acid synthesis.

Diurnal changes in carbohydrates and nitrate reductase (NR) activity were compared in tobacco (Nicotiana tabacum. L.cv. Gatersleben) plants growing in a long (18 h light/6 h dark) and a short (6 h light/18 h dark) day growth regime, or after short-term changes in the light regime. In long-day-grown plants, source leaves contained high levels of sugars throughout the light and dark periods. In short-day-grown plants, levels of sucrose and reducing sugars were very low at the end of the night and, although they rose during the light period, remained much lower than in long days and declined to very low levels again by the middle of the night. Starch accumulated more rapidly in short-day-than long-day-grown plants. Starch was completely remobilised during the night in short days, but not in long days. A single short day/long night cycle sufficed to stimulate starch accumulation during the following light period. In long-day-grown plants, the Nia transcript level was high at the end of the night, decreased during the day, and recovered gradually during the night. In short-day-grown plants, the Nia transcript level was relatively low at the end of the night, decreased to very low levels at the end of the light period, increased to a marked maximum in the middle of the night, and decreased during the last 5 h of the dark period. In long-day-grown plants, NR activity in source leaves rose by 2- to 3-fold in the first part of the light period and decreased in the second part of the light period. In short-day-grown plants, NR activity was low at the end of the night, and only increased slightly after illumination. Dark inactivation of source-leaf NR was partially reversed in long-day-grown plants, but not in short day-grown plants. In both growth regimes, mutants with one instead of four functional copies of the Nia gene had a 60% reduction in maximum NR activity in the source leaves, compared to wild-type plants. The diurnal changes in NR activity were almost completely suppressed in the mutants in long days, whereas the mutants showed similar or slightly larger diurnal changes than wild-type plants in short days. When short-day-grown plants were transferred to long-day conditions for 3 d, NR activity and the diurnal changes in NR activity resembled those in long-day-grown plants. Phloem export from source leaves of short-day-grown plants was partially inhibited by applying a cold-girdle for one light and dark cycle. The resulting increase in leaf sugar was accompanied by an marked increase in the Nia transcript level and a 2-fold increase in NR activity at the end of the dark period. When wild-type plants were subjected to a single short day/long night cycle of increasing severity, NR activity in source leaves at the end of the night decreased when the endogenous sugars declined below about 3 mumol hexose (g FW)-1. In sink leaves in short-day conditions, sugars were higher and the light-induced rise in NR activity was much larger than in source leaves on the same plants. The source leaves of wild-type plants in short-day conditions contained very high levels of nitrate, very low levels of glutamine, low levels of total amino acids, and lower protein and chlorophyll, compared to long-day-grown plants. Plants grown in short days had relatively high levels of glutamate and aspartate, and extremely low levels of most of the minor amino acids in their source leaves at the end of the night. Illumination led to a decrease in glutamate and an increase in the minor amino acids. A single short day/long night cycle led to an increase in glutamate, and a large decrease in the minor acids at the end of the dark period, and reillumination led to a decrease in glutamate and an increase in the minor amino acids. It is proposed that sugar-mediated control of Nia expression and NR activity overrides regulation by nitrogenous compounds when sugars are in short supply, resulting in a severe inhibition of nitrate assimilation. It is also proposed that su

Amino Acids↗

Genetic evidence that the two isozymes of sucrose synthase present in developing maize endosperm are critical, one for cell wall integrity and the other for starch biosynthesis.

In maize, two paralogous genes, Sh1 and Sus1, encode two biochemically similar isozymes of sucrose synthase, SS1 and SS2, respectively. Previous studies have attributed the mild starch deficiency of the shrunken1 (sh1) endosperm to the loss of the SS1 isozyme in the mutant. Here we describe the first mutation in the sucrose synthase1 (Sus1) gene, sus1-1, and the isolation of a double recessive genotype, sh1 sus1-1. Combined data from diverse studies, including Northern and Western analyses, RT-PCR and genomic PCR, cloning and sequencing data for the 3' region, show that the mutant sus1-1 gene has a complex pattern of expression, albeit at much reduced levels as compared to the Sus1 gene. Endosperm sucrose synthase activity in sh1 sus1-1 was barely 0.5% of the total activity in the Sh1 Sus1 genotype. Significantly, comparative analyses of Sh1 Sus1, sh1 Sus1 and sh1 sus1-1 genotypes have, for the first time, allowed us to dissect the relative contributions of each isozyme to endosperm development. Starch contents in endosperm of the three related genotypes were 100, 78 and 53%, respectively. Anatomical analyses, which confirmed the previously described early cell degeneration phenotype unique to the sh1 Sus1 endosperm, revealed no detectable difference between the two sh1 genotypes. We conclude that the SS1 isozyme plays the dominant role in providing the substrate for cellulose biosynthesis, whereas the SS2 protein is needed mainly for generating precursors for starch biosynthesis.

Base Sequence↗

Enzymes from Sulfolobus shibatae for the production of trehalose and glucose from starch.

Enzymes that convert starch and dextrins to alpha,alpha-trehalose and glucose were found in cell homogenates of the hyperthermophilic acidophilic archaeon Sulfolobus shibatae DMS 5389. Three enzymes were purified and characterized. The first, the S. shibatae trehalosyl dextrin-forming enzyme (SsTDFE), transformed starch and dextrins to the corresponding trehalosyl derivatives with an intramolecular transglycosylation process that converted the glucosidic linkage at the reducing end from alpha-1,4 to alpha-1,1. The second, the S. shibatae trehalose-forming enzyme (SsTFE), hydrolyzed the alpha-1,4 linkage adjacent to the alpha-1,1 bond of trehalosyl dextrins, forming trehalose and lower molecular weight dextrins. These two enzymes had molecular masses of 80 kDa and 65 kDa, respectively, and showed the highest activities at pH 4.5. The apparent optimal temperature for activity was 70 degrees C for SsTDFE and 85 degrees C for SsTFE. The third enzyme identified was an alpha-glycosidase (Ss alpha Gly), which catalyzed the hydrolysis of the alpha-1,4 glucosidic linkages in starch and dextrins, releasing glucose in a stepwise manner from the nonreducing end of the polysaccharide chain. The enzyme had a molecular mass of 313 kDa and showed the highest activity at pH 5.5 and at 85 degrees C.

Glucose↗

The effect of starch-based biomaterials on leukocyte adhesion and activation in vitro.

Leukocyte adhesion to biomaterials has long been recognised as a key element to determine their inflammatory potential. Results regarding leukocyte adhesion and activation are contradictory in some aspects of the material's effect in determining these events. It is clear that together with the wettability or hydrophilicity/hydrophobicity, the roughness of a substrate has a major effect on leukocyte adhesion. Both the chemical and physical properties of a material influence the adsorbed proteins layer which in turn determines the adhesion of cells. In this work polymorphonuclear (PMN) cells and a mixed population of monocytes/macrophages and lymphocytes (mononuclear cells) were cultured separately with a range of starch-based materials and composites with hydroxyapatite (HA). A combination of both reflected light microscopy and scanning electron microscopy (SEM) was used in order to study the leukocyte morphology. The quantification of the enzyme lactate dehydrogenase (LDH) was used to determine the number of viable cells adhered to the polymers. Cell adhesion and activation was characterised by immunocytochemistry based on the expression of several adhesion molecules, crucial in the progress of an inflammatory response. This work supports previous in vitro studies with PMN and monocytes/macrophages, which demonstrated that there are several properties of the materials that can influence and determine their biological response. From our study, monocytes/macrophages and lymphocytes adhere in similar amounts to more hydrophobic (SPCL) and to moderately hydrophilic (SEVA-C) surfaces and do not preferentially adhere to rougher substrates (SCA). Contrarily, more hydrophilic surfaces (SCA) induced higher PMN adhesion and lower activation. In addition, the hydroxyapatite reinforcement induces changes in cell behaviour for some materials but not for others. The observed response to starch-based biodegradable polymers was not significantly different from the control materials. Thus, the results reported herein indicate the low potential of the starch-based biodegradable polymers to induce inflammation especially the HA reinforced composite materials.

Biocompatible Materials↗

Synergistic action of recombinant alpha-amylase and glucoamylase on the hydrolysis of starch granules.

Barley alpha-amylase 1 mutant (AMY) and Lentinula edodes glucoamylase (GLA) were cloned and expressed in Saccharomyces cerevisiae. The purified recombinant AMY hydrolyzed corn and wheat starch granules, respectively, at rates 1.7 and 2.5 times that of GLA under the same reaction conditions. AMY and GLA synergistically enhanced the rate of hydrolysis by approximately 3x for corn and wheat starch granules, compared to the sum of the individual activities. The exo-endo synergism did not change by varying the ratio of the two enzymes when the total concentration was kept constant. A yield of 4% conversion was obtained after 25 min 37 degrees C incubation (1 unit total enzyme, 15 mg raw starch granules, pH 5.3). The temperature stability of the enzyme mixtures was < or =50 degrees C, but the initial rate of hydrolysis continued to increase with higher temperatures. Ca(++) enhanced the stability of the free enzymes at 50 degrees C incubation. Inhibition was observed with the addition of 10 mM Fe(++) or Cu(++), while Mg(++ )and EDTA had lesser effect.

Enzyme Stability↗

Effect of cooking procedures and storage on starch bioavailability in common beans (Phaseolus vulgaris L.).

Common commercial beans were cooked using two procedures: under pressure (autoclaving) and traditional cooking. Total starch extraction was higher in beans cooked with the traditional procedure (41.69-42.81%) than in the autoclaved samples (37.04-38.16%) and did not change during storage at 4 degrees C. However, available and total resistant starch levels in vitro were not influenced by the cooking procedure or storage. Retrograded resistant starch content was higher in beans cooked with the traditional process (2.65-2.79%) than in autoclaved beans (1.62-1.94%). The initial in vitro alpha-amylolysis rate in freshly cooked beans was higher in the autoclaved preparation than in the beans cooked by the traditional process, but final hydrolysis indices (90 min) were similar for both samples. None of the bean samples showed statistical differences in alpha-amylolysis behavior (alpha = 0.05) after storage at 4 degrees C for 96 hour.

Biological Availability↗

Extraction of starch by dimethyl sulfoxide and quantitation by enzymatic assay.

A method for the rapid, sensitive, and specific determination of starch in plant tissues is described. Starch from a variety of plant tissues is solubilized by stirring for 24 h or by sonication for 40 min in dimethyl sulfoxide. Dilution of this extract to less than 20% dimethyl sulfoxide permits a nearly complete hydrolysis of the starch in less than 3 h with glucoamylase from Rhizopus niveus. Quantitation of liberated glucose by a coupled hexokinase and glucose-6-phosphate dehydrogenase method provides an additional degree of specificity.

Amylopectin↗

Preparation and application of Procion Yellow starch for amylase assay.

A new starch derivative for the determination of amylase activity has been synthesized by coupling Procion Yellow dye with starch. The product of this reaction is intensely yellow and is easily suspended in water, in neutral buffer solution, and also in acidic solution. Amylase from pancreatin, saliva, urine and serum readily hydrolyzes this chromogenic substrate. A method for determining amylase activity based on the use of Procion Yellow Starch substrate is described. The procedure requires 0.1 ml of sample and an incubation time of 30 min. The soluble chromogen, which is liberated by enzymatic hydrolysis, is measured at 420 nm and the amylase activity-absorbance relationship at this wavelength is linear. The normal range for this method is 50--150 Somogyi units/dl.

Amylases↗

Starch flavor: apparent discrimination between amylopectin and amylose by rats.

Rats given a choice between dilute suspensions of corn amylopectin and corn amylose generally preferred amylopectin. The preference threshold for amylopectin was lower than the preference threshold for amylose (0.1% and 0.5%, respectively). Two sources of evidence indicate that the difference in preference for these two types of starch is due to an off-taste component in corn amylose rather than to an ability to discriminate between amylopectin and amylose per se: 1) rats given a choice of purified amylopectin and amylose from potato did not show a significant preference, and 2) aqueous extracts of amylose reduce preference for water and amylopectin, respectively. Extensive washing of corn amylose with ammonia-methanol, water and methanol did not completely remove the off-taste of corn amylose. Despite the difference in off-taste, rats trained to avoid amylopectin also avoided amylose. It is proposed that starch has two flavor components: a component due to starch itself that induces preference, and a component due to impurities that reduces preference.

Amylopectin↗

Electron microscopic investigation of the diffusion of Bacillus licheniformis alpha-amylase into corn starch granules.

A method for the direct electron microscopic observation of amylases in interaction with starch granules is presented. The technique involves immuno-gold labeling of the enzymes and cross-sectioning of hydrated starch granules. This approach allows the analysis of the internal degradation of starch with a concomitant visualization of enzymes at the sites of hydrolysis. The visualization of enzymes at the surface, inside the channel and inside the core of the degraded granules shows that the alpha-amylase molecules first proceed from the surface toward the center (centripetal hydrolysis). Then the core is completely degraded from within by erosion of its periphery (centrifugal hydrolysis). In the first case (centripetal hydrolysis), the enzymes act by progressing along the polysaccharide chains. By contrast, the centrifugal hydrolysis leads to even erosion, indicative of a more diffusive motion of the enzymes.

Bacillus↗

Interaction of beta-cyclodextrin with the granular starch binding domain of glucoamylase.

The granular starch binding domain of glucoamylase 1 (EC 3.2.1.3 1,4-alpha-D-glucan glucohydrolase) binds two molecules of beta-cyclodextrin, with a dissociation constant (Kd) for the second ligand of 1.68 microM. The catalytic domain showed no interaction with beta-cyclodextrin. Beta-cyclodextrin competitively inhibited the adsorption of the binding domain onto granular starch with an inhibition constant (Ki) of 11.0 +/- 1.9 microM. The results show that beta-cyclodextrin binds to the binding domain of glucoamylase at the same site(s) as granular starch.

Aspergillus niger↗

Domain structure and multiplicity of raw-starch-digesting amylase from Bacillus circulans: extensive proteolysis with proteinase K, endopeptidase Glu-C and thermolysin.

Raw-starch-digesting amylase (RSDA) is a key extracellular enzyme of mesophilic Bacillus circulans F-2 which uses raw starch granules as a carbon source. Previous work has demonstrated that there are two domains of the enzyme during digestion with subtilisin, and that RSDA activity is selectively inactivated by limited proteolysis with subtilisin, which cleaves the enzyme between these hydrolytic and adsorption domains (Kim, C.-H., Kwon, S.-T., Taniguchi, H. and Lee, D.-S. (1992) Biochim. Biophys. Acta 1122, 243-250). In this work we show that a similar phenomenon is observed during limited proteinase K, thermolysin and endopeptidase Glu-C proteolysis of the enzyme. Fragments resulting from proteolysis were characterized by immunoblotting with anti-RSDA. The proteolytic patterns resulting from proteinase K and subtilisin were the same, producing 63 and 30-kDa fragments. Similar patterns were obtained with endopeptidase Glu-C or thermolysin. All proteolytic digests contained a common, major 63-kDa fragment. Inactivation of RSDA activity results from splitting off the C-terminal domain. Hence, it seems probable that the proteinase-sensitive locus is in a hinge region susceptible to cleavage. Extracellular enzymes immunoreactive towards anti-RSDA were detected through whole bacterial cultivation. 93, 75, 63, 55, 38 and 31-kDa proteins were immunologically identical to RSDA. Of these, the 75-kDa and 63-kDa proteins correspond to the major products of proteolysis with Glu-C and thermolysin. These results suggest that enzyme heterogeneity of the raw-starch hydrolysis system might arise from the endogenous proteolytic activity of the bacterium.

Amylases↗

The effect of glucose, starch, and pH on growth, enterotoxin and haemolysin production by strains of Bacillus cereus associated with food poisoning and non-gastrointestinal infection.

Brain-Heart Infusion medium, modified by (a) 1.0% w/v glucose supplement, (b) 1.0% w/v soluble starch supplement, (c) pH adjustment to 8.8 or (d) pH adjustment to 5.0, was used to investigate the influence of glucose, starch and pH on growth, enterotoxin and haemolysin production by Bacillus cereus. The four test strains selected for comparison originated from episodes of emetic-syndrome food poisoning, diarrhoeal-syndrome food poisoning, traumatic wound infection and bovine mastitis, respectively. In the presence of either glucose or starch, growth of all strains was found to be near-optimum and accompanied by enhanced enterotoxin production. However, under the moderately acid and alkaline test conditions B. cereus strains exhibited varying degrees of growth inhibition and partial repression of enterotoxin and haemolysin production. In this respect the food-poisoning isolates proved to have greater resistance to adverse pH environments than did the non-gastrointestinal infection isolates.

Animals↗

Persorption of raw starch: a cause of senile dementia?

Intact starch granules in food can pass through the intestinal wall and enter the circulation. They remain intact if they have not been cooked for long enough in the presence of water. Some of these granules embolise arterioles and capillaries. In most organs the collateral circulation suffices for continued function. In the brain, however, neurones may be lost. Over many decades the neuronal loss could be of clinical importance. To test this hypothesis, there is a need to examine brains for the presence of embolised starch granules. Examining tissues polariscopically clearly distinguishes starch granules from other objects of similar appearance.

Animals↗

Starch and sugar tastes in rodents: an update.

Rats are strongly attracted to the sweet taste of sugar. Recent behavioral studies demonstrate that rats also have a well-developed taste for starch-derived polysaccharides (e.g., Polycose). In fact, rats prefer Polycose to sucrose and other sugars at low concentrations. Polycose appetite develops at a very young age (9 days) and, thus, appears to be innate. The results of conditioned taste aversion tests suggest that rats taste Polycose as qualitatively different from sucrose. Recent electrophysiological findings support the idea that rodents have separate taste channels for polysaccharides and sugars. In particular, copper chloride suppresses the chorda tympani nerve response to sucrose and other sugars but has minimal effect on the neural response to Polycose. Also, Polycose evokes a profile of neural activity in the nucleus tractus solitarius that differs substantially from that produced by sucrose. Preliminary results indicate that polysaccharide and sugar tastes also differ in their metabolic consequences, i.e., unlike sugars, Polycose does not elicit a cephalic phase insulin response. The presumed function of polysaccharide taste is to facilitate the identification of starch-rich foods. Recent findings demonstrate that rats can readily detect starch even at low concentrations, but whether polysaccharide taste receptors or other orosensory receptors mediate this response remains to be clarified.

Animals↗

Prevention of post-ischemic brain lipid conjugated diene production and neurological injury by hydroxyethyl starch-conjugated deferoxamine.

Hydroxyethyl starch conjugated deferoxamine (DFO) was administered to rats following resuscitation from 6.5 min cardiac arrest (CA) in an attempt to prevent the iron-catalyzed production of oxygen free radicals which may lead to neurologic injury and ultimately death following restoration of spontaneous circulation (ROSC). Brain conjugated dienes were analyzed spectrophotometrically 4 and 24 hr following ROSC, and were found to be significantly elevated when compared to non-ischemic controls. Hydroxyethyl starch-DFO treated rats demonstrated no increased conjugated diene production at either period. Neurologic injury was significantly less in drug treated rats surviving 24 or 72 hours when compared to controls. While mortality was similar in drug treated or control rats for the first 24 hours following ROSC, delayed mortality (days 1-10) was significantly less in drug treated animals, presumably as a result of neurologic protection afforded by post-ischemic drug administration. Administration of DFO conjugated to hydroxyethyl starch appears to modulate the neurologic injury which occurs during brain ischemia and reperfusion.

Alkenes↗