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Academic literature on the topic 'Maltose'

Author: Grafiati

Published: 4 June 2021

Last updated: 5 March 2023

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Journal articles on the topic "Maltose"

1

Visnapuu, Triinu, Aivar Meldre, Kristina Põšnograjeva, Katrin Viigand, Karin Ernits, and Tiina Alamäe. "Characterization of a Maltase from an Early-Diverged Non-Conventional Yeast Blastobotrys adeninivorans." International Journal of Molecular Sciences 21, no. 1 (December 31, 2019): 297. http://dx.doi.org/10.3390/ijms21010297.

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Genome of an early-diverged yeast Blastobotrys (Arxula) adeninivorans (Ba) encodes 88 glycoside hydrolases (GHs) including two α-glucosidases of GH13 family. One of those, the rna_ARAD1D20130g-encoded protein (BaAG2; 581 aa) was overexpressed in Escherichia coli, purified and characterized. We showed that maltose, other maltose-like substrates (maltulose, turanose, maltotriose, melezitose, malto-oligosaccharides of DP 4‒7) and sucrose were hydrolyzed by BaAG2, whereas isomaltose and isomaltose-like substrates (palatinose, α-methylglucoside) were not, confirming that BaAG2 is a maltase. BaAG2 was competitively inhibited by a diabetes drug acarbose (Ki = 0.8 µM) and Tris (Ki = 70.5 µM). BaAG2 was competitively inhibited also by isomaltose-like sugars and a hydrolysis product—glucose. At high maltose concentrations, BaAG2 exhibited transglycosylating ability producing potentially prebiotic di- and trisaccharides. Atypically for yeast maltases, a low but clearly recordable exo-hydrolytic activity on amylose, amylopectin and glycogen was detected. Saccharomyces cerevisiae maltase MAL62, studied for comparison, had only minimal ability to hydrolyze these polymers, and its transglycosylating activity was about three times lower compared to BaAG2. Sequence identity of BaAG2 with other maltases was only moderate being the highest (51%) with the maltase MalT of Aspergillus oryzae.

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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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Houghton-Larsen, Jens, and Anders Brandt. "Fermentation of High Concentrations of Maltose by Saccharomyces cerevisiae Is Limited by the COMPASS Methylation Complex." Applied and Environmental Microbiology 72, no. 11 (September 15, 2006): 7176–82. http://dx.doi.org/10.1128/aem.01704-06.

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ABSTRACT In Saccharomyces cerevisiae, genes encoding maltose permeases and maltases are located in the telomeric regions of different chromosomes. The COMPASS methylation complex, which methylates lysine 4 on histone H3, controls the silencing of telomeric regions. Yeast strains deleted for SWD1, SWD3, SDC1, SET1, BRE2, or SPP1, encoding components of the COMPASS complex, fermented a medium containing 22% maltose with noticeably higher attenuation than did the wild type, resulting in production of up to 29% more ethanol. The least effective strain was spp1. Absence of COMPASS components had no effect on the fermentation of media with 20% glucose, 20% sucrose, or 16% maltose. Deletion of SWD3 resulted in larger amounts of MAL12 transcript, encoding maltase, at the late stages of fermentation of 22% maltose. A similar effect on maltase activity and maltose uptake capability was seen. The lysine 4 residue of histone H3 was trimethylated in wild-type cells at the late stages, while only small amounts of the dimethylated form were detected. Trimethylation and dimethylation of this residue were not detected in strains deleted for SWD1, SWD3, SET1, BRE2, or SDC1. Trimethylated lysine 4 was apparent only at the early stages (48 and 96 h) of fermentation in an spp1 strain. This work indicates that the COMPASS complex represses the expression of maltose utilization genes during the late stages of fermentation of a high concentration of maltose.

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WIMMER, Bernhard, Friedrich LOTTSPEICH, Johannes RITTER, and Karin BRONNENMEIER. "A novel type of thermostable α-D-glucosidase from Thermoanaerobacter thermohydrosulfuricus exhibiting maltodextrinohydrolase activity." Biochemical Journal 328, no. 2 (December 1, 1997): 581–86. http://dx.doi.org/10.1042/bj3280581.

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An α-glucosidase with the ability to attack polymeric substrates was purified to homogeneity from culture supernatants of Thermoanaerobacter thermohydrosulfuricus DSM 567. The enzyme is apparently a glycoprotein with a molecular mass of 160 kDa. Maximal activity is observed between pH 5 and 7 at 75 °C. The α-glucosidase is active towards p-nitrophenyl-α-D-glucoside, maltose, malto-oligosaccharides, starch and pullulan. Highest activity is displayed towards the disaccharide maltose. In addition to glucose, maltohexaose and maltoheptaose can be detected as the initial products of starch hydrolysis. After short incubations of pullulan, glucose is found as the only product. At high substrate concentrations, maltose and malto-oligosaccharide, but not glucose, are used as acceptors for glucosyl-transfer. These findings indicate that the T. thermohydrosulfuricus enzyme represents a novel type of α-glucosidase exhibiting maltase, glucohydrolase and ‘maltodextrinohydrolase’ activity.

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Ferreira, Julio C., Anita D. Panek, and Pedro S. de Araujo. "Inactivation of maltose permease and maltase in sporulatingSaccharomyces cerevisiae." Canadian Journal of Microbiology 46, no. 4 (April 1, 2000): 383–86. http://dx.doi.org/10.1139/w99-136.

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Maltose transport and maltase activities were inactivated during sporulation of a MAL constitutive yeast strain harboring different MAL loci. Both activities were reduced to almost zero after 5 h of incubation in sporulation medium. The inactivation of maltase and maltose permease seems to be related to optimal sporulation conditions such as a suitable supply of oxygen and cell concentration in the sporulating cultures, and occurs in the fully derepressed conditions of incubation in the sporulation acetate medium. The inactivation of maltase and maltose permease under sporulation conditions in MAL constitutive strains suggests an alternative mechanism for the regulation of the MAL gene expression during the sporulation process.Key words: maltase activity, maltose permease activity, sporulation, Saccharomyces cerevisiae.

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Dubin, R. A., E. L. Perkins, R. B. Needleman, and C. A. Michels. "Identification of a second trans-acting gene controlling maltose fermentation in Saccharomyces carlsbergensis." Molecular and Cellular Biology 6, no. 8 (August 1986): 2757–65. http://dx.doi.org/10.1128/mcb.6.8.2757-2765.1986.

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Maltose fermentation in Saccharomyces spp. requires the presence of a dominant MAL locus. The MAL6 locus has been cloned and shown to encode the structural genes for maltose permease (MAL61), maltase (MAL62), and a positively acting regulatory gene (MAL63). Induction of the MAL61 and MAL62 gene products requires the presence of maltose and the MAL63 gene. Mutations within the MAL63 gene produce nonfermenting strains unable to induce the two structural gene products. Reversion of these mal63 nonfermenters to maltose fermenters nearly always leads to the constitutive expression of maltase and maltose permease, and constitutivity is always linked to MAL6. We demonstrated that for one such revertant, strain C2, constitutivity did not require the MAL63 gene, since deletion disruption of this gene did not affect the constitutive expression of the structural genes. In addition, constitutivity was trans acting. Deletion disruption of the MAL6-linked structural genes for maltase and maltose permease in this strain did not affect the constitutive expression of a second, unlinked maltase structural gene. We isolated new maltose-fermenting revertants of a nonfermenting strain which carried a deletion disruption of the MAL63 gene. All 16 revertants isolated expressed maltase constitutively. In one revertant studied in detail, strain R10, constitutive expression was demonstrated to be linked to MAL6, semidominant, trans acting, and residing outside the MAL63-MAL61-MAL62 genes. From these studies we propose the existence of a second trans-acting regulatory gene at the MAL6 locus. We call this new gene MAL64. We mapped the MAL64 gene 2.3 centimorgans to the left of MAL63. The role of the MAL64 gene product in maltose fermentation is discussed.

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Dubin, R. A., E. L. Perkins, R. B. Needleman, and C. A. Michels. "Identification of a second trans-acting gene controlling maltose fermentation in Saccharomyces carlsbergensis." Molecular and Cellular Biology 6, no. 8 (August 1986): 2757–65. http://dx.doi.org/10.1128/mcb.6.8.2757.

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Maltose fermentation in Saccharomyces spp. requires the presence of a dominant MAL locus. The MAL6 locus has been cloned and shown to encode the structural genes for maltose permease (MAL61), maltase (MAL62), and a positively acting regulatory gene (MAL63). Induction of the MAL61 and MAL62 gene products requires the presence of maltose and the MAL63 gene. Mutations within the MAL63 gene produce nonfermenting strains unable to induce the two structural gene products. Reversion of these mal63 nonfermenters to maltose fermenters nearly always leads to the constitutive expression of maltase and maltose permease, and constitutivity is always linked to MAL6. We demonstrated that for one such revertant, strain C2, constitutivity did not require the MAL63 gene, since deletion disruption of this gene did not affect the constitutive expression of the structural genes. In addition, constitutivity was trans acting. Deletion disruption of the MAL6-linked structural genes for maltase and maltose permease in this strain did not affect the constitutive expression of a second, unlinked maltase structural gene. We isolated new maltose-fermenting revertants of a nonfermenting strain which carried a deletion disruption of the MAL63 gene. All 16 revertants isolated expressed maltase constitutively. In one revertant studied in detail, strain R10, constitutive expression was demonstrated to be linked to MAL6, semidominant, trans acting, and residing outside the MAL63-MAL61-MAL62 genes. From these studies we propose the existence of a second trans-acting regulatory gene at the MAL6 locus. We call this new gene MAL64. We mapped the MAL64 gene 2.3 centimorgans to the left of MAL63. The role of the MAL64 gene product in maltose fermentation is discussed.

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Charron, M. J., and C. A. Michels. "The naturally occurring alleles of MAL1 in Saccharomyces species evolved by various mutagenic processes including chromosomal rearrangement." Genetics 120, no. 1 (September 1, 1988): 83–93. http://dx.doi.org/10.1093/genetics/120.1.83.

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Abstract In order for a yeast strain to ferment maltose it must contain any one of the five dominant MAL loci. Each dominant MAL locus thus far analyzed contains three genes: GENE 1, encoding maltose permease, GENE 2 encoding maltase and GENE 3 encoding a positive trans-acting regulatory protein. In addition to these dominant MAL loci, several naturally occurring, partially functional alleles of MAL1 and MAL3 have been identified. Here, we present genetic and molecular analysis of the three partially functional alleles of MAL1: the MAL1p allele which can express only the MAL activator; the MAL1 g allele which can express both a maltose permease and maltase; and the mal1(0) allele which can express only maltase. Based on our results, we propose that the MAL1p, MAL1g and mal1(0) alleles evolved from the dominant MAL1 locus by a series of rearrangements and/or deletions of this yeast telomere-associated locus as well as by other mutagenic processes of gene inactivation. One surprising finding is that the MAL1g-encoded maltose permease exhibits little sequence homology to the MAL1-encoded maltose permease though they appear to be functionally homologous.

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Hong, S. H., and J. Marmur. "Upstream regulatory regions controlling the expression of the yeast maltase gene." Molecular and Cellular Biology 7, no. 7 (July 1987): 2477–83. http://dx.doi.org/10.1128/mcb.7.7.2477-2483.1987.

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The expression of the maltase (MALS) and the maltose permease (MALT) genes in Saccharomyces species is coregulated at the transcriptional level; they are coordinately induced by maltose in the presence of a positively acting regulatory (MALR) gene and carbon catabolite repressed by glucose. We generated a series of deletions in the upstream region of the MAL6S gene to examine the regulatory elements in detail. The results showed that inducible expression by maltose was lost when the region between 320 and 380 base pairs upstream of the translation initiation codon was deleted. This region contained an imperfect inverted repeat sequence (-361 to -327) or four copies of short direct repeats that might serve as components of the upstream activation site (UASM) for the maltase gene, or both. When a stretch of T-rich sequence (-253 to -237) was deleted, the susceptibility of the maltase gene to carbon catabolite repression was affected.

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Hong, S. H., and J. Marmur. "Upstream regulatory regions controlling the expression of the yeast maltase gene." Molecular and Cellular Biology 7, no. 7 (July 1987): 2477–83. http://dx.doi.org/10.1128/mcb.7.7.2477.

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The expression of the maltase (MALS) and the maltose permease (MALT) genes in Saccharomyces species is coregulated at the transcriptional level; they are coordinately induced by maltose in the presence of a positively acting regulatory (MALR) gene and carbon catabolite repressed by glucose. We generated a series of deletions in the upstream region of the MAL6S gene to examine the regulatory elements in detail. The results showed that inducible expression by maltose was lost when the region between 320 and 380 base pairs upstream of the translation initiation codon was deleted. This region contained an imperfect inverted repeat sequence (-361 to -327) or four copies of short direct repeats that might serve as components of the upstream activation site (UASM) for the maltase gene, or both. When a stretch of T-rich sequence (-253 to -237) was deleted, the susceptibility of the maltase gene to carbon catabolite repression was affected.

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Dissertations / Theses on the topic "Maltose"

1

Dalgleish, Pamela Weir. "The yeast maltose transporter." Thesis, Heriot-Watt University, 1997. http://hdl.handle.net/10399/678.

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Laba, Marija. "Optimalizace metody HPLC-ELSD pro stanovení sacharidů v potravinách." Master's thesis, Vysoké učení technické v Brně. Fakulta chemická, 2017. http://www.nusl.cz/ntk/nusl-295706.

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This master's thesis deals with the optimalization of HPLC-ELSD method for the determination of carbohydrates in food. The theoretical part focuses on the classification and characterization of carbohydrates, the occurrence of carbohydrates in food and their physiological importance. There was targeted mainly glucose, fructose, sucrose and maltose. There is a brief summary of the analytical methods that can be used to determine carbohydrates. Experimental part is based on a literary review. It also deals with high performance liquid chromatography with evaporative light scattering detector. The main content in this part is the optimalization of condition for reliable and rapid separation of the most frequently occurring carbohydrates in foods. The carbohydrates were identified and quantified under optimum condition in real samples specifically in fruit juice, beer, ketchup and red pepper powder. The result is commented in conclusion.

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Luo, Xing. "Roles of regulatory RNAs in Vibrio pathogenic to species of aquaculture interest." Thesis, Université Paris-Saclay (ComUE), 2019. http://www.theses.fr/2019SACLS226.

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Les petits ARN régulateurs bactériens, généralement de 50 à 300 nt de long, agissent en appariant les bases avec des cibles d'ARNm spécifiques, affectant ainsi leur traduction et/ou leur stabilité, sont des éléments importants qui régulent divers processus. V. tasmaniensis LGP32 est un pathogène de l'huître facultatif. Un ARNs Vsr217 s'est révélé être conservé dans les vibrions et fortement régulé à la hausse lors de l'infection des huîtres. J'ai trouvé que vsr217 et le gène en aval malK (codant pour une sous-unité du transporteur principal de maltose) sont tous deux exprimés à partir d'un promoteur en amont régulé par l'activateur de maltose MalT, Vsr217 étant généré à partir de la longue 5' UTR de l'ARNm de malK. Outre un effet cis sur l’expression du malK, qui diminue chez le mutant Δvsr217, nous avons constaté que l’absence de cet ARNs entraînait, lors de la croissance de cellules dans du maltose, l’augmentation de deux enzymes importantes impliquées dans la voie de la glycolyse/néoglucogenèse, Fbp et PpsA et cet ARNm de fbp étaient une cible directe de Vsr217. J'ai également exploré la régulation de la biosynthèse des acides aminés à chaîne ramifiée (BCAA: Leucine, Valine et Isoleucine) chez V. alginolyticus, un agent pathogène des poissons et mollusques et des poissons de mer et un agent pathogène humain émergent opportuniste. Nous avons constaté que l'opéron ilvGMEDA (codant la voie principale pour la biosynthèse des BCAAs) est régulé par un peptide leader traduit. Ainsi, la traduction d'un peptide riche en BCAA codé en amont des gènes de structure fournit une réponse adaptative par un mécanisme similaire au modèle canonique de E. coli. Cette étude portant sur un organisme non modèle à Gram-négatif met en évidence la conservation mécanistique de l'atténuation de la transcription malgré l'absence de conservation de la séquence primaire
Bacterial regulatory small RNAs, usually 50-300 nt long, act by base-pairing with specific mRNA targets, affecting their translation and/or stability, are important elements which regulate a variety of processes. V. tasmaniensis LGP32 is a facultative oyster pathogen. A sRNA Vsr217 was found to be conserved within vibrios and highly upregulated during oyster infection. I found that vsr217 and the downstream gene malK (encoding a subunit of the major maltose transporter) are both expressed from an upstream promoter regulated by the maltose activator MalT with Vsr217 being generated from the long 5' UTR of the malK mRNA. Beside a cis-effect on malK expression, which decreases in the Δvsr217 mutant, we found that the absence of this sRNA resulted, when cells grown in maltose, in the increase of two important enzymes involved in the glycolysis/neoglucogenesis pathway, Fbp and PpsA and that fbp mRNA was a direct target of Vsr217. I also explored the regulation of the biosynthesis of branched-chain amino acids (BCAAs: Leucine, Valine and Isoleucine) in V. alginolyticus, a marine fish and shellfish pathogen and an emerging opportunistic human pathogen. We found that the ilvGMEDA operon (encoding the main pathway for biosynthesis of BCAAs) is regulated by a translated leader peptide. Thus, the translation of a BCAA rich peptide encoded upstream of the structural genes provides an adaptive response by a mechanism similar to the E. coli canonical model. This study with a non-model Gram-negative organism highlights the mechanistic conservation of transcription attenuation despite the absence of primary sequence conservation

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Yip, Hopi. "Genetic manipulation of baker's yeast for improved maltose utilisation /." [Richmond, N.S.W.] : Centre for Biostructural and Biomolecular Resarch, Faculty of Science and Technolocy, University of Western Sydney, Hawkesbury, 1999. http://library.uws.edu.au/adt-NUWS/public/adt-NUWS20030625.100807/index.html.

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Schönert, Stefan. "Maltose- und Maltodextrin-Verwertung in Bacillus subtilis." [S.l. : s.n.], 2004. http://deposit.ddb.de/cgi-bin/dokserv?idn=973091967.

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Bao, Huan. "The regulatory mechanisms of the maltose transporter." Thesis, University of British Columbia, 2014. http://hdl.handle.net/2429/46285.

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ATP-binding cassette (ABC) transporters couple ATP hydrolysis to import and export of a large array of substances across cell membranes in all kingdoms of life. Since the transport reaction consumes cellular energy, substrate translocation mediated by ABC transporters must be regulated according to the requirements of the cell. This thesis uses the Escherichia coli maltose transporter MalFGK2 to understand the regulatory mechanisms of ABC importers. Biochemical and biophysical approaches were employed to investigate how this transport process is modulated by maltose, the maltose-binding protein MalE and the glucose-specific enzyme EIIAGlc. First, I show that ATP facilitates MalE binding to MalFGK2, which forms the complex of MalE-MalFGK2 for efficient maltose transport. In addition, when the external maltose level exceeds that required, maltose is able to limit the maximal transport rate by promoting dissociation of MalE from MalFGK2. Finally, I find that the N-terminal tail of EIIAGlc and acidic phospholipids are essential for the binding of the protein to the MalK dimer, so that cleavage of ATP by MalFGK2 is inhibited. These results, combined with previous genetic, biochemical and structural work, provide valuable insights into our understanding of the regulatory mechanisms of the maltose transport system.

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Hamid, Mas Rina Wati Haji Abdul. "Maltose metabolism in Bacillus licheniformis NCIB 6346." Thesis, Heriot-Watt University, 1992. http://hdl.handle.net/10399/801.

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Hollingsworth, Kristian. "The synthesis of a maltose responsive switch." Thesis, University of Leeds, 2015. http://etheses.whiterose.ac.uk/12160/.

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A cells interaction with its surroundings is governed by the flora of the cell surface. This complex landscape of structures provides an opportunity for the re-engineering of the surface and so the cells properties without the use of genetic modification. Applying the principles of supramolecular chemistry; surface proteins can be targeted with carbohydrate based ligands to form both stable and metabolite-responsive non-covalent complexes. This redecoration of the surfaces of bacteria will make it possible to control the interactions that a bacterium makes with its environment, whether in a patient or a bioreactor. In this project the transport protein maltoporin and maltose binding protein (MBP) will be utilised in the construction of a maltose responsive switch. Both proteins will be targeted with a maltose-based polymer which can thread through maltoporin on the cell surface to interact with MBP in the periplasm. In addition, the synthesis of molecules to probe the binding of maltoporin through biophysical experiments will be investigated.

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Yip, Hopi, of Western Sydney Hawkesbury University, and Faculty of Science and Technology. "Genetic manipulation of baker's yeast for improved maltose utilisation." THESIS_FSTA_SFS_Yip_H.xml, 1999. http://handle.uws.edu.au:8081/1959.7/223.

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Two yeast/E.coli shuttle vector plasmids were studied in 1994, termed pIBIDB and pBP33. According to this study, each plasmid should contain at least one ADH2UAS (upstream activation sequence in the alcohol dehydrogenase 2 gene) insert. In the present study, the constructed plasmids were analysed and transformed into laboratory strain yeast. The aim of this project was to identify the orientation, quantity and quality of the insert in the selected plasmids. Methods such as restriction analysis, polymerase chained reaction (PCR), sequencing, plate assays and enzyme assays were used to identify and evaluate the novel inserts. The data presented in this thesis suggest the inserted ADH2UAS fragment did enhance the production of maltose permease and maltase when the transformants were cultivated in maltose and ethanol-glycerol medium. The results suggested that transformants containing two inserts of ADH2UAS had a greater influence on the transformants than a single insert. But the inserts within the vectors and in transformed laboratory stain yeast appeared unstable. This could be due to the method used for plasmid construction and the storage condition of the transformants
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Scott, Peter. "The metabolism of sucrose and maltose by barley microspores." Thesis, University of Cambridge, 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.239199.

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Books on the topic "Maltose"

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Quynh, Nguyen Khac. Sweetness from starch: A manual for making maltose from starch. Rome: Food and Agricultural Industries Service, Agricultural Support Systems Division, Food and Agriculture Organization of the United Nations, 1996.

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Characterization of the maltose regulon of Vibrio cholerae: Involvement of maltose in production of outer membrane proteins and secretion of virulence factors. Uppsala: Swedish University of Agricultural Sciences, Dept. of Molecular Genetics, Uppsala Genetic Center, 1993.

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Mangion, Giovanni. Studi italo-maltesi =: Italo-Maltese studies. Valletta, Malta: Said International, 1992.

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Maltese. Vero Beach, FL: Rourke Pub., 2009.

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Giacomo. Maltese. Neptune City, NJ: T.F.H. Publications, 1994.

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Borg, Albert J. Maltese. London: Routledge, 1997.

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Maltese. Neptune City, NJ: T.F.H. Publications, 2007.

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J, Bergquist Barbara, ed. Maltese. Neptune, NJ: T.F.H. Publications, 1994.

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Maltese. Edina, Minn: Abdo Pub., 2005.

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Concise Maltese English, English Maltese dictionary. Sta Venera, Malta: Midsea Books, 2006.

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Book chapters on the topic "Maltose"

1

Bährle-Rapp, Marina. "Maltose." In Springer Lexikon Kosmetik und Körperpflege, 338. Berlin, Heidelberg: Springer Berlin Heidelberg, 2007. http://dx.doi.org/10.1007/978-3-540-71095-0_6268.

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Schomburg, Dietmar, and Dörte Stephan. "Maltose synthase." In Enzyme Handbook 12, 653–55. Berlin, Heidelberg: Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-642-61117-9_139.

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Schomburg, Dietmar, and Dörte Stephan. "Maltose phosphorylase." In Enzyme Handbook 12, 119–22. Berlin, Heidelberg: Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-642-61117-9_21.

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Schomburg, Dietmar, and Dörte Stephan. "Maltose O-acetyltransferase." In Enzyme Handbook 11, 985–87. Berlin, Heidelberg: Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-642-61030-1_211.

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Boos, Winfried, Ralf Peist, Katja Decker, and Eva Zdych. "The Maltose System." In Regulation of Gene Expression in Escherichia coli, 201–29. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4684-8601-8_10.

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Schomburg, Dietmar, and Dörte Stephan. "Maltose-6’-phosphate glucosidase." In Enzyme Handbook 15, 283–85. Berlin, Heidelberg: Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-642-58948-5_64.

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Winkelmann, Jochen. "Diffusion coefficient of maltose in water." In Diffusion in Gases, Liquids and Electrolytes, 993. Berlin, Heidelberg: Springer Berlin Heidelberg, 2017. http://dx.doi.org/10.1007/978-3-540-73735-3_769.

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Winkelmann, Jochen. "Diffusion coefficient of maltose in water." In Diffusion in Gases, Liquids and Electrolytes, 1437–40. Berlin, Heidelberg: Springer Berlin Heidelberg, 2018. http://dx.doi.org/10.1007/978-3-662-54089-3_984.

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Pattenden, Leonard K., and Walter G. Thomas. "Amylose Affinity Chromatography of Maltose-Binding Protein." In Affinity Chromatography, 169–90. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-582-4_12.

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Winkelmann, Jochen. "Diffusion coefficient of maltose in dideuterium oxide." In Diffusion in Gases, Liquids and Electrolytes, 1416. Berlin, Heidelberg: Springer Berlin Heidelberg, 2018. http://dx.doi.org/10.1007/978-3-662-54089-3_974.

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Conference papers on the topic "Maltose"

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Lo Leggio, Leila, Florence Dal Degan, Peter Poulsen, and Sine Larsen. "STRUCTURE OF MALTOSE O-ACETYLTRANSFERASE." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.468.

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Machinami, Tomoya, Yoshihiro Mitsutsuka, Takashi Fujimoto, Motoaki Imai, and Tetsuo Suami. "CRYSTAL STRUCTURE OF 1,6-ANHYDRO-BETA-MALTOSE." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.509.

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Zawicki, Ignacy, Marian Filipiak, Marta Jarzyna, and Janina Laskowska. "Amperometric biosensors for determination of glucose, maltose, and sucrose." In Optoelectronic and Electronic Sensors, edited by Ryszard Jachowicz and Zdzislaw Jankiewicz. SPIE, 1995. http://dx.doi.org/10.1117/12.213156.

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Kožár, Tibor, and Claus Wilhelm von der Lieth. "Modeling conformational properties of maltose in gas phase and solvent." In The first European conference on computational chemistry (E.C.C.C.1). AIP, 1995. http://dx.doi.org/10.1063/1.47746.

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Guice, Justin, Morgan Hollins, Caroline Best, Kelly Tinker, and Sean Garvey. "Fungal Multi-enzyme Blend Promotes Improved Macronutrient Hydrolysis of Mixed Meal Substrates in the INFOGEST in vitro Simulation of Digestion." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/fsgu7847.

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Fungal enzymes are often combined in dietary supplements to support digestive health. The purpose of this study was to test the effects of a mixture of 6 fungal enzymes (BC-006) on macronutrient digestion in the INFOGEST static simulation of gastrointestinal digestion in vitro. Substrates included an oral nutritional supplement (ONS), heated test meal (HTM) with grilled chicken, steamed peas, and potatoes, and a canned test meal (CTM) version. BC-006 contains fungal protease (Aspergillus oryzae), acid protease (A. niger), peptidase (A. melleus), lipase (Candida cylindracea), alpha-amylase (A. oryzae), and glucoamylase (A. niger). Three doses of BC-006 (0.5X, 1X, and 2X recommended dose) were evaluated on free amino nitrogen (FAN), glycerol, maltose, and glucose release from substrates. Following the gastric simulation, all doses of BC-006 increased FAN concentrations across all substrates, compared to control conditions with pepsin alone (p≤0.0001). HPLC analysis showed that BC-006 treatment increased the concentrations of leucine (ONS: 4.5-fold, HTM: 4.1-fold, CTM: 3.7-fold) and total essential amino acids (2.8-fold, 87%, 71%, respectively), compared to controls (p<0.05). In the intestinal phase, however, no differences in FAN concentrations were observed. BC-006 (1X) increased glycerol concentrations at least 3.3-fold higher in the gastric simulation (HTM, p=0.0446) and at least 76% higher in the intestinal simulation (HTM, p=0.0003). Glucose released increased with BC-006 dose for all substrates in the gastric and intestinal simulations (p<0.0001). Maltose release increased with BC-006 dose in the gastric simulation of ONS digestion (p<0.0001), but no differences were observed with HTM and CTM. In the intestinal simulation, maltose release increased with BC-006 dose in the gastric simulation of ONS digestion (p=0.0002), but decreased with increasing BC-006 dose in the gastric simulation with HTM (p=0.0077) and CTM (p=0.0083). Altogether, the BC-006 blend improved hydrolysis of all macronutrients in the gastric simulation, and lipid and carbohydrate hydrolysis in the intestinal simulation.

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Guice, Justin, Caroline Best, Morgan Hollins, Kelly Tinker, and Sean Garvey. "Fungal Digestive Enzymes Promote Macronutrient Hydrolysis in the INFOGEST in vitro Simulation of Digestion." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/agsn3911.

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Fungal enzymes are common ingredients in dietary supplements that support digestion. At adequate concentrations, exogenous enzymes may improve digestion by hydrolyzing macronutrients beyond acid-mediated hydrolysis, endogenous gastric pepsin, and pancreatic enzymes alone. The purpose of this study was to test the hydrolytic efficacy of 6 commercial fungal enzymes—three proteases, a lipase, an amylase, and a glucoamylase—in the INFOGEST static in vitro simulation of gastrointestinal digestion. The efficacy of 5 doses of each enzyme was determined by measuring free amino nitrogen (FAN), glycerol, maltose, and glucose concentrations following salivary-gastric (SG) and full salivary-gastric-intestinal (SGI) simulations of digestion of an oral nutritional supplement. In the SG simulation, the 3 proteases, lipase, and combination of amylase and glucoamylase promoted greater hydrolysis of dietary protein, fat, and carbohydrates, respectively, compared to control conditions. Acid protease (Aspergillus niger) treatment increased FAN concentrations than controls from 27% at the lowest dose to 142% greater than controls at the highest dose (p<0.0001). Fungal protease (A. oryzae) treatment increased FAN concentration at the highest dose (160,000 HUT, p=0.0115). Peptidase (A. melleus) treatment promoted higher FAN concentrations, up to 50% increase at the highest dose (160 LAPU, p<0.0001). Glycerol concentrations increased across all lipase treatments (p<0.0001), from 4.1-fold to 11.2-fold increases at the lowest and highest doses, respectively. All doses of amylase increased glucose concentrations (p<0.0001), and maltose concentrations started increasing at 4,000 SKB units (p=0.0010). In the SGI simulation, FAN concentrations following protease treatments were similar to control, suggesting little benefit beyond pancreatin alone in this static simulation of healthy digestion. Lipase and amylase/glucoamylase treatments, however, did increase glycerol (p<0.0001) and maltose/glucose concentrations (p<0.0001), respectively, compared to controls in the full SGI simulation. These data demonstrate that exogenous, fungal enzymes can improve macronutrient digestion under the acidic conditions of the gastric simulation, as well as the intestinal simulation.

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Madsen, J., Y. Ghrabigi, T. Castillo Hernandez, T. Greenhough, A. Shrive, and H. Clark. "Characterisation of the Structural Requirements for the Immunomodulatory Surfactant Protein D (SP-D) to Bind to Maltose Based Ligands." In American Thoracic Society 2022 International Conference, May 13-18, 2022 - San Francisco, CA. American Thoracic Society, 2022. http://dx.doi.org/10.1164/ajrccm-conference.2022.205.1_meetingabstracts.a2609.

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Lea, Michael A., and Charles desBordes. "Abstract 227: Maltose enhanced the growth of bladder and colon cancer cells unlike some other disaccharides: Cellobiose, isomaltose, lactose, and sucrose." In Proceedings: AACR Annual Meeting 2020; April 27-28, 2020 and June 22-24, 2020; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-227.

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Bekiroglu, Somer, Corine Sandstrom, and Lennart Kenne. "1H NMR STUDIES OF MALTOSE, ALPHA-, BETA-, GAMMA-CYCLODEXTRINS AND COMPLEXES IN AQUEOUS SOLUTIONS BY USING HYDROXY PROTONS AS STRUCTURAL PROBES." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.551.

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Toda, Atsushi, Kuriko Yamada, Shigeo Shibatani, Susumu Nishiguchi, Hiroaki Nakagawa, Masaki Kurogochi, and Shin-Ichiro Nishimura. "EXPRESSION OF BETA 1,3-N-ACETYLGLUCOSAMINYLTRANSFERASE FROM STREPTOCOCCUS AGALACTIAE TYPE IA IN ESCHERICHIA COLI AS A FUSION WITH MALTOSE-BINDING PROTEIN." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.765.

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Reports on the topic "Maltose"

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Sharkey, Thomas D. Maltose Biochemistry and Transport in Plant Leaves. Office of Scientific and Technical Information (OSTI), January 2010. http://dx.doi.org/10.2172/971070.

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Weber, Andreas P. M. Maltose Biochemistry and Transport in Plant Leaves. Office of Scientific and Technical Information (OSTI), April 2008. http://dx.doi.org/10.2172/928757.

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Sharkey, Thomas D. Maltose Biochemistry and Transport in Plant Leaves. Office of Scientific and Technical Information (OSTI), May 2012. http://dx.doi.org/10.2172/1039496.

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Gershoni, Jonathan M., David E. Swayne, Tal Pupko, Shimon Perk, Alexander Panshin, Avishai Lublin, and Natalia Golander. Discovery and reconstitution of cross-reactive vaccine targets for H5 and H9 avian influenza. United States Department of Agriculture, January 2015. http://dx.doi.org/10.32747/2015.7699854.bard.

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Research objectives: Identification of highly conserved B-cell epitopes common to either H5 or H9 subtypes of AI Reconstruction of conserved epitopes from (1) as recombinantimmunogens, and testing their suitability to be used as universal vaccine components by measuring their binding to Influenza vaccinated sera of birds Vaccination of chickens with reconstituted epitopes and evaluation of successful vaccination, clinical protection and viral replication Development of a platform to investigate the dynamics of immune response towards infection or an epitope based vaccine Estimate our ability to focus the immune response towards an epitope-based vaccine using the tool we have developed in (D) Summary: This study is a multi-disciplinary study of four-way collaboration; The SERPL, USDA, Kimron-Israel, and two groups at TAU with the purpose of evaluating the production and implementation of epitope based vaccines against avian influenza (AI). Systematic analysis of the influenza viral spike led to the production of a highly conserved epitope situated at the hinge of the HA antigen designated “cluster 300” (c300). This epitope consists of a total of 31 residues and was initially expressed as a fusion protein of the Protein 8 major protein of the bacteriophagefd. Two versions of the c300 were produced to correspond to the H5 and H9 antigens respectively as well as scrambled versions that were identical with regard to amino acid composition yet with varied linear sequence (these served as negative controls). The recombinantimmunogens were produced first as phage fusions and then subsequently as fusions with maltose binding protein (MBP) or glutathioneS-transferase (GST). The latter were used to immunize and boost chickens at SERPL and Kimron. Furthermore, vaccinated and control chickens were challenged with concordant influenza strains at Kimron and SEPRL. Polyclonal sera were obtained for further analyses at TAU and computational bioinformatics analyses in collaboration with Prof. Pupko. Moreover, the degree of protection afforded by the vaccination was determined. Unfortunately, no protection could be demonstrated. In parallel to the main theme of the study, the TAU team (Gershoni and Pupko) designed and developed a novel methodology for the systematic analysis of the antibody composition of polyclonal sera (Deep Panning) which is essential for the analyses of the humoral response towards vaccination and challenge. Deep Panning is currently being used to monitor the polyclonal sera derived from the vaccination studies conducted at the SEPRL and Kimron.

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Uni, Zehava, and Peter Ferket. Enhancement of development of broilers and poults by in ovo feeding. United States Department of Agriculture, May 2006. http://dx.doi.org/10.32747/2006.7695878.bard.

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The specific objectives of this research were the study of the physical and nutritional properties of the In Ovo Feeding (IOF) solution (i.e. theosmostic properties and the carbohydrate: protein ratio composition). Then, using the optimal solution for determining its effect on hatchability, early nutritional status and intestinal development of broilers and turkey during the last quarter of incubation through to 7 days post-hatch (i.e. pre-post hatch period) by using molecular, biochemical and histological tools. The objective for the last research phase was the determination of the effect of in ovo feeding on growth performance and economically valuable production traits of broiler and turkey flocks reared under practical commercial conditions. The few days before- and- after hatch is a critical period for the development and survival of commercial broilers and turkeys. During this period chicks make the metabolic and physiological transition from egg nutriture (i.e. yolk) to exogenous feed. Late-term embryos and hatchlings may suffer a low glycogen status, especially when oxygen availability to the embryo is limited by low egg conductance or poor incubator ventilation. Much of the glycogen reserve in the late-term chicken embryo is utilized for hatching. Subsequently, the chick must rebuild that glycogen reserve by gluconeogenesis from body protein (mostly from the breast muscle) to support post-hatch thermoregulation and survival until the chicks are able to consume and utilize dietary nutrients. Immediately post-hatch, the chick draws from its limited body reserves and undergoes rapid physical and functional development of the gastrointestinal tract (GIT) in order to digest feed and assimilate nutrients. Because the intestine is the nutrient primary supply organ, the sooner it achieves this functional capacity, the sooner the young bird can utilize dietary nutrients and efficiently grow at its genetic potential and resist infectious and metabolic disease. Feeding the embryo when they consume the amniotic fluid (IOF idea and method) showed accelerated enteric development and elevated capacity to digest nutrients. By injecting a feeding solution into the embryonic amnion, the embryo naturally consume supplemental nutrients orally before hatching. This stimulates intestinal development to start earlier as was exhibited by elevated gene expression of several functional genes (brush border enzymes an transporters , elvated surface area, elevated mucin production . Moreover, supplying supplemental nutrients at a critical developmental stage by this in ovo feeding technology improves the hatchling’s nutritional status. In comparison to controls, administration of 1 ml of in ovo feeding solution, containing dextrin, maltose, sucrose and amino acids, into the amnion of the broiler embryo increased dramatically total liver glycogen in broilers and in turkeys in the pre-hatch period. In addition, an elevated relative breast muscle size (% of broiler BW) was observed in IOF chicks to be 6.5% greater at hatch and 7 days post-hatch in comparison to controls. Experiment have shown that IOF broilers and turkeys increased hatchling weights by 3% to 7% (P<0.05) over non injected controls. These responses depend upon the strain, the breeder hen age and in ovo feed composition. The weight advantage observed during the first week after hatch was found to be sustained at least through 35 days of age. Currently, research is done in order to adopt the knowledge for commercial practice.

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Farazi, Mena, Michael Houghton, Margaret Murray, and Gary Williamson. Systematic review of the inhibitory effect of extracts from edible parts of nuts on α-glucosidase activity. INPLASY - International Platform of Registered Systematic Review and Meta-analysis Protocols, August 2022. http://dx.doi.org/10.37766/inplasy2022.8.0061.

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Review question / Objective: The aim of this review is to examine inhibitory effect of functional components in extracts from edible nuts on α-glucosidase activity. At the end of this review the following questions will be addressed by summarizing data of in-vitro studies: which nut extract has the strongest inhibitory effect? Which functional component (e.g. polyphenols) has the strongest inhibitory effect against α-glucosidase? Are there any differences between inhibition of α-glucosidase from different sources (e.g. yeast and mammalian)? Condition being studied: Any papers looking at inhibition of α-glucosidase activity (a carbohydrate digestive enzyme; includes sucrase, maltase and isomaltase activities) by extracts of edible parts of nut will be included in this review. Papers looking at other parts of nut plants and other enzymes will be excluded.

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