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Maltose analysis

In situ quantitation The in situ fluorimetric analysis was made under long-wavelength UV light (2eic = 365 nm, An > 560 nm) and is illustrated in Figure 1. The detection limits for maltose, glucose and fructose were ca. 10 ng substance per chromatogram zone. [Pg.165]

The separation was carried out on a TSKgel Amide-80 column 4.6 mm i.d. and 25 cm long with a mobile phase consisting of a 80% acetonitrile 20% water mixture. The flow rate was 1 ml/min and the column was operated at an elevated temperature of 80°C. The saccharides shown were 1/ rhamnose, 2/ fucose, 3/ xylose, 4/ fructose, 5/ mannose, 6/ glucose, 7/ sucrose and 8/ maltose. The analysis was completed in less than 20 minutes. These types of separations including other biomonomers, dimers and polymers are frequently carried out employing refractive index detection. [Pg.186]

With data obtained by the analysis of fusion proteins consisting of a domain unrelated to poly(3HB) metabolism (e.g., maltose binding protein MalE or glutathione-S-transferase and the poly(3HB) depolymerase binding domain [57,59-61]. [Pg.305]

Early reports on levan are obscured by incomplete descriptions of impure products.2 96 Greig-Smith found that Bacillus levaniformans(1) produced levan from sucrose96" in suitable nutrient solutions, but not from D-glucose, D-fructose, lactose or maltose.966 He therefore assumed that levan could only be formed from the nascent D-fructose and D-glucose resulting from the inversion of sucrose. Hydrolysis of levan yielded D-fructose only, and analysis of levan agreed with the empirical formula (C HiriOi) it was noted that levan was closely related to inulin but was not identical with it. [Pg.243]

CL emission. The system allows a simple determination of phosphate in 3 min with a linear range of 4.8-160 pM. Owing to its sensitivity, this method could be satisfactorily applied to the analysis of maximum permissible phosphate concentrations in natural waters [42-44], Also, the maltose-phosphorylase, mutar-ose, and glucose oxidase (MP-MUT-GOD) reaction system combined with an ARP-luminol reaction system has been used in a highly sensitive CL-FIA sensor [45], In this system, MP-MUT-GOD is immobilized on A-hydroxysuccinimide beads and packed in a column. A linear range of 10 nM-30 pM and a measuring time of 3 min were provided, yielding a limit of detection of 1.0 pM as well as a satisfactory application in the analysis of river water. [Pg.578]

An analytical method for a butterscotch would run as follows dilute the sample 1 2000 and pass through a 0.2-micron filter. The dextrose, fructose, maltose and maltotriose can then be measured directly. In contrast, the same analysis would probably require two chromatograms performed with different mobile phases using the amino-column HPLC method. [Pg.24]

In order to gain some information about the fundamentals of the hydrothermal carbonization process, the hydrothermal carbonization of different carbohydrates and carbohydrate products was examined [12, 13]. For instance, hydrothermal carbons synthesized from diverse biomass (glucose, xylose, maltose, sucrose, amylopectin, starch) and biomass derivatives (HMF and furfural) were treated under hydrothermal conditions at 180 °C and were analyzed with respect to their chemical and morphological structures by SEM,13 C solid-state NMR and elemental analysis. This was combined with GC-MS experiments on residual liquor solutions to analyze side products... [Pg.202]

Figure 3. Schematic diagram of the hydrogen-bond structure of p-maltose monohydrate (MALTOS11). The anrows indicate infinite chains. Distances and angles are from the neutron diffraction analysis. Figure 3. Schematic diagram of the hydrogen-bond structure of p-maltose monohydrate (MALTOS11). The anrows indicate infinite chains. Distances and angles are from the neutron diffraction analysis.
MALTOSE 1-EPIMERASE MALTOSE PHOSPHORYLASE MALTOSE PHOSPHORYLA.se MALYL-CoA LYASE MAMILLARY MODEL CATENARY MODEL COMPARTMENTAL ANALYSIS Mandelate,... [Pg.759]

When maltose was treated with 8 molar equivalents of benzoyl chloride in pyridine at —40°, it afforded octa-0-benzoyl-/3-maltose, l,2,6,2, 3, 4, 6 -hepta-0-benzoyl-/3-maltose, and l,2,6,2, 3, 6 -hexa-0-benzoyl-/3-maltose in yields of 3, 79, and 12%, respectively.69 Similar treatment of methyl /3-maltoside with 7 molar proportions of benzoyl chloride in pyridine gave crystalline methyl 2,6,2, 3, 4, 6 -hexa-0-benzoyl -/3 - maltoside and methyl 2,6,2, 3, 6 -penta-O -benzoyl -/3 -maltoside in yields of 71 and 23%, respectively.69 Analysis of the relative yields of the products of these reactions suggests that, after HO-3, the 4 -hydroxyl group in maltose and methyl /3-maltoside is the most hindered. Benzoylation of methyl 4, 6 -0-benzylidene-/3-maltoside with 10 molar proportions of reagent gave 2,6,2, 3 -tetra-0-benzoyl-4, 6 -0-benzylidene-/3-maltoside (71%) and an equimolar mixture (22%) of the 2,6,2 - and 2,6,3 -tribenzoates. These results indicated that the order of reactivity of the hydroxyl groups towards acid halides in pyridine is HO-2, HO-6 > HO-2 HO-3 > HO-3. [Pg.226]

Table I (104) shows the yields of products from maltose to malto-pentaose recovered from digests of 0.2 M crystalline a-D-glucosyl fluoride with crystalline a-amylase preparations from six different biological sources. The digests were incubated at 30 °C for 10 minutes, heat inactivated, and chromatographed for product isolation and analysis. Table I (104) shows the yields of products from maltose to malto-pentaose recovered from digests of 0.2 M crystalline a-D-glucosyl fluoride with crystalline a-amylase preparations from six different biological sources. The digests were incubated at 30 °C for 10 minutes, heat inactivated, and chromatographed for product isolation and analysis.
The analysis of maltose syrups is carried out similarly to that of glucose, determinations of the reducing sugars and dextrin being of particular importance. With malt extracts, a determination of the diastatic power may also be required. [Pg.143]


See other pages where Maltose analysis is mentioned: [Pg.477]    [Pg.453]    [Pg.9]    [Pg.320]    [Pg.354]    [Pg.339]    [Pg.105]    [Pg.120]    [Pg.136]    [Pg.250]    [Pg.433]    [Pg.73]    [Pg.73]    [Pg.17]    [Pg.328]    [Pg.362]    [Pg.12]    [Pg.288]    [Pg.290]    [Pg.379]    [Pg.495]    [Pg.223]    [Pg.46]    [Pg.58]    [Pg.68]    [Pg.292]    [Pg.295]    [Pg.138]    [Pg.477]    [Pg.16]    [Pg.23]    [Pg.336]    [Pg.649]    [Pg.661]    [Pg.661]    [Pg.669]    [Pg.81]   
See also in sourсe #XX -- [ Pg.33 ]




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