D-Panose structure
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Common Name | D-Panose | ||
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| CAS Number | 33401-87-5 | Molecular Weight | 504.43700 | |
| Density | 1.75 g/cm3 | Boiling Point | 960ºC at 760 mmHg | |
| Molecular Formula | C18H32O16 | Melting Point | 223ºC | |
| MSDS | USA | Flash Point | 330.1ºC | |
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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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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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Transcriptional analysis of prebiotic uptake and catabolism by Lactobacillus acidophilus NCFM.
PLoS ONE 7(9) , e44409, (2012) The human gastrointestinal tract can be positively modulated by dietary supplementation of probiotic bacteria in combination with prebiotic carbohydrates. Here differential transcriptomics and functional genomics were used to identify genes in Lactobacillus a... |
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Synthesis of glucopyranoside-based ligands for D-myo-inositol 1,4,5-trisphosphate receptors.
Carbohydr. Res. 337(12) , 1067-82, (2002) Adenophostins A and B are naturally occurring glyconucleotides that interact potently with receptors for D-myo-inositol 1,4,5-trisphosphate, an important second messenger molecule in most cell types. Here we describe the design and synthesis of glucopyranosid... |
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Determination of the number of sucrose and acceptor binding sites for Leuconostoc mesenteroides B-512FM dextransucrase, and the confirmation of the two-site mechanism for dextran synthesis.
Arch. Biochem. Biophys. 308(2) , 471-6, (1994) In previous studies on dextransucrase using pulse and chase experiments with [14C]sucrose, Robyt et al. [Arch. Biochem. Biophys. 165 (1974) 634-640] proposed a two-site insertion mechanism to explain the data for the synthesis of dextran. To further establish... |
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The hydrolytic and transferase action of alternanase on oligosaccharides.
Carbohydr. Res. 332(4) , 373-9, (2001) Alternanase is an enzyme which endo-hydrolytically cleaves the alpha-(1-->3), alpha-(1-->6)-linked D-glucan, alternan. The main products are isomaltose, alpha-D-Glcp-(1-->3)-alpha-D-Glcp-(1-->6)-D-Glc and the cyclic tetrasaccharide cyclo[-->6)-alpha-D-Glcp-(1... |
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Panose, a new prebiotic candidate.
Lett. Appl. Microbiol. 49(6) , 666-72, (2009) To investigate the prebiotic potential of two novel candidates, sophorose and panose, with in vitro methods.The growth of single microbial strains was first assessed for both substrates in pure cultures, and panose was further analysed in the simulated colon ... |
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Insights into the reaction mechanism of glycosyl hydrolase family 49. Site-directed mutagenesis and substrate preference of isopullulanase.
Eur. J. Biochem. 271(22) , 4420-7, (2004) Aspergillus niger isopullulanase (IPU) is the only pullulan-hydrolase in glycosyl hydrolase (GH) family 49 and does not hydrolyse dextran at all, while all other GH family 49 enzymes are dextran-hydrolysing enzymes. To investigate the common catalytic mechani... |
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Synthesis of 6'-S-alpha-D-glucopyranosyl-6'-thiomaltose (6(2)-thiopanose) and its effect on the enzymic activity of glucoamylases from Aspergillus niger.
Carbohydr. Res. 228(1) , 299-305, (1992)
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