![]() Isomaltotriose structure
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Common Name | Isomaltotriose | ||
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CAS Number | 3371-50-4 | Molecular Weight | 504.43700 | |
Density | 1.8 g/cm3 | Boiling Point | 856.6ºC | |
Molecular Formula | C18H32O16 | Melting Point | N/A | |
MSDS | USA | Flash Point | 471.9ºC |
Phytochemical fingerprints of lime honey collected in serbia.
J. AOAC Int. 97(5) , 1259-67, (2015) Composition of phenolic compounds and the sugar content were determined as the basis for characterization of lime honey from Serbia. Particular attention was given to differences in phytochemical profiles of ripe and unripe lime honey and lime tree nectar. Me... |
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Automated deconvolution of overlapped ion mobility profiles.
J. Am. Soc. Mass Spectrom. 25(10) , 1810-9, (2014) Presence of unresolved ion mobility (IM) profiles limits the efficient utilization of IM mass spectrometry (IM-MS) systems for isomer differentiation. Here, we introduce an automated ion mobility deconvolution (AIMD) computer software for streamlined deconvol... |
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Expression, purification and characterization of recombinant α-glucosidase in Pichia pastoris.
Folia Microbiol. (Praha) 55(6) , 582-7, (2010) An expression plasmid containing the agdA gene encoding Aspergillus oryzae ZL-1 α-glucosidase was constructed and expressed in Pichia pastoris X-33. The molar mass of the purified protein was estimated by SDS-PAGE. HPLC analysis showed that the purified enzym... |
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The Gram-negative bacterium Azotobacter chroococcum NCIMB 8003 employs a new glycoside hydrolase family 70 4,6-α-glucanotransferase enzyme (GtfD) to synthesize a reuteran like polymer from maltodextrins and starch.
Biochim. Biophys. Acta 1860 , 1224-36, (2016) Originally the glycoside hydrolase (GH) family 70 only comprised glucansucrases of lactic acid bacteria which synthesize α-glucan polymers from sucrose. Recently we have identified 2 novel subfamilies of GH70 enzymes represented by the Lactobacillus reuteri 1... |
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Analysis of sugars in Chinese rice wine by Fourier transform near-infrared spectroscopy with partial least-squares regression.
J. Agric. Food Chem. 56(16) , 7271-8, (2008) The feasibility of rapid analysis for oligosaccharides, including isomaltose, isomaltotriose, maltose, and panose, in Chinese rice wine by Fourier transform near-infrared (FT-NIR) spectroscopy together with partial least-squares regression (PLSR) was studied ... |
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Transport of sugars, including sucrose, by the msm transport system of Streptococcus mutans.
J. Dent. Res. 72(10) , 1386-90, (1993) The range of substrates transported by the sugar-binding protein-dependent msm (multiple sugar metabolism) system of S. mutans was investigated. By determining the ability of unlabeled sugar to compete with radiolabeled melibiose transport, we have demonstrat... |
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A binding protein-dependent transport system in Streptococcus mutans responsible for multiple sugar metabolism.
J. Biol. Chem. 267(7) , 4631-7, (1992) An 11-kilobase gene region of Streptococcus mutans has been identified which contains eight contiguous genes involved with the uptake and metabolism of multiple sugars (the msm system). Sequence analysis of this region indicates that several of these genes sp... |
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Cooperative action of alpha-glucanotransferase and maltogenic amylase for an improved process of isomaltooligosaccharide (IMO) production.
J. Agric. Food Chem. 50(10) , 2812-7, (2002) Maltogenic amylase and alpha-glucanotransferase (alpha-GTase) were employed in an effort to develop an efficient process for the production of isomaltooligosaccharides (IMOs). Bacillus stearothermophilus maltogenic amylase (BSMA) and alpha-GTase from Thermoto... |
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Effect of sugars on storage stability of lyophilized liposome/DNA complexes with high transfection efficiency.
Int. J. Pharm. 356(1-2) , 69-75, (2008) Cationic lipid-based gene delivery systems have shown promise in transfecting cells in vitro and in vivo. However, liposome/DNA complexes tend to form aggregates after preparation. Lyophilization of these systems, therefore, has become of increasing interest.... |
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Characterization of novel thermostable dextranase from Thermotoga lettingae TMO.
Appl. Microbiol. Biotechnol. 85(3) , 581-7, (2010) Biochemical properties of a putative thermostable dextranase gene from Thermotoga lettingae TMO were determined in a recombinant protein (TLDex) expressed in Escherichia coli and purified to sevenfold apparent homogeneity. The 64-kDa protein displayed maximum... |