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PubMed2003

The phosphorylation site in double helical amylopectin as investigated by a combined approach using chemical synthesis, crystallography and molecular modeling.

The only known in planta substitution of starch is phosphorylation. Whereas the function of starch phosphorylation is poorly understood, phosphorylated starch possesses improved functionality in vitro. Molecular models of native crystalline starch are currently being developed and the starch phosphorylating enzyme has recently been discovered. Accordingly, it is desirable to obtain a more exact description of the molecular structures of phosphorylated starch. We have determined the crystal structure of methyl alpha-D-glucopyranoside 6-O-phosphate as its potassium salt which is thought to be the starch phosphate counterion in vivo. From this structure and previously known glucophosphate structures we describe the possible 6-O-phosphate geometries and through modeling extrapolate the results to the double helical structure of the crystalline part of amylopectin. The geometries of the existing crystal structures of 6-O-phosphate groups were found to belong to two main adiabatic valleys. One of these conformations could be fitted into the double helical amylopectin part without perturbing the double helical amylopectin structure and without creating steric problems for the hexagonal chain-chain packing.

Amylopectin↗
PubMed2003

Effect of high temperature on fine structure of amylopectin in rice endosperm by reducing the activity of the starch branching enzyme.

Rice (Oryza sativa L.) grain quality is affected by the environmental temperature it experiences. To investigate the physiological molecular mechanisms of the effect of high temperatures on rice grain, a non-waxy indica rice was grown under two temperature conditions, (29/35 degrees C) and (22/28 degrees C), during the ripening stage in two phytotrons. The activities and gene expression of key enzymes for the biosynthesis of amylose and amylopectin were examined. The activity and expression levels of soluble endosperm starch synthase I were higher at 29/35 degrees C than that at 22/28 degrees C. In contrast, the activities and expression levels of the rice branching enzyme1, the branching enzyme3 and the granule bound starch synthase of the endosperm were lower at 29/35 degrees C than those at 22/28 degrees C. These results suggest that the decreased activity of starch branching enzyme reduces the branching frequency of the branches of amylopectin, which results in the increased amount of long chains of amylopectin of endosperm in rice grain at high temperature.

1,4-alpha-Glucan Branching Enzyme↗
PubMed2001

Amylopectin aggregation as a function of starch phosphate content studied by size exclusion chromatography and on-line refractive index and light scattering.

Starches with a natural 65-fold span in covalently bound phosphate content were prepared from five different crops including sorghum, cassava, three potato varieties and an exotic ginger plant, Curcuma zedoaria, with extreme starch phosphate content. These starches were subjected to size exclusion chromatography with refractive index detection (SEC/RI). A simple and rapid method for starch solubilisation was used. The conditions during solubilisation (2 M NaOH) and separation (10 mM NaOH, 50 degrees C) were such as enabling > 94% recovery of the starch without detectable degradation. The aggregation properties of the starch was investigated using on line refractive index/multi angle laser light scattering (RI/MALLS) detection. Three major regions in the SEC profile were identified, consisting of large amylopectin aggregates, amylopectin particles with radius of gyration (Rg) of approx 200 nm (400 nm blocklets) and amylose. A procedure for correction of light scattering signals spread over the SEC profile as a result of aggregate tailing was developed. The significance of the relative amounts of these three molecular species on standard starch pasting parameters, as measured by a Rapid Visco Analyzer (RVA), was investigated. Starches with a high amount of amylopectin aggregates showed high peak viscosities. Moreover, very high amounts of starch bound phosphate or amylose appears to suppress the content of large aggregates resulting in low viscosity.

Amylopectin↗
PubMed1999

An ESR assay for alpha-amylase activity toward succinylated starch, amylose and amylopectin.

The esterification of the three polysaccharides, starch, amylose and amylopectin was carried out in pyridine-DMSO by succinic anhydride. The carboxylic groups in the succinylated polysaccharides were measured by FT-IR spectroscopy. The succinic derivatives were tested as alpha-amylase (1,4-alpha-D-glucan glucano hydrolase, E.C. 3.2.1.1) substrates. A colorimetric assay of the alpha-amylase activity indicated that this enzyme is active on succinic esters of starch and amylose and that the activity shows a linear decrease with the number of succinic units introduced into the polysaccharide. Since the colorimetric test was not suitable for the detection of the alpha-amylase activity when succinylated amylopectin was the substrate, we set-up an assay based on the labeling by a paramagnetic probe of the free carboxylic groups of succinylated polysaccharides. The kinetics of the alpha-amylase reaction were monitored by ESR spectroscopy through the increase of the mobility of the paramagnetic probe. The spin label used was the commercially available 4-amino-tempo. By this method we demonstrated that alpha-amylase is active on succinylated amylopectin. The utility of the assay for monitoring alpha-amylase activity when other methods (i.e. colorimetric tests) fail, is discussed.

Amylopectin↗
PubMed1980

Effects of storage time and temperature on amylopectin levels and oocyst production of Eimeria meleagrimitis oocysts.

Eimeria meleagrimitis oocysts were stored at 4, 22, 32, or 41.5 degrees C for up to 1 year. Decreases in amylopectin levels (measured as glucose) and viability (measured as oocyst production and mortality in turkeys) of the oocysts were generally related to the length of time in storage and the storage temperature. Oocysts assayed immediately after harvest contained 58.29 +/- 0.75 micrograms of glucose/10(6) oocysts. When the oocysts were stored at 4 degree C for 162 days, the amylopectin level decreased to 65% of the original level. In oocysts stored at 22, 32 and 41.5 degrees C, amylopectin declined to approximately 20% within 162, 76, and 41 days, respectively. Oocysts stored at 4 degree C for 1 year produced more oocysts in turkeys than the original fresh isolate, but caused no mortality. Oocyst production from oocysts stored at 22 and 32 degrees C decreased gradually until, after 9 and 7 months respectively, no patent infections were produced. Oocyst production from oocysts stored at 41.5 degree C markedly reduced within 1 month and was not detected after 4 months.

Amylopectin↗
PubMedDate not supplied

Amylopectin molecular structure reflected in macromolecular organization of granular starch.

For lintners with negligible amylose retrogradation, crystallinity related inversely to starch amylose content and, irrespective of starch source, incomplete removal of amorphous material was shown. The latter was more pronounced for B-type than for A-type starches. The two predominant lintner populations, with modal degrees of polymerization (DP) of 13-15 and 23-27, were best resolved for amylose-deficient and A-type starches. Results indicate a more specific hydrolysis of amorphous lamellae in such starches. Small-angle X-ray scattering showed a more intense 9-nm scattering peak for native amylose-deficient A-type starches than for their regular or B-type analogues. The experimental evidence indicates a lower contrasting density within the "crystalline" shells of the latter starches. A higher density in the amorphous lamellae, envisaged by the lamellar helical model, explains the relative acid resistance of linear amylopectin chains with DP > 20, observed in lintners of B-type starches. Because amylopectin chain length distributions were similar for regular and amylose-deficient starches of the same crystal type, we deduce that the more dense (and ordered) packing of double helices into lamellar structures in amylose-deficient starches is due to a different amylopectin branching pattern.

Amylopectin↗
PubMed2005

Influence of amylopectin structure and amylose content on the gelling properties of five cultivars of cassava starches.

Five cassava genotypes were investigated to identify the fine amylopectin structures and granule chemical compositions, which differentiated the starches into high (T(o) = 63.7 degrees C on average) and low (57.3 degrees C on average) gelatinization temperatures. The amylose contents (15.9-22.4%) and granular dimensions (12.9-17.2 microm) significantly differed among the starches. Diverse amylopectin structural elements resulted in significant swelling power, viscoelastic properties, and gel firmness. Debranched starches revealed a trimodal amylopectin distribution of three fractions: FIII (DP 12), FII (DP 24.31), and FI (DP 63) and FIII (DP 12), FII (DP 24.69), and FI (DP 67) for the low and high gelatinization starch groups, respectively. The higher proportion of FI long chain entanglement with amylose chain lengths to form longer helical structures was confirmed in the high gelatinization starch group, which developed "true" gels with better shear resistance, frequency independence, and higher gel firmness. Significant amounts of resistant starch fractions revealed the potential for application of these genotype starches in diverse foods.

Amylopectin↗
PubMed2006

Soluble starch synthase I effects differences in amylopectin structure between indica and japonica rice varieties.

The effect of soluble starch synthase I (SSI) on differences of amylopectin structure between the indica and japonica rice varieties was investigated. Native-PAGE/active staining analysis showed that the SSI activity of an indica rice variety, "Kasalath", was significantly lower than that of a japonica rice variety, "Nipponbare", and that the low activity in "Kasalath" was maintained during seed development. The result of northern blot analyses suggests that the low expression of SSI in "Kasalath" is controlled at the transcription levels of SSI mRNA. Chain length distribution of amylopectin in F3 endosperms derived from a cross between two varieties showed that not only SSIIa but also SSI regulated the population of short chains. These results indicate that the low activity of SSI gives rise to the decrease of short chains in amylopectin of indica rice varieties, suggesting that SSI effects the differences in physicochemical properties between two varieties.

Amylopectin↗
PubMed1989

Diets containing high amylose vs amylopectin starch: effects on metabolic variables in human subjects.

Twelve men consumed a diet containing 34% of calories as 70% amylose or amylopectin starch to determine if the structure of starch could influence metabolic factors associated with abnormal states. Each starch was fed to subjects for 5 wk in a crossover design. No significant differences were observed in glucose or insulin levels when a glucose tolerance was given after 4 wk on each starch. However, glucose and insulin responses were significantly lower when a meal containing amylose compared with amylopectin was consumed after 5 wk on each starch. Summation of 0.5 through 2-h levels of insulin but not glucose were significantly lower after amylose compared with levels after amylopectin. Mean fasting triglyceride and cholesterol levels were significantly lower during the period when amylose was consumed. Long-term intake of dietary amylose may be valuable in decreasing insulin response while maintaining proper control of glucose tolerance and low levels of blood lipids.

Adult↗
PubMed2005

Amylopectin induces fumonisin B1 production by Fusarium verticillioides during colonization of maize kernels.

Fusarium verticillioides, a fungal pathogen of maize, produces fumonisin mycotoxins that adversely affect human and animal health. Basic questions remain unanswered regarding the interactions between the host plant and the fungus that lead to the accumulation of fumonisins in maize kernels. In this study, we evaluated the role of kernel endosperm composition in regulating fumonisin B1 (FB1) biosynthesis. We found that kernels lacking starch due to physiological immaturity did not accumulate FB1. Quantitative polymerase chain reaction analysis indicated that kernel development also affected the expression of fungal genes involved in FB1 biosynthesis, starch metabolism, and nitrogen regulation. A mutant strain of F. verticillioides with a disrupted a-amylase gene was impaired in its ability to produce FB1 on starchy kernels, and both the wild-type and mutant strains produced significantly less FB1 on a high-amylose kernel mutant of maize. When grown on a defined medium with amylose as the sole carbon source, the wild-type strain produced only trace amounts of FB1, but it produced large amounts of FB1 when grown on amylopectin or dextrin, a product of amylopectin hydrolysis. We conclude that amylopectin induces FB1 production in F. verticillioides. This study provides new insight regarding the interaction between the fungus and maize kernel during pathogenesis and highlights important areas that need further study.

Amylopectin↗
PubMed2004

Complementation of sugary-1 phenotype in rice endosperm with the wheat isoamylase1 gene supports a direct role for isoamylase1 in amylopectin biosynthesis.

To examine the role of isoamylase1 (ISA1) in amylopectin biosynthesis in plants, a genomic DNA fragment from Aegilops tauschii was introduced into the ISA1-deficient rice (Oryza sativa) sugary-1 mutant line EM914, in which endosperm starch is completely replaced by phytoglycogen. A. tauschii is the D genome donor of wheat (Triticum aestivum), and the introduced fragment effectively included the gene for ISA1 for wheat (TaISA1) that was encoded on the D genome. In TaISA1-expressing rice endosperm, phytoglycogen synthesis was substantially replaced by starch synthesis, leaving only residual levels of phytoglycogen. The levels of residual phytoglycogen present were inversely proportional to the expression level of the TaISA1 protein, although the level of pullulanase that had been reduced in EM914 was restored to the same level as that in the wild type. Small but significant differences were found in the amylopectin chain-length distribution, gelatinization temperatures, and A-type x-ray diffraction patterns of the starches from lines expressing TaISA1 when compared with wild-type rice starch, although in the first two parameters, the effect was proportional to the expression level of TaISA. The impact of expression levels of ISA1 on starch structure and properties provides support for the view that ISA1 is directly involved in the synthesis of amylopectin.

Amylopectin↗
PubMed2005

Mutants of Arabidopsis lacking a chloroplastic isoamylase accumulate phytoglycogen and an abnormal form of amylopectin.

Mutant lines defective for each of the four starch debranching enzyme (DBE) genes (AtISA1, AtISA2, AtISA3, and AtPU1) detected in the nuclear genome of Arabidopsis (Arabidopsis thaliana) were produced and analyzed. Our results indicate that both AtISA1 and AtISA2 are required for the production of a functional isoamylase-type of DBE named Iso1, the major isoamylase activity found in leaves. The absence of Iso1 leads to an 80% decrease in the starch content in both lines and to the accumulation of water-soluble polysaccharides whose structure is similar to glycogen. In addition, the residual amylopectin structure in the corresponding mutant lines displays a strong modification when compared to the wild type, suggesting a direct, rather than an indirect, function of Iso1 during the synthesis of amylopectin. Mutant lines carrying a defect in AtISA3 display a strong starch-excess phenotype at the end of both the light and the dark phases accompanied by a small modification of the amylopectin structure. This result suggests that this isoamylase-type of DBE plays a major role during starch mobilization. The analysis of the Atpu1 single-mutant lines did not lead to a distinctive phenotype. However, Atisa2/Atpu1 double-mutant lines display a 92% decrease in starch content. This suggests that the function of pullulanase partly overlaps that of Iso1, although its implication remains negligible when Iso1 is present within the cell.

Amylases↗
PubMed1992

Waxy Chlamydomonas reinhardtii: monocellular algal mutants defective in amylose biosynthesis and granule-bound starch synthase activity accumulate a structurally modified amylopectin.

Amylose-defective mutants were selected after UV mutagenesis of Chlamydomonas reinhardtii cells. Two recessive nuclear alleles of the ST-2 gene led to the disappearance not only of amylose but also of a fraction of the amylopectin. Granule-bound starch synthase activities were markedly reduced in strains carrying either st-2-1 or st-2-2, as is the case for amylose-deficient (waxy) endosperm mutants of higher plants. The main 76-kDa protein associated with the starch granule was either missing or greatly diminished in both mutants, while st-2-1-carrying strains displayed a novel 56-kDa major protein. Methylation and nuclear magnetic resonance analysis of wild-type algal storage polysaccharide revealed a structure identical to that of higher-plant starch, while amylose-defective mutants retained a modified amylopectin fraction. We thus propose that the waxy gene product conditions not only the synthesis of amylose from endosperm storage tissue in higher-plant amyloplasts but also that of amylose and a fraction of amylopectin in all starch-accumulating plastids. The nature of the ST-2 (waxy) gene product with respect to the granule-bound starch synthase activities is discussed.

Alleles↗
PubMed1977

[Cytochemical study of different stages in the life cycle of Toxoplasma gondii. I. Amylopectin and lipids in endozoites].

Attempts were made to localize cytochemically acid micopolysaccharides, in addition to sulphate groups of mucosubstances in Toxoplasma endozoites of SS-119 and RH strains with negative results. Amylopectin was found to be the only polysaccharide so far detected in the endozoite stage, using the PAS technique. With RH strain toxoplasmas, the dynamics of amylopectin was followed within 6 days after mouse inoculation. On day 2, toxoplasmas and the host cells of the mouse peritoneal exudate being practically PAS-negative, the amount of amylopectin increased progressively towards day 6. The immune response of the host may be presumably involved in the pattern of this dynamics. Phospholipids were detected in the cytoplasm of intra- and extracellular endozoites of strain SS-119. Little, if any, amount of neutral fat was observed. Of special interest is the increased phospholipid content in the infected host cells.

Amylopectin↗
PubMed2002

Mapping of a gene responsible for the difference in amylopectin structure between japonica-type and indica-type rice varieties.

The present investigation revealed that the alk and gel(t) genes, which cause the differences between a japonica rice variety Nipponbare and an indica rice variety Kasalath in terms of the disintegration of endosperm starch granules in alkali solution and their gelatinisation in a 4 M urea solution, respectively, cosegregated in backcross inbred lines derived from a cross between the two varieties. The segregation pattern of the profile for amylopectin chain-length, which was distinguished by enrichment in short chains of DP<==11 and depletion in intermediate-size chains of 12<==DP<==24 in japonica as compared with indica, was exactly the same as those of the above physico-chemical properties of starch granules, and the gene was designated as acl(t). Gene-mapping analysis showed that the starch synthase IIa ( SSIIa) gene is located at the alk locus on chromosome 6 in the rice genome. These results lead us to the possibility that different alleles of the SSIIa gene are responsible for differences in amylopectin structure between the two varieties, in that SSIIa plays a distinct role in the elongation of short chains within clusters (A+B(1) chains) of amylopectin. It is proposed that the activity of SSIIa in japonica rice is reduced in amount or functional capacity relative to the activity of this enzyme in indica rice. This, in turn, would explain why starch from japonica rice has a lower gelatinisation temperature than starch from indica rice and is more susceptible to disintegration in alkali or urea. The evidence for this hypothesis is that the alk(t), gel(t), acl(t) and SSIIa genes all map to the same locus.

Journal Article↗
PubMed1999

The starch-debranching enzymes isoamylase and pullulanase are both involved in amylopectin biosynthesis in rice endosperm

The activities of the two types of starch debranching enzymes, isoamylase and pullulanase, were greatly reduced in endosperms of allelic sugary-1 mutants of rice (Oryza sativa), with the decrease more pronounced for isoamylase than for pullulanase. However, the decrease in isoamylase activity was not related to the magnitude of the sugary phenotype (the proportion of the phytoglycogen region of the endosperm), as observed with pullulanase. In the moderately mutated line EM-5, the pullulanase activity was markedly lower in the phytoglycogen region than in the starch region, and isoamylase activity was extremely low or completely lost in the whole endosperm tissue. These results suggest that both debranching enzymes are involved in amylopectin biosynthesis in rice endosperm. We presume that isoamylase plays a predominant role in amylopectin synthesis, but pullulanase is also essential or can compensate for the role of isoamylase in the construction of the amylopectin multiple-cluster structure. It is highly possible that isoamylase was modified in some sugary-1 mutants such as EM-273 and EM-5, since it was present in significant and trace amounts, respectively, in these mutants but was apparently inactive. The results show that the Sugary-1 gene encodes the isoamylase gene of the rice genome.

Journal Article↗
PubMed1978

Amylopectin degradation in pea chloroplast extracts.

Phosphorolysis rather than phosphorylation of amylolysis products was found to be the major pathway of sugar phosphate formation from amylopectin by pea (Pisum sativum L.) chloroplast stromal proteins. The K(m) for inorganic phosphate incorporation was 2.5 mm, and ATP did not stimulate amylopectin-dependent phosphate incorporation. Arsenate (10 mm) inhibited phosphate incorporation into glucose monophosphates up to 46% and phosphoglucomutase activity 96%, resulting in glucose 1-phosphate accumulation as a product of amylopectin degradation. The intracellular distribution of enzymes of starch utilization was determined. Phosphorylase, phosphoglucomutase, and hexokinase were found in the chloroplast and cytoplasm, while beta-amylase was restricted to the cytoplasm. Maltase was not detectable; maltose phosphorylase was active in the chloroplast.

Journal Article↗
PubMed1999

A monoclonal antibody reacts species-specifically with amylopectin granules of Eimeria bovis merozoites.

An IgG1 monoclonal antibody (mAb 35B9) developed against first-generation merozoites of Eimeria bovis was shown by immunoelectron microscopy to react selectively with antigens localized in amylopectin granules. Amylopectin does not contribute to the epitope, as enzymatic degradation of carbohydrates in the parasite did not alter the binding pattern of mAb 35B9. When tested by immunoblotting, despite its organelle specificity the mAb recognized a variety of E. bovis merozoite I components with predominant molecules of 135 and 200 kDa. The epitope was not affected by treatment with endoglycosidase H; thus, N-linked sugar residues should not be involved in it. Alkaline cleavage (beta-elimination), however, destroyed the epitope; thus, the involvement of O-linked carbohydrates cannot be excluded. Treatment of E. bovis merozoite extract with phospholipase C changed the binding pattern of mAb 35B9 in a way that suggests the presence of phosphorylcholine molecules on several antigens recognized by the mAb, albeit not belonging to the epitope but rather masking it. The epitope was not found in free sporozoites of E. bovis or young intracellular parasites up to day 4 after invasion of cells in vitro, whereas 5-day-old trophozoites were found to contain it. It seems to be species-specific, as it could not be shown in sporozoites or merozoites of E. tenella or in stages of several other Coccidia.

Amylopectin↗