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Journal articles on the topic 'Maltosine'

Author: Grafiati

Published: 4 June 2021

Last updated: 5 February 2022

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1

Ledl, Franz, Helga Osiander, Otto Pachmayr, and Theodor Severin. "Formation of maltosine, a product of the Maillard reaction with a pyridone structure." Zeitschrift für Lebensmittel-Untersuchung und -Forschung 188, no. 3 (March 1989): 207–11. http://dx.doi.org/10.1007/bf02112876.

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2

Geissler, Stefanie, Michael Hellwig, Fritz Markwardt, Thomas Henle, and Matthias Brandsch. "Synthesis and intestinal transport of the iron chelator maltosine in free and dipeptide form." European Journal of Pharmaceutics and Biopharmaceutics 78, no. 1 (May 2011): 75–82. http://dx.doi.org/10.1016/j.ejpb.2010.12.032.

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3

Hellwig, Michael, Magdalena Kiessling, Sandra Rother, and Thomas Henle. "Quantification of the glycation compound 6-(3-hydroxy-4-oxo-2-methyl-4(1H)-pyridin-1-yl)-l-norleucine (maltosine) in model systems and food samples." European Food Research and Technology 242, no. 4 (October 7, 2015): 547–57. http://dx.doi.org/10.1007/s00217-015-2565-0.

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4

Shashkov, Alexander S., Grigory M. Lipkind, and Nikolay K. Kochetkov. "Nuclear overhauser effects for methyl β-maltoside and the conformational states of maltose in aqueous solution." Carbohydrate Research 147, no. 2 (March 1986): 175–82. http://dx.doi.org/10.1016/s0008-6215(00)90628-1.

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5

Ferrer, Manuel, M. Angeles Cruces, Francisco J. Plou, Manuel Bernabé, and Antonio Ballesteros. "A Simple Procedure for the Regioselective Synthesis of Fatty Acid Esters of Maltose, Leucrose, Maltotriose and n-Dodecyl Maltosides." Tetrahedron 56, no. 24 (June 2000): 4053–61. http://dx.doi.org/10.1016/s0040-4020(00)00319-7.

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6

Hamid, Hairul A. A., Rauzah Hashim, John M. Seddon, and Nicholas J. Brooks. "Lyotropic Phase Behaviour and Structural Parameters of Monosaccharide and Disaccharide Guerbet Branched-Chain β-D-Glycosides." Advanced Materials Research 895 (February 2014): 111–15. http://dx.doi.org/10.4028/www.scientific.net/amr.895.111.

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The phase behaviour and self-assembly structural parameters of a pair of monosaccharide and disaccharide Guerbet branched-chain β-D-glycosides, namely 2-octyldodecyl β-D-glucoside (β-Glc-C12C8) and 2-octyldodecyl β-D-maltoside (β-Mal-C12C8), have been studied by means of optical polarizing microscopy (OPM) and small-angle X-ray diffraction at room temperature (25°C). These compounds are sugar-based glycolipid surfactants having a total chain length of C20, and differ based on the increasing number of hydroxyl groups of the sugar headgroup (glucose and maltose). The repeat spacings obtained by X-ray diffraction as a function of water content have been used to determine the limiting hydration for the two glycosides. At room temperature, β-Glc-C12C8 and β-Mal-C12C8 have limiting hydrations of 22 wt% and 25 wt%, corresponding to 8 10 and 10 12 water molecules per glycoside, respectively. At all water contents between 5 and 29 wt % water, these compounds adopt inverse hexagonal (HII) or fluid lamellar (Lα) phases. The structural parameters of these phases have been determined from the diffraction data, from the X-ray repeat spacings, densities and concentration of the glycosides.

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7

Reyes, M., N. A. Treptow, and H. A. Shuman. "Transport of p-nitrophenyl-alpha-maltoside by the maltose transport system of Escherichia coli and its subsequent hydrolysis by a cytoplasmic alpha-maltosidase." Journal of Bacteriology 165, no. 3 (1986): 918–22. http://dx.doi.org/10.1128/jb.165.3.918-922.1986.

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8

Katsuragi, Hisashi, Kei Shimoda, Eriko Kimura, and Hiroki Hamada. "Synthesis of Capsaicin Glycosides and 8-Nordihydrocapsaicin Glycosides as Potential Weight-Loss Formulations." Biochemistry Insights 3 (January 2010): BCI.S2676. http://dx.doi.org/10.4137/bci.s2676.

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The enzymatic synthesis of capsaicin glycosides and 8-nordihydrocapsaicin glycosides was investigated using almond β-glucosidase and cyclodextrin glucanotransferase (CGTase). Capsaicin and 8-nordihydrocapsaicin were converted into their β-glucoside and β-maltooligosaccharide (amylose conjugate), i.e. β-maltoside and β-maltotrioside, by sequencial glycosylation with almond β-glucosidase and CGTase. The β-glucoside and β-maltoside of capsaicin and β-glucoside of 8-nordihydrocapsaicin showed inhibitory effects on high-fat-diet-induced elevations in body weight of mice.

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9

Wang, Xin, Mehtap Bali, Igor Medintz, and Corinne A. Michels. "Intracellular Maltose Is Sufficient To Induce MAL Gene Expression in Saccharomyces cerevisiae." Eukaryotic Cell 1, no. 5 (October 2002): 696–703. http://dx.doi.org/10.1128/ec.1.5.696-703.2002.

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ABSTRACT The presence of maltose induces MAL gene expression in Saccharomyces cells, but little is known about how maltose is sensed. Strains with all maltose permease genes deleted are unable to induce MAL gene expression. In this study, we examined the role of maltose permease in maltose sensing by substituting a heterologous transporter for the native maltose permease. PmSUC2 encodes a sucrose transporter from the dicot plant Plantago major that exhibits no significant sequence homology to maltose permease. When expressed in Saccharomyces cerevisiae, PmSUC2 is capable of transporting maltose, albeit at a reduced rate. We showed that introduction of PmSUC2 restores maltose-inducible MAL gene expression to a maltose permease-null mutant and that this induction requires the MAL activator. These data indicate that intracellular maltose is sufficient to induce MAL gene expression independently of the mechanism of maltose transport. By using strains expressing defective mal61 mutant alleles, we demonstrated a correlation between the rate of maltose transport and the level of the induction, which is particularly evident in medium containing very limiting concentrations of maltose. Moreover, our results indicate that a rather low concentration of intracellular maltose is needed to trigger MAL gene expression. We also showed that constitutive overexpression of either MAL61 maltose permease or PmSUC2 suppresses the noninducible phenotype of a defective mal13 MAL-activator allele, suggesting that this suppression is solely a function of maltose transport activity and is not specific to the sequence of the permease. Our studies indicate that maltose permease does not function as the maltose sensor in S. cerevisiae.

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10

Rouse, Sarah L., Julien Marcoux, Carol V. Robinson, and Mark S. P. Sansom. "Dodecyl Maltoside Protects Membrane Proteins In Vacuo." Biophysical Journal 105, no. 3 (August 2013): 648–56. http://dx.doi.org/10.1016/j.bpj.2013.06.025.

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11

Hamada, Hiroki, Hatsuyuki Hamada, Kei Shimoda, Tadakatsu Mandai, Kohji Ishihara, Yuya Kiriake, and Atsuhito Kuboki. "Synthesis of Ester-Linked Paclitaxel-Glycoside Conjugate as a Water-Soluble Paclitaxel Derivative—Maltoside Modification of Paclitaxel through Ester-Linker (Ester-Spacer)." Natural Product Communications 16, no. 9 (September 2021): 1934578X2110387. http://dx.doi.org/10.1177/1934578x211038788.

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To synthesize a water-soluble paclitaxel derivative, the anomers of diols of allyl 2,3,4-tri- O-benzyl-6- O-tritylglycoside (maltoside) were prepared, which can be separated by chromatographic procedure. One anomer was converted into α-glycosyloxyacetic acid (maltosyloxyacetic acid) by oxidative cleavage of the diol and subsequent oxidation. Ester-linked paclitaxel-glycoside conjugate, 7-glycolylpaclitaxel 2″- O-α-maltoside, was provided by condensation of 2′-TES paclitaxel with α-glycosyloxyacetic acid (maltosyloxyacetic acid) followed by deprotection of hydroxy groups.

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12

Kuile, B. H. Ter, and M. Müller. "Maltose utilization by extracellular hydrolysis followed by glucose transport in Trichomonas vaginalis." Parasitology 110, no. 1 (January 1995): 37–44. http://dx.doi.org/10.1017/s0031182000081026.

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The amitochondriate parasitic protist Trichomonas vaginalis can utilize either glucose or maltose as carbon and energy source. The mechanisms of maltose utilization were explored with uptake experiments using radio-isotope labelled maltose in combination with the silicone-oil centrifugation technique and enzymatic assays measuring maltose hydrolysis. The uptake of maltose label became saturated after 2–3 h. The uptake of maltose as a function of the external maltose concentration was linear at low concentrations with no further increase at higher levels, kinetics characteristic of reactions obeying Michaelis–Menten kinetics preceded by a diffusion-limited step. Increased viscosity of the medium resulted in decreased maltose uptake, indicating an extracellular location of the diffusion-limited step. Most of the cellular α-glucosidase activity of T. vaginalis was detected on the cell surface, suggesting that maltose is hydrolysed to glucose outside the cell. Glucose interfered more with maltose uptake, and maltose less with glucose uptake, than would be expected if 1 mol of maltose were the equivalent of 2 mol of glucose. This pattern of interaction indicated that the interference occurs before the common metabolic pathway and even before the transport step, supporting the idea of extracellular maltose hydrolysis. We conclude that maltose is hydrolysed to glucose in the boundary layer of the cell, a process akin to membrane digestion in vertebrate enterocytes and on the teguments of helminths. The glucose formed is then transported by the glucose carrier of the organism.

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13

Jansen, Mickel L. A., Pascale Daran-Lapujade, Johannes H. de Winde, Matthew D. W. Piper, and Jack T. Pronk. "Prolonged Maltose-Limited Cultivation of Saccharomyces cerevisiae Selects for Cells with Improved Maltose Affinity and Hypersensitivity." Applied and Environmental Microbiology 70, no. 4 (April 2004): 1956–63. http://dx.doi.org/10.1128/aem.70.4.1956-1963.2004.

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ABSTRACT Prolonged cultivation (>25 generations) of Saccharomyces cerevisiae in aerobic, maltose-limited chemostat cultures led to profound physiological changes. Maltose hypersensitivity was observed when cells from prolonged cultivations were suddenly exposed to excess maltose. This substrate hypersensitivity was evident from massive cell lysis and loss of viability. During prolonged cultivation at a fixed specific growth rate, the affinity for the growth-limiting nutrient (i.e., maltose) increased, as evident from a decreasing residual maltose concentration. Furthermore, the capacity of maltose-dependent proton uptake increased up to 2.5-fold during prolonged cultivation. Genome-wide transcriptome analysis showed that the increased maltose transport capacity was not primarily due to increased transcript levels of maltose-permease genes upon prolonged cultivation. We propose that selection for improved substrate affinity (ratio of maximum substrate consumption rate and substrate saturation constant) in maltose-limited cultures leads to selection for cells with an increased capacity for maltose uptake. At the same time, the accumulative nature of maltose-proton symport in S. cerevisiae leads to unrestricted uptake when maltose-adapted cells are exposed to a substrate excess. These changes were retained after isolation of individual cell lines from the chemostat cultures and nonselective cultivation, indicating that mutations were involved. The observed trade-off between substrate affinity and substrate tolerance may be relevant for metabolic engineering and strain selection for utilization of substrates that are taken up by proton symport.

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14

Higgins, Vincent J., Mark Braidwood, Phil Bell, Peter Bissinger, Ian W. Dawes, and Paul V. Attfield. "Genetic Evidence That High Noninduced Maltase and Maltose Permease Activities, Governed by MALx3-Encoded Transcriptional Regulators, Determine Efficiency of Gas Production by Baker’s Yeast in Unsugared Dough." Applied and Environmental Microbiology 65, no. 2 (February 1, 1999): 680–85. http://dx.doi.org/10.1128/aem.65.2.680-685.1999.

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ABSTRACT Strain selection and improvement in the baker’s yeast industry have aimed to increase the speed of maltose fermentation in order to increase the leavening activity of industrial baking yeast. We identified two groups of baker’s strains of Saccharomyces cerevisiae that can be distinguished by the mode of regulation of maltose utilization. One group (nonlagging strains), characterized by rapid maltose fermentation, had at least 12-fold more maltase and 130-fold-higher maltose permease activities than maltose-lagging strains in the absence of inducing sugar (maltose) and repressing sugar (glucose). Increasing the noninduced maltase activity of a lagging strain 13-fold led to an increase in CO2 production in unsugared dough. This increase in CO2 production also was seen when the maltose permease activity was increased 55-fold. Only when maltase and maltose permease activities were increased in concert was CO2 production by a lagging strain similar to that of a nonlagging strain. The noninduced activities of maltase and maltose permease constitute the largest determinant of whether a strain displays a nonlagging or a lagging phenotype and are dependent upon theMALx3 allele. Previous strategies for strain improvement have targeted glucose derepression of maltase and maltose permease expression. Our results suggest that increasing noninduced maltase and maltose permease levels is an important target for improved maltose metabolism in unsugared dough.

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15

SEELERT, Holger, Ansgar POETSCH, Meino ROHLFS, and Norbert A. DENCHER. "Dye-ligand chromatographic purification of intact multisubunit membrane protein complexes: application to the chloroplast H+-F0F1-ATP synthase." Biochemical Journal 346, no. 1 (February 8, 2000): 41–44. http://dx.doi.org/10.1042/bj3460041.

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n-Dodecyl-β-D-maltoside was used as a detergent to solubilize the ammonium sulphate precipitate of chloroplast FOF1-ATP synthase, which was purified further by dye-ligand chromatography. Upon reconstitution of the purified protein complex into phosphatidylcholine/phosphatidic acid liposomes, ATP synthesis, driven by an artificial ∆pH/∆ψ, was observed. The highest activity was achieved with ATP synthase solubilized in n-dodecyl-β-D-maltoside followed by chromatography with Red 120 dye. The optimal dye for purification with CHAPS was Green 5. All known subunits were present in the monodisperse proton-translocating ATP synthase preparation obtained from chloroplasts.

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16

Palevsky, Paul M. "Maltose-Induced Hyponatremia." Annals of Internal Medicine 118, no. 7 (April 1, 1993): 526. http://dx.doi.org/10.7326/0003-4819-118-7-199304010-00007.

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17

Flegler, Vanessa Judith, Akiko Rasmussen, Karina Borbil, Lea Boten, Hsuan-Ai Chen, Hanna Deinlein, Julia Halang, et al. "Mechanosensitive channel gating by delipidation." Proceedings of the National Academy of Sciences 118, no. 33 (August 10, 2021): e2107095118. http://dx.doi.org/10.1073/pnas.2107095118.

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The mechanosensitive channel of small conductance (MscS) protects bacteria against hypoosmotic shock. It can sense the tension in the surrounding membrane and releases solutes if the pressure in the cell is getting too high. The membrane contacts MscS at sensor paddles, but lipids also leave the membrane and move along grooves between the paddles to reside as far as 15 Å away from the membrane in hydrophobic pockets. One sensing model suggests that a higher tension pulls lipids from the grooves back to the membrane, which triggers gating. However, it is still unclear to what degree this model accounts for sensing and what contribution the direct interaction of the membrane with the channel has. Here, we show that MscS opens when it is sufficiently delipidated by incubation with the detergent dodecyl-β-maltoside or the branched detergent lauryl maltose neopentyl glycol. After addition of detergent-solubilized lipids, it closes again. These results support the model that lipid extrusion causes gating: Lipids are slowly removed from the grooves and pockets by the incubation with detergent, which triggers opening. Addition of lipids in micelles allows lipids to migrate back into the pockets, which closes the channel even in the absence of a membrane. Based on the distribution of the aliphatic chains in the open and closed conformation, we propose that during gating, lipids leave the complex on the cytosolic leaflet at the height of highest lateral tension, while on the periplasmic side, lipids flow into gaps, which open between transmembrane helices.

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18

Zhang, Lei, P. Somasundaran, and C. Maltesh. "Adsorption ofn-Dodecyl-β-d-maltoside on Solids." Journal of Colloid and Interface Science 191, no. 1 (July 1997): 202–8. http://dx.doi.org/10.1006/jcis.1997.4923.

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19

Jaramillo, Carlos, Alfonso Fernandez-Mayoralas, and Manuel Martin-Lomas. "Acetonation of methyl β-maltoside with 2-methoxypropene." Carbohydrate Research 182, no. 1 (October 1988): 153–59. http://dx.doi.org/10.1016/0008-6215(88)84100-4.

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20

Mandal, Taraknath, and Ronald G. Larson. "Prediction of striped cylindrical micelles (SCMs) formed by dodecyl-β-d-maltoside (DDM) surfactants." Soft Matter 14, no. 14 (2018): 2694–700. http://dx.doi.org/10.1039/c8sm00274f.

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21

Wagner, Michaela, Alexander Wagner, Xiaoqing Ma, Julia Christin Kort, Abhrajyoti Ghosh, Bernadette Rauch, Bettina Siebers, and Sonja-Verena Albers. "Investigation of themalEPromoter and MalR, a Positive Regulator of the Maltose Regulon, for an Improved Expression System in Sulfolobus acidocaldarius." Applied and Environmental Microbiology 80, no. 3 (November 22, 2013): 1072–81. http://dx.doi.org/10.1128/aem.03050-13.

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ABSTRACTIn this study, the regulator MalR (Saci_1161) of the TrmB family fromSulfolobus acidocaldariuswas identified and was shown to be involved in transcriptional control of the maltose regulon (Saci_1660 to Saci_1666), including the ABC transporter (malEFGK), α-amylase (amyA), and α-glycosidase (malA). The ΔmalRdeletion mutant exhibited a significantly decreased growth rate on maltose and dextrin but not on sucrose. The expression of the genes organized in the maltose regulon was induced only in the presence of MalR and maltose in the growth medium, indicating that MalR, in contrast to its TrmB and TrmB-like homologues, is an activator of the maltose gene cluster. Electrophoretic mobility shift assays revealed that the binding of MalR tomalEwas independent of sugars. Here we report the identification of the archaeal maltose regulator protein MalR, which acts as an activator and controls the expression of genes involved in maltose transport and metabolic conversion inS. acidocaldarius, and its use for improvement of theS. acidocaldariusexpression system under the control of an optimized maltose binding protein (malE) promoter by promoter mutagenesis.

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22

Jones, C. R., M. Ray, K. A. Dawson, and H. J. Strobel. "High-Affinity Maltose Binding and Transport by the Thermophilic Anaerobe Thermoanaerobacter ethanolicus 39E." Applied and Environmental Microbiology 66, no. 3 (March 1, 2000): 995–1000. http://dx.doi.org/10.1128/aem.66.3.995-1000.2000.

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ABSTRACT Thermoanaerobacter ethanolicus is a gram-positive thermophile that produces considerable amounts of ethanol from soluble sugars and polymeric substrates, including starch. Growth on maltose, a product of starch hydrolysis, was associated with the production of a prominent membrane-associated protein that had an apparent molecular weight of 43,800 and was not detected in cells grown on xylose or glucose. Filter-binding assays revealed that cell membranes bound maltose with high affinity. Metabolic labeling ofT. ethanolicus maltose-grown cells with [14C]palmitic acid showed that this protein was posttranslationally acylated. A maltose-binding protein was purified by using an amylose resin affinity column, and the binding constant was 270 nM. Since maltase activity was found only in the cytosol of fractionated cells and unlabeled glucose did not compete with radiolabeled maltose for uptake in whole cells, it appeared that maltose was transported intact. In whole-cell transport assays, the affinity for maltose was approximately 40 nM. Maltotriose and α-trehalose competitively inhibited maltose uptake in transport assays, whereas glucose, cellobiose, and a range of disaccharides had little effect. Based on these results, it appears that T. ethanolicus possesses a high-affinity, ABC type transport system that is specific for maltose, maltotriose, and α-trehalose.

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23

Dippel, Renate, and Winfried Boos. "The Maltodextrin System of Escherichia coli: Metabolism and Transport." Journal of Bacteriology 187, no. 24 (December 15, 2005): 8322–31. http://dx.doi.org/10.1128/jb.187.24.8322-8331.2005.

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ABSTRACT The maltose/maltodextrin regulon of Escherichia coli consists of 10 genes which encode a binding protein-dependent ABC transporter and four enzymes acting on maltodextrins. All mal genes are controlled by MalT, a transcriptional activator that is exclusively activated by maltotriose. By the action of amylomaltase, we prepared uniformly labeled [14C]maltodextrins from maltose up to maltoheptaose with identical specific radioactivities with respect to their glucosyl residues, which made it possible to quantitatively follow the rate of transport for each maltodextrin. Isogenic malQ mutants lacking maltodextrin phosphorylase (MalP) or maltodextrin glucosidase (MalZ) or both were constructed. The resulting in vivo pattern of maltodextrin metabolism was determined by analyzing accumulated [14C]maltodextrins. MalP− MalZ+ strains degraded all dextrins to maltose, whereas MalP+ MalZ− strains degraded them to maltotriose. The labeled dextrins were used to measure the rate of transport in the absence of cytoplasmic metabolism. Irrespective of the length of the dextrin, the rates of transport at a submicromolar concentration were similar for the maltodextrins when the rate was calculated per glucosyl residue, suggesting a novel mode for substrate translocation. Strains lacking MalQ and maltose transacetylase were tested for their ability to accumulate maltose. At 1.8 nM external maltose, the ratio of internal to external maltose concentration under equilibrium conditions reached 106 to 1 but declined at higher external maltose concentrations. The maximal internal level of maltose at increasing external maltose concentrations was around 100 mM. A strain lacking malQ, malP, and malZ as well as glycogen synthesis and in which maltodextrins are not chemically altered could be induced by external maltose as well as by all other maltodextrins, demonstrating the role of transport per se for induction.

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24

Tarigan, Daniel. "SYNTHESIS OF SURFACTANS DILAUROYL MALTOSE THROUGH ACETILATION REACTION OF MALTOSE FOLLOWED BY TRANSESTERIFICATION REACTION WITH METHYL LAURATE." Indonesian Journal of Chemistry 9, no. 3 (June 24, 2010): 445–51. http://dx.doi.org/10.22146/ijc.21513.

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Maltose has been partially acetylated from the reaction of melted maltose and acetic anhydride without solvent and catalyst to produce maltocyl acetate with the yield of 67%. Lauryc acid can be methanolized using H2SO4 as the catalyst to produce methyl laurate with the yield of 92%. The transesterification of methyl laurate and maltocyl acetate in methanol using sodium methoxyde as the catalyst at reflux, yielded a novel compound dilauroyl maltose after isolated by column chromatography, with the yield of 59%. Methyl laurate, maltocyl acetate, and dilauroyl maltose were confirmed by FT-IR and 'H-NMR spectroscopy, and the surface tension of dilauroyl maltose solution was determined by Du-Nuoy tensiometer to obtain the HLB value of 2.67. Keywords: Surfactant Transesterification, Maltose

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25

Hu, Zhen, Yingzi Yue, Hua Jiang, Bin Zhang, Peter W. Sherwood, and Corinne A. Michels. "Analysis of the Mechanism by Which Glucose Inhibits Maltose Induction of MAL Gene Expression in Saccharomyces." Genetics 154, no. 1 (January 1, 2000): 121–32. http://dx.doi.org/10.1093/genetics/154.1.121.

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Abstract Expression of the MAL genes required for maltose fermentation in Saccharomyces cerevisiae is induced by maltose and repressed by glucose. Maltose-inducible regulation requires maltose permease and the MAL-activator protein, a DNA-binding transcription factor encoded by MAL63 and its homologues at the other MAL loci. Previously, we showed that the Mig1 repressor mediates glucose repression of MAL gene expression. Glucose also blocks MAL-activator-mediated maltose induction through a Mig1p-independent mechanism that we refer to as glucose inhibition. Here we report the characterization of this process. Our results indicate that glucose inhibition is also Mig2p independent. Moreover, we show that neither overexpression of the MAL-activator nor elimination of inducer exclusion is sufficient to relieve glucose inhibition, suggesting that glucose acts to inhibit induction by affecting maltose sensing and/or signaling. The glucose inhibition pathway requires HXK2, REG1, and GSF1 and appears to overlap upstream with the glucose repression pathway. The likely target of glucose inhibition is Snf1 protein kinase. Evidence is presented indicating that, in addition to its role in the inactivation of Mig1p, Snf1p is required post-transcriptionally for the synthesis of maltose permease whose function is essential for maltose induction.

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26

Gould, Alister D., Patrick G. Telmer, and Brian H. Shilton. "Stimulation of the Maltose Transporter ATPase by Unliganded Maltose Binding Protein." Biochemistry 48, no. 33 (August 25, 2009): 8051–61. http://dx.doi.org/10.1021/bi9007066.

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27

Vongsangnak, Wanwipa, Margarita Salazar, Kim Hansen, and Jens Nielsen. "Genome-wide analysis of maltose utilization and regulation in aspergilli." Microbiology 155, no. 12 (December 1, 2009): 3893–902. http://dx.doi.org/10.1099/mic.0.031104-0.

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Maltose utilization and regulation in aspergilli is of great importance for cellular physiology and industrial fermentation processes. In Aspergillus oryzae, maltose utilization requires a functional MAL locus, composed of three genes: MALR encoding a regulatory protein, MALT encoding maltose permease and MALS encoding maltase. Through a comparative genome and transcriptome analysis we show that the MAL regulon system is active in A. oryzae while it is not present in Aspergillus niger. In order to utilize maltose, A. niger requires a different regulatory system that involves the AmyR regulator for glucoamylase (glaA) induction. Analysis of reporter metabolites and subnetworks illustrates the major route of maltose transport and metabolism in A. oryzae. This demonstrates that overall metabolic responses of A. oryzae occur in terms of genes, enzymes and metabolites when the carbon source is altered. Although the knowledge of maltose transport and metabolism is far from being complete in Aspergillus spp., our study not only helps to understand the sugar preference in industrial fermentation processes, but also indicates how maltose affects gene expression and overall metabolism.

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28

Li, Y., A. Naqui, T. G. Frey, and B. Chance. "A new procedure for the purification of monodisperse highly active cytochrome c oxidase from bovine heart." Biochemical Journal 242, no. 2 (March 1, 1987): 417–23. http://dx.doi.org/10.1042/bj2420417.

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A simple and rapid method for the isolation of a large quantity of cytochrome c oxidase from bovine heart mitochondria was developed, based on selective solubilization of mitochondrial protein with first Triton and then lauryl maltoside. Gel filtration shows that the lauryl maltoside-solubilized oxidase preparation is in a hydrodynamically homogeneous state with a Stokes radius of 7.5 +/- 0.2 nm. It contains 8.0 mumol of haem (with an a/a3 ratio of 1)/g of protein. The catalytic constant (maximum turnover number) with respect to cytochrome c approaches 600 S-1. After further purification of the solubilized enzyme on a sucrose-gradient centrifugation, the purified enzyme has a haem content of 10.3 mumol/g of protein and eight major polypeptide bands shown on SDS/polyacrylamide-gel electrophoresis.

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29

Liang, Xin Hong, Bin Li, Gang Li, Yu Tang, and Zu Feng Guo. "Determination of Sugars in β-Amylase Hydrolysates by High Performance Liquid Chromatography." Advanced Materials Research 396-398 (November 2011): 1575–78. http://dx.doi.org/10.4028/www.scientific.net/amr.396-398.1575.

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Abstract. The chromatographic conditions for the separation of glucose, maltose and maltotriose on a ZORBAX Eclipse XDB-C18 column (4 um, 4.6×250mm) by use of a 2414 differential refractometer detector were determined. The square of the correlation coefficient of glucose, sucrose, maltose and maltotriose was 0.9973, 0.9981, 0.9977 and 0.9987, respectively. When the ratio of signal and noise was 3, the detection limit of glucose, sucrose, maltose and maltotriose was 0.3, 0.3, 0.20, 0.20 mg/mL the β-amylase hydrolysates consisted mainly of maltose, and maltotriose next, glucose only in trace amount, and no sucrose. The RSD of glucose, maltose and maltotriose was 2.08%, 2.41% and 2.61%, respectively. And the recovery of glucose, maltose and maltotriose was 101.3%, 98.4% and 93.5%. It was credible to separate sugars from hydrolysates. The method is important for improving the inducible enzymes activity.

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30

Velayutham, T. S., H. S. Nguan, B. K. Ng, W. C. Gan, V. Manickam Achari, N. I. Zahid, W. H. Abd. Majid, C. Zannoni, and R. Hashim. "Molecular dynamics of anhydrous glycolipid self-assembly in lamellar and hexagonal phases." Physical Chemistry Chemical Physics 18, no. 22 (2016): 15182–90. http://dx.doi.org/10.1039/c6cp00583g.

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31

Ichikawa, Takanori, Mizuki Tanaka, Takayasu Watanabe, Sitong Zhan, Akira Watanabe, Takahiro Shintani, and Katsuya Gomi. "Crucial role of the intracellular α-glucosidase MalT in the activation of the transcription factor AmyR essential for amylolytic gene expression in Aspergillus oryzae." Bioscience, Biotechnology, and Biochemistry 85, no. 9 (July 10, 2021): 2076–83. http://dx.doi.org/10.1093/bbb/zbab125.

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ABSTRACT We examined the role of the intracellular α-glucosidase gene malT, which is part of the maltose-utilizing cluster (MAL cluster) together with malR and malP, in amylolytic gene expression in Aspergillus oryzae. malT disruption severely affected fungal growth on medium containing maltose or starch. Furthermore, the transcription level of the α-amylase gene was significantly reduced by malT disruption. Given that the transcription factor AmyR responsible for amylolytic gene expression is activated by isomaltose converted from maltose incorporated into the cells, MalT may have transglycosylation activity that converts maltose to isomaltose. Indeed, transglycosylated products such as isomaltose/maltotriose and panose were generated from the substrate maltose by MalT purified from a malT-overexpressing strain. The results of this study, taken together, suggests that MalT plays a pivotal role in AmyR activation via its transglycosylation activity that converts maltose to the physiological inducer isomaltose.

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32

Polidori, Ange, Simon Raynal, Laurie-Anne Barret, Mohamed Dahani, Cherone Barrot-Ivolot, Colette Jungas, Erik Frotscher, et al. "Sparingly fluorinated maltoside-based surfactants for membrane-protein stabilization." New J. Chem. 40, no. 6 (2016): 5364–78. http://dx.doi.org/10.1039/c5nj03502c.

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33

McCleary, Barry V., Francoise Bouhet, and Hugues Driguez. "Measurement of amyloglucosidase usingP-nitrophenyl β-maltoside as substrate." Biotechnology Techniques 5, no. 4 (July 1991): 255–58. http://dx.doi.org/10.1007/bf02438658.

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34

Alpes, H., K. Allmann, H. Plattner, J. Reichert, R. Rick, and S. Schulz. "Formation of large unilamellar vesicles using alkyl maltoside detergents." Biochimica et Biophysica Acta (BBA) - Biomembranes 862, no. 2 (November 1986): 294–302. http://dx.doi.org/10.1016/0005-2736(86)90231-2.

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35

Hollander, Robert C. "Recognizing Maltose-induced Hyponatremia." Annals of Internal Medicine 120, no. 3 (February 1, 1994): 248. http://dx.doi.org/10.7326/0003-4819-120-3-199402010-00018.

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Palevsky, Paul M. "Recognizing Maltose-induced Hyponatremia." Annals of Internal Medicine 120, no. 3 (February 1, 1994): 248. http://dx.doi.org/10.7326/0003-4819-120-3-199402010-00019.

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37

Ehrmann, Michael, Rainer Ehrle, Eckhard Hofmann, Winfried Boos, and Andreas Schlösser. "The ABC maltose transporter." Molecular Microbiology 29, no. 3 (August 1998): 685–94. http://dx.doi.org/10.1046/j.1365-2958.1998.00915.x.

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38

DANILCHUK, Yulia V. D. "SELECTIVE CRYSTALLIZATION OF MALTOSE BY ISOPROPANOL AND ACETONE FROM GLUCOSE–MALTOSE SYRUPS." Banat's Journal of Biotechnology VII, no. 14 (October 26, 2016): 120–25. http://dx.doi.org/10.7904/2068-4738-vii(14)-120.

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39

Malik, Heinz, Winfried Boos, and Richard R. Schmidt. "Maltose and Maltotriose Derivatives as Potential Inhibitors of the Maltose-Binding Protein." European Journal of Organic Chemistry 2008, no. 12 (April 2008): 2084–99. http://dx.doi.org/10.1002/ejoc.200701139.

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40

Lu, Yan, Jon M. Steichen, Sean E. Weise, and Thomas D. Sharkey. "Cellular and organ level localization of maltose in maltose-excess Arabidopsis mutants." Planta 224, no. 4 (April 5, 2006): 935–43. http://dx.doi.org/10.1007/s00425-006-0263-7.

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41

Karzis, Joanne, Inge-Marié Petzer, Edward F. Donkin, Vinny Naidoo, and Eric M. C. Etter. "Surveillance of Antibiotic Resistance of Maltose-Negative Staphylococcus aureus in South African Dairy Herds." Antibiotics 9, no. 9 (September 18, 2020): 616. http://dx.doi.org/10.3390/antibiotics9090616.

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Antibiotic resistance has been reported since the 1940s in both human and veterinary medicine. Many years of monitoring milk samples in South Africa led to identification of a novel maltose-negative Staphylococcus aureus (S. aureus) strain, which appears to be an emerging pathogen. In this study, the susceptibility of this strain to antibiotics was evaluated over time, during diverse seasons in various provinces and according to somatic cell count (SCC) categories. A data set of 271 maltose-negative S. aureus isolates, from milk samples of 117 dairy herds, was examined using the disk diffusion method, between 2010 and 2017. This study also compared the susceptibility testing of 57 maltose-negative and 57 maltose-positive S. aureus isolated from 38 farms, from three provinces using minimum inhibitory concentration (MIC). The MIC results for the maltose-negative S. aureus isolates showed highest resistance to ampicillin (100%) and penicillin (47.4) and lowest resistance (1.8%) to azithromycin, ciprofloxacin and erythromycin. The maltose-negative S. aureus isolates showed overall significantly increased antibiotic resistance compared to the maltose-positive strains, as well as multidrug resistance. Producers and veterinarians should consider probability of cure of such organisms (seemingly non-chronic) when adapting management and treatment, preventing unnecessary culling.

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42

Van Leeuwen, C. C. M., R. A. Weusthuis, E. Postma, P. J. A. Van den Broek, and J. P. Van Dijken. "Maltose/proton co-transport in Saccharomyces cerevisiae. Comparative study with cells and plasma membrane vesicles." Biochemical Journal 284, no. 2 (June 1, 1992): 441–45. http://dx.doi.org/10.1042/bj2840441.

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Maltose/proton co-transport was studied in intact cells and in plasma membrane vesicles of the yeast Saccharomyces cerevisiae. In order to determine uphill transport in vesicles, plasma membranes were fused with proteoliposomes containing cytochrome c oxidase as a proton-motive force-generating system. Maltose accumulation, dependent on the electrical and pH gradients, was observed. The initial uptake velocity and accumulation ratio in vesicles proved to be dependent on the external pH. Moreover, kinetic analysis of maltose transport showed that Vmax. values greatly decreased with increasing pH, whereas the Km remained virtually constant. These observations were in good agreement with results obtained with intact cells, and suggest that proton binding to the carrier proceeds with an apparent pK of 5.7. The observation with intact cells that maltose is co-transported with protons in a one-to-one stoichiometry was ascertained in the vesicle system by measuring the balance between proton-motive force and the chemical maltose gradient. These results show that maltose transport in vesicles prepared by fusion of plasma membranes with cytochrome c oxidase proteoliposomes behaves in a similar way as in intact cells. It is therefore concluded that this vesicle model system offers a wide range of new possibilities for the study of maltose/proton co-transport in more detail.

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Cvetkovic, Jelena, Ilka Haferkamp, Regina Rode, Isabel Keller, Benjamin Pommerrenig, Oliver Trentmann, Jacqueline Altensell, et al. "Ectopic maltase alleviates dwarf phenotype and improves plant frost tolerance of maltose transporter mutants." Plant Physiology 186, no. 1 (February 26, 2021): 315–29. http://dx.doi.org/10.1093/plphys/kiab082.

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Abstract Maltose, the major product of starch breakdown in Arabidopsis (Arabidopsis thaliana) leaves, exits the chloroplast via the maltose exporter1 MEX1. Consequently, mex1 loss-of-function plants exhibit substantial maltose accumulation, a starch-excess phenotype and a specific chlorotic phenotype during leaf development. Here, we investigated whether the introduction of an alternative metabolic route could suppress the marked developmental defects typical for mex1 loss-of-function mutants. To this end, we ectopically expressed in mex1chloroplasts a functional maltase (MAL) from baker’s yeast (Saccharomyces cerevisiae, chloroplastidial MAL [cpMAL] mutants). Remarkably, the stromal MAL activity substantially alleviates most phenotypic peculiarities typical for mex1 plants. However, the cpMAL lines contained only slightly less maltose than parental mex1 plants and their starch levels were, surprisingly, even higher. These findings point to a threshold level of maltose responsible for the marked developmental defects in mex1. While growth and flowering time were only slightly retarded, cpMAL lines exhibited a substantially improved frost tolerance, when compared to wild-types. In summary, these results demonstrate the possibility to bypass the MEX1 transporter, allow us to differentiate between possible starch-excess and maltose-excess responses, and demonstrate that stromal maltose accumulation prevents frost defects. The latter insight may be instrumental for the development of crop plants with improved frost tolerance.

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44

Kovačević, D., and K. Mastanjević. "Cryoprotective effect of trehalose and maltose on washed and frozen stored beef meat." Czech Journal of Food Sciences 29, No. 1 (February 14, 2011): 15–23. http://dx.doi.org/10.17221/1042-cjfs.

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The cryoprotective effects of trehalose and maltose (w = 2–10%) on washed beef meat were investigated. Washed beef meat produced from fresh beef meat was frozen and stored for 360 days at –30°C. Myofibrillar protein functional stability was monitored by salt extractable protein (SEP) and differential scanning calorimetry (DSC). Salt extractable protein (SEP) showed that the addition of trehalose and maltose causeda smaller loss of protein solubility during the frozen storage. Peak thermal transition (T<sub>p</sub>) and denaturation enthalpy (ΔH) of myofibrillar proteins were evaluated. Differential scanning calorimetry (DSC) revealed a shift in the peak thermal transition temperature (T<sub>p</sub>) of myosin and actin to higher temperature as the mass fractions of trehalose and maltose increased. The transitions enthalpies of myosin and actin of the washed beef meat samples showed a higher increase with the increase of mass fraction of trehalose then of that of maltose. Since the value of denaturation enthalpy is directly related to the amount of native proteins, higher values of ΔH point to higher cryoprotective effects of trehalose.

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45

Day, Rachel E., Peter J. Rogers, Ian W. Dawes, and Vincent J. Higgins. "Molecular Analysis of Maltotriose Transport and Utilization by Saccharomycescerevisiae." Applied and Environmental Microbiology 68, no. 11 (November 2002): 5326–35. http://dx.doi.org/10.1128/aem.68.11.5326-5335.2002.

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ABSTRACT Efficient fermentation of maltotriose is a desired property of Saccharomyces cerevisiae for brewing. In a standard wort, maltotriose is the second most abundant sugar, and slower uptake leads to residual maltotriose in the finished product. The limiting factor of sugar metabolism is its transport, and there are conflicting reports on whether a specific maltotriose permease exists or whether the mechanisms responsible for maltose uptake also carry out maltotriose transport. In this study, radiolabeled maltotriose was used to show that overexpression of the maltose permease gene, MAL61, in an industrial yeast strain resulted in an increase in the rate of transport of maltotriose as well as maltose. A strain derived from W303-1A and lacking any maltose or maltotriose transporter but carrying a functional maltose transport activator (MAL63) was developed. By complementing this strain with permeases encoded by MAL31, MAL61, and AGT1, it was possible to measure their specific transport kinetics by using maltotriose and maltose. All three permeases were capable of high-affinity transport of maltotriose and of allowing growth of the strain on the sugar. Maltotriose utilization from the permease encoded by AGT1 was regulated by the same genetic mechanisms as those involving the maltose transcriptional activator. Competition studies carried out with two industrial strains, one not containing any homologue of AGT1, showed that maltose uptake and maltotriose uptake were competitive and that maltose was the preferred substrate. These results indicate that the presence of residual maltotriose in beer is not due to a genetic or physiological inability of yeast cells to utilize the sugar but rather to the lower affinity for maltotriose uptake in conjunction with deteriorating conditions present at the later stages of fermentation. Here we identify molecular mechanisms regulating the uptake of maltotriose and determine the role of each of the transporter genes in the cells.

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46

Baturin, Simon, Jamie J. Galka, Hadeesha Piyadasa, S. Gajjeraman, and Joe D. O’Neil. "The effects of a protein osmolyte on the stability of the integral membrane protein glycerol facilitator." Biochemistry and Cell Biology 92, no. 6 (December 2014): 564–75. http://dx.doi.org/10.1139/bcb-2014-0076.

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Osmolytes are naturally occurring molecules used by a wide variety of organisms to stabilize proteins under extreme conditions of temperature, salinity, hydrostatic pressure, denaturant concentration, and desiccation. The effects of the osmolyte trimethylamine N-oxide (TMAO) as well as the influence of detergent head group and acyl chain length on the stability of the Escherichia coli integral membrane protein glycerol facilitator (GF) tetramer to thermal and chemical denaturation by sodium dodecyl sulphate (SDS) are reported. TMAO promotes the association of the normally tetrameric α-helical protein into higher order oligomers in dodecyl-maltoside (DDM), but not in tetradecyl-maltoside (TDM), lyso-lauroylphosphatidyl choline (LLPC), or lyso-myristoylphosphatidyl choline (LMPC), as determined by dynamic light scattering (DLS); an octameric complex is particularly stable as indicated by SDS polyacrylamide gel electrophoresis. TMAO increases the heat stability of the GF tetramer an average of 10 °C in the 4 detergents and also protects the protein from denaturation by SDS. However, it did not promote re-association to the tetramer when added to SDS-dissociated protein. TMAO also promotes the formation of rod-like detergent micelles, and DLS was found to be useful for monitoring the structure of the protein and the redistribution of detergent during thermal dissociation of the protein. The protein is more thermally stable in detergents with the phosphatidylcholine head group (LLPC and LMPC) than in the maltoside detergents. The implications of the results for osmolyte mechanism, membrane protein stability, and protein–protein interactions are discussed.

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47

LACAPÈRE, Jean-Jacques, Jean-Claude ROBERT, and Annick THOMAS-SOUMARMON. "Efficient solubilization and purification of the gastric H+,K+-ATPase for functional and structural studies." Biochemical Journal 345, no. 2 (January 10, 2000): 239–45. http://dx.doi.org/10.1042/bj3450239.

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When gastric H+,K+-ATPase-containing microsomes are solubilized by detergents, a rapid loss of ATPase activity is generally observed. In this article, SDS/PAGE of octa(ethylene glycol)dodecyl monoether (C12E8)- and n-dodecyl β-D-maltoside-solubilized microsomes and their purifications by affinity chromatography on Reactive Red column reveal that inactivation is due to two main effects. (i) Solubilization activates an aspartic protease that cleaves down the α-subunit of the H+,K+-ATPase. Addition of pepstatin A at slightly acidic pH and at low temperature prevents the proteolysis. (ii) A too-harsh delipidation inactivates the ATPase. When n-dodecyl-β-D-maltoside is the detergent, the soluble H+,K+-ATPase is highly active (2.5 μmol/mg per h at pH 6.0 and 5 °C) as long as ATP is added. When C12E8 is used, the detergent induces an inactivation due to delipidation, since addition of lipids restores activity. The two subunits of the H+,K+-ATPase are present in equimolar ratio in the n-dodecyl β-D-maltoside-purified complex. Moreover, two main types of complex (330 and 660 kDa) were resolved in non-denaturing gels and should be the dimeric (αβ)2 and tetrameric (αβ)4 heterodimers respectively. In conclusion, purification of active, stable, soluble complexes of H+,K+-ATPase with few lipids (a lipid/protein ratio of 0.25, w/w) has been achieved. This material should be useful for further structural studies.

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48

Salema-Oom, Madalena, Vera Valadão Pinto, Paula Gonçalves, and Isabel Spencer-Martins. "Maltotriose Utilization by Industrial Saccharomyces Strains: Characterization of a New Member of the α-Glucoside Transporter Family." Applied and Environmental Microbiology 71, no. 9 (September 2005): 5044–49. http://dx.doi.org/10.1128/aem.71.9.5044-5049.2005.

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ABSTRACT Maltotriose utilization by Saccharomyces cerevisiae and closely related yeasts is important to industrial processes based on starch hydrolysates, where the trisaccharide is present in significant concentrations and often is not completely consumed. We undertook an integrated study to better understand maltotriose metabolism in a mixture with glucose and maltose. Physiological data obtained for a particularly fast-growing distiller's strain (PYCC 5297) showed that, in contrast to what has been previously reported for other strains, maltotriose is essentially fermented. The respiratory quotient was, however, considerably higher for maltotriose (0.36) than for maltose (0.16) or glucose (0.11). To assess the role of transport in the sequential utilization of maltose and maltotriose, we investigated the presence of genes involved in maltotriose uptake in the type strain of Saccharomyces carlsbergensis (PYCC 4457). To this end, a previously constructed genomic library was used to identify maltotriose transporter genes by functional complementation of a strain devoid of known maltose transporters. One gene, clearly belonging to the MAL transporter family, was repeatedly isolated from the library. Sequence comparison showed that the novel gene (designated MTY1) shares 90% and 54% identity with MAL31 and AGT1, respectively. However, expression of Mty1p restores growth of the S. cerevisiae receptor strain on both maltose and maltotriose, whereas the closely related Mal31p supports growth on maltose only and Agt1p supports growth on a wider range of substrates, including maltose and maltotriose. Interestingly, Mty1p displays higher affinity for maltotriose than for maltose, a new feature among all the α-glucoside transporters described so far.

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Vidgren, Virve, Laura Ruohonen, and John Londesborough. "Characterization and Functional Analysis of the MAL and MPH Loci for Maltose Utilization in Some Ale and Lager Yeast Strains." Applied and Environmental Microbiology 71, no. 12 (December 2005): 7846–57. http://dx.doi.org/10.1128/aem.71.12.7846-7857.2005.

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ABSTRACT Maltose and maltotriose are the major sugars in brewer's wort. Brewer's yeasts contain multiple genes for maltose transporters. It is not known which of these express functional transporters. We correlated maltose transport kinetics with the genotypes of some ale and lager yeasts. Maltose transport by two ale strains was strongly inhibited by other α-glucosides, suggesting the use of broad substrate specificity transporters, such as Agt1p. Maltose transport by three lager strains was weakly inhibited by other α-glucosides, suggesting the use of narrow substrate specificity transporters. Hybridization studies showed that all five strains contained complete MAL1, MAL2, MAL3, and MAL4 loci, except for one ale strain, which lacked a MAL2 locus. All five strains also contained both AGT1 (coding a broad specificity α-glucoside transporter) and MAL11 alleles. MPH genes (maltose permease homologues) were present in the lager but not in the ale strains. During growth on maltose, the lager strains expressed AGT1 at low levels and MALx1 genes at high levels, whereas the ale strains expressed AGT1 at high levels and MALx1 genes at low levels. MPHx expression was negligible in all strains. The AGT1 sequences from the ale strains encoded full-length (616 amino acid) polypeptides, but those from both sequenced lager strains encoded truncated (394 amino acid) polypeptides that are unlikely to be functional transporters. Thus, despite the apparently similar genotypes of these ale and lager strains revealed by hybridization, maltose is predominantly carried by AGT1-encoded transporters in the ale strains and by MALx1-encoded transporters in the lager strains.

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Krause, Felix S., Alexander Henrich, Bastian Blombach, Reinhard Krämer, Bernhard J. Eikmanns, and Gerd M. Seibold. "Increased Glucose Utilization in Corynebacterium glutamicum by Use of Maltose, and Its Application for the Improvement of l-Valine Productivity." Applied and Environmental Microbiology 76, no. 1 (October 30, 2009): 370–74. http://dx.doi.org/10.1128/aem.01553-09.

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ABSTRACT Corynebacterium glutamicum efficiently utilizes maltose as a substrate. We show here that the presence of maltose increases glucose utilization by raising the expression of ptsG, which encodes the glucose-specific EII permease of the phosphotransferase system. Consequently, the l-valine productivity of a pyruvate dehydrogenase complex-deficient C. glutamicum strain was improved by the presence of maltose.

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