Maltohexaose
Maltohexaose structure
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Common Name | Maltohexaose | ||
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| CAS Number | 34620-77-4 | Molecular Weight | 990.85900 | |
| Density | 1.87g/cm3 | Boiling Point | 1307.8ºC at 760mmHg | |
| Molecular Formula | C36H62O31 | Melting Point | 204-206°C | |
| MSDS | Chinese USA | Flash Point | 744.7ºC | |
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Microbiota and metabolites of aged bottled gueuze beers converge to the same composition.
Food Microbiol. 47 , 1-11, (2015) Gueuze beers are prepared by mixing young and old lambic beers and are bottle-refermented spontaneously for aging. The present study analyzed the microbiota and metabolites present in gueuze beers that were aged between a few months and up to 17 years. Yeasts... |
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Octanoylation of early intermediates of mycobacterial methylglucose lipopolysaccharides.
Sci. Rep. 5 , 13610, (2015) Mycobacteria synthesize unique intracellular methylglucose lipopolysaccharides (MGLP) proposed to modulate fatty acid metabolism. In addition to the partial esterification of glucose or methylglucose units with short-chain fatty acids, octanoate was invariabl... |
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Tandem mass spectrometry of isomeric aniline-labeled N-glycans separated on porous graphitic carbon: Revealing the attachment position of terminal sialic acids and structures of neutral glycans.
Rapid Commun. Mass Spectrom. 29 , 1268-78, (2015) Quantitative monitoring of changes in the N-glycome upon disease has gained significance in the context of biomarker discovery. Separation and quantification of isobaric glycan isomers can be attained by using high-performance liquid chromatography/electrospr... |
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Development of brewing science in (and since) the late 19th century: molecular profiles of 110-130year old beers.
Food Chem. 183 , 227-34, (2015) The 19th century witnessed many advances in scientific enzymology and microbiology that laid the foundations for modern biotechnological industries. In the current study, we analyze the content of original lager beer samples from the 1880s, 1890s and 1900s wi... |
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UP-HILIC-MS/MS to Determine the Action Pattern of Penicillium sp. Dextranase.
J. Am. Soc. Mass Spectrom. 26 , 1174-85, (2015) Investigation of the action pattern of enzymes acting on carbohydrates is challenging, as both the substrate and the digestion products are complex mixtures. Dextran and its enzyme-derived oligosaccharides are widely used for many industrial applications. In ... |
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Properties and functions of the storage sites of glycogen phosphorylase.
J. Biochem. 157 , 451-8, (2015) Glycogen phosphorylase (GP) is biologically active as a dimer of identical subunits. Each subunit has two distinct maltooligosaccharide binding sites: a storage site and a catalytic site. Our characterization of the properties of these sites suggested that GP... |
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Expression, crystallization and preliminary X-ray crystallographic studies of Klebsiella pneumoniae maltohexaose-producing alpha-amylase.
Acta Crystallogr. D Biol. Crystallogr. 60(Pt 12 Pt 2) , 2352-4, (2004) A recombinant form of Klebsiella pneumoniae maltohexaose-producing alpha-amylase has been overexpressed in Escherichia coli and purified to homogeneity. Crystals were obtained at 293 K by the microbatch technique using 80 mM sodium/potassium phosphate buffer ... |
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Role of Trp140 at subsite -6 on the maltohexaose production of maltohexaose-producing amylase from alkalophilic Bacillus sp.707.
Protein Sci. 15(3) , 468-77, (2006) Maltohexaose-producing amylase (G6-amylase) from alkalophilic Bacillus sp.707 predominantly produces maltohexaose (G6) in the yield of >30% of the total products from short-chain amylose (DP=17). Our previous crystallographic study showed that G6-amylase has ... |
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Characterization of a Novel Maltose-Forming α-Amylase from Lactobacillus plantarum subsp. plantarum ST-III.
J. Agric. Food Chem. 64 , 2307-14, (2016) A novel maltose (G2)-forming α-amylase from Lactobacillus plantarum subsp. plantarum ST-III was expressed in Escherichia coli and characterized. Analysis of conserved amino acid sequence alignments showed that L. plantarum maltose-producing α-amylase (LpMA) b... |
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Oligosaccharide binding in Escherichia coli glycogen synthase.
Biochemistry 48(42) , 10089-97, (2009) Glycogen/starch synthase elongates glucan chains and is the key enzyme in the synthesis of glycogen in bacteria and starch in plants. Cocrystallization of Escherichia coli wild-type glycogen synthase (GS) with substrate ADPGlc and the glucan acceptor mimic HE... |