Industrial Application of Enzymes on Carbohydrate-Based Material Downloaded from pubs.acs.org by 179.61.201.83 on 11/24/18. For personal use only.
Figure 4.2. Sacchrification of maize amylopectin by a-l,4-glucan layse to 7,5anhydrqfructose (AF). (A). Before dosing of the glucan layse. (B). 3 days after the dosing of the algal GLql-glucan lyase.
Figure 6.3. Photograph of the use of the Eggleston (14) titration method to measure the activity of commercial dextranases at the factory
Figure 6.4. Changes in activity of "concentrated" and "non-concentrated" dextranases stored under (top) simulatedfactory storage conditions (ambient temperature -25 °C), and (bottom) refrigerated conditions (4 °C) over a 90 day sugarcane processing season. From Eggleston and Monge (1).
Figure 6.5. Effect of Brix on dextranase activity. The "concentrated" dextranase was diluted 4.6Xto make it economically equivalent to the nearest priced "non-concentrated" dextranase. From Eggleston and Monge (1).
Figure 6.6. Diagram to illustrate the contact between dextranase and different concentrations of dextran. Circles depict volumes and squares depict enzyme molecules. The action of a working solution of "concentrated" dextranase (>25,000 - 58,000 DU/mL) to improve contact in factory process is also shown. Modifiedfrom Eggleston et al. (15).
Figure 11.4. Enzymatic production of hydrogen peroxide with and without fabric with increasing dosage of GO.
Figure 11.5. Whiteness increase of cotton fabric based on GO concentration compared to the unbleached control; at two pH settings (7, 10.5). The fabric was present in the bath during the entire process.
Figure 11.6. Light-sensitized production of hydrogen peroxide by riboflavin with reaction time at pH 12.3 and 13.3 (white lamp 75 W).
Figure 11.7. Whiteness increase of cotton fabric treated with riboflavin as a function of treatment time and pH compared to the scoured control (pH value of previous step: 13.3).
Figure 11.8. Production of hydrogen peroxide by riboflavin and lumiflavin with various combinations of His, Lys, Asp, and Arg in equal mole ratio. The amount of each amino acid used in this experiment was 3.2 x 1(T M. 4
Figure 11.9. Production of hydrogen peroxide by lumiflavin, riboflavin, and FMN with a mole ratio of His and Lys of 1:1.
glycopeptide are the following: L Lysozyme, 2. Asp-48, 3. Asp-66,4. Asp-87, 5. Asp-119, 6. COOH-129, 7. Glu-35
Figure 12.1. Molecular models of lysozyme-bound conjugates of cellopentaose-(3) Gly-O-6-glycyl-glycine ester. The eight structures shown are CPK models. Atom color types are as follows: oxygen (red); carbon (green); nitrogen (blue); sulfur (yellow) and the cellopentaose is highlighted in blue: all models are oriented with the enzyme active site cleft in the right lower quadrant of the protein structure. The lysozyme (1) crystal structure may be compared with glycoprotein conjugates structures 2-7 to visualize potential contact regions between the cellulose (represented here by the cellopentaose) and the lysozyme. Amide linkages to the protein with the
Figure 12.7. Reaction progress curves of the paranitroanilide peptide conjugate Cellulose-APS-suc-Ala-Ala-Pro-Val-pNA toparanitroaniline was monitored at 405 nm (see figure 6 for reaction) for 1 hr. Hydrolysis of substrate was monitored by combining ~ 5mg of sample with the indicated concentration of elastase. The elastase (Athens) was prepared in a phosphate buffer with a pH of 7.6 (0.2 M sodium phosphate, 0.5 MNaCl, and 6.6% DMSO). HNE units of activity employed in the assay rangedfrom 5.0 x 1 Or units to 6.0 units. In each well of a 96-well microtiter plate 50 pL of enzyme was reacted with -5 mg of HNE substrate bound paper. The enzymatic hydrolysis of the immobilized substrate on paper was monitored at 405 nm with incubation at$7°C using a Bio-Rad Microplate Reader for 1 h. The color that developed on the HNE substrate-bound paper was analyzed by Datacolor International Spectra/lash 500. Data was obtained in reflectance mode and converted to absorbance. 3
Figure 15.1. fl-Cellobiose from its crystal structure (11) showing the linkage torsion angles (p and if/, as well as the numbering of carbon and ring and linkage oxygen atoms. We define cp and if/ (here cp05 '-CI '-04-C4 = -76.3° and y/C5-C4-04-Cl' = -132.3°) based on the ring atoms 05' and C5 instead of the commonly used HI ' and H4 atoms because protons are not found experimentally in most studies of proteins, and are not well located even in many studies of small molecule crystals.
Figure 15.2. The endocellulase El catalytic domain (balls and sticks) with a complexed cellotetraose molecule (space-filling model) from the 1ECE crystal structure (12). The 1ECE designation is an ID code from the Protein Data Bank. Each entry has its own ID code. See (13).
^igure 15.3. Comparison of cellotetraose fragments from the Protein Data Bank. (See page 211 for the full caption.)
Figure 15.7. Cellobiose-like 3'-deoxy-fi-lactose in the reported conformation from the 1FV3 protein complex (upper drawing). See also Figure 5 for the location in
