15718
D-(+)-Maltose monohydrate
Synonym(s):
4-O-α-D-Glucopyranosyl-D-glucose, Maltobiose
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About This Item
Empirical Formula (Hill Notation):
C12H22O11 · H2O
CAS Number:
Molecular Weight:
360.31
Beilstein:
93798
EC Number:
MDL number:
UNSPSC Code:
12352201
PubChem Substance ID:
optical activity
[α]20/D +137±2°, c = 10% in H2O (calc.of H2O free subst.)
impurities
≤0.001% heavy metals (as Pb)
5-6% water (Karl Fischer)
ign. residue
≤0.05% (as SO4)
solubility
H2O: soluble 180 g/L at 20 °C
anion traces
chloride (Cl-): ≤50 mg/kg
sulfate (SO42-): ≤50 mg/kg
SMILES string
O.OC[C@@H](O)[C@@H](O[C@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@H]1O)[C@H](O)[C@@H](O)C=O
InChI
1S/C12H22O11.H2O/c13-1-4(16)7(18)11(5(17)2-14)23-12-10(21)9(20)8(19)6(3-15)22-12;/h1,4-12,14-21H,2-3H2;1H2/t4-,5+,6+,7+,8+,9-,10+,11+,12+;/m0./s1
InChI key
HBDJFVFTHLOSDW-DNDLZOGFSA-N
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Application
D-Maltose has been used for preparing Diamond′s modified TYM medium which is utilized for studying the pharmacodynamic impacts of metronidazole on Trichomonas vaginalis by using time-kill assay. It has also been used as a substrate for the identification, differentiation and characterization of enzymes such as maltase(s); maltose alpha-D-glucosyltransferase(s); maltose-transporting ATPase(s); maltose O-acetyltransferase(s), maltose epimerase(s) and phosphorylase(s). Further, D-Maltose has been used to study maltose-binding proteins and disaccharide transport systems. Other application of D-maltose was in disproportionation activity enzyme assays.
Biochem/physiol Actions
D-Maltose is broken down in the presence of beta-amylases to produce two molecule of glucose followed by glucose metabolism and release of energy. The malP and malQ genes in bacterial genome produce essential enzymes required for maltose metabolism. Beta-amylases are present in plants and bacteria whereas maltase present in humans breaks down the maltose in diet.
Maltose is a disaccharide containing two glucose molecules with an α(1→4) glycosidic linkage. Maltose can be derived from starch in food through the action of amylase. Maltose can be found in many food products, including beer, cereals, and pasta.
Storage Class Code
13 - Non Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
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B A van der Veen et al.
European journal of biochemistry, 267(3), 658-665 (2000-01-29)
Cyclodextrin glycosyltransferase (CGTase) catalyzes three transglycosylation reactions via a double displacement mechanism involving a covalent enzyme-intermediate complex (substituted-enzyme intermediate). Characterization of the three transglycosylation reactions, however, revealed that they differ in their kinetic mechanisms. Disproportionation (cleavage of an alpha-glycosidic bond
B A van der Veen et al.
The Journal of biological chemistry, 276(48), 44557-44562 (2001-09-14)
Cyclodextrin-glycosyltransferases (CGTases) (EC ) preferably catalyze transglycosylation reactions with glucosyl residues as acceptor, whereas the homologous alpha-amylases catalyze hydrolysis reactions using water as acceptor. This difference in reaction specificity is most likely caused by the acceptor binding site. To investigate
G M Gray
The Journal of nutrition, 122(1), 172-177 (1992-01-01)
Starch digestion and absorption is augmented appreciably by physical processing of grain or legume and by heating to 100 degrees C for several minutes before its ingestion. Starch, a polysaccharide composed of alpha 1,4-linked glucose units (amylose) and alpha 1,4-1,6-linked
D E Nix et al.
Antimicrobial agents and chemotherapy, 39(8), 1848-1852 (1995-08-01)
The pharmacodynamic effects of metronidazole on Trichomonas vaginalis have been poorly characterized. The present in vitro study was performed to characterize the relationship between killing of trichomonads and metronidazole exposure (metronidazole concentration and time of exposure). Five laboratory strains and
W Boos et al.
Microbiology and molecular biology reviews : MMBR, 62(1), 204-229 (1998-04-08)
The maltose system of Escherichia coli offers an unusually rich set of enzymes, transporters, and regulators as objects of study. This system is responsible for the uptake and metabolism of glucose polymers (maltodextrins), which must be a preferred class of
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