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Loading reactions

LOAD REACTION WITH 5 GRAMS DI-T-BUTYL PEROXIDE WAIT 60 MINUTES ... [Pg.186]

The sequential batch reactor (SBR) consists of a vessel operated under batch conditions according to the time schedule reported in Fig. 3. The symbols Fill, React, Settle, Draw and Idle refer to the typical sequential phases of operation loading, reaction, biophase settling, discharging and the idle time. The reaction period may be split into two sub-phases an anaerobic phase and an aerobic phase. The aerobic sub-phase is devoted to convert products of the azo-dye anaerobic... [Pg.111]

To make the DERA-catalyzed process commercially attractive, improvements were required in catalyst load, reaction time, and volumetric productivity. We undertook an enzyme discovery program, using a combination of activity- and sequence-based screening, and discovered 15 DERAs that are active in the previously mentioned process. Several of these enzymes had improved catalyst load relative to the benchmark DERA from E. coli. In the first step of our process, our new DERA enzymes catalyze the enantioselective tandem aldol reaction of two equivalents of acetaldehyde with one equivalent of chloroacetaldehyde (Scheme 20.6). Thus, in 1 step a 6-carbon lactol with two stereogenic centers is formed from achiral 2-carbon starting materials. In the second step, the lactol is oxidized to the corresponding lactone 7 with sodium hypochlorite in acetic acid, which is crystallized to an exceptionally high level of purity (99.9% ee, 99.8% de). [Pg.413]

Steps 3-4 of Figure 29.5 Carboxylatlon and Acyl Transfer The third step is a loading reaction in which acetyl GoA is carboxylated by reaction with HG03 and ATP to yield malonyl GoA plus ADP. This step requires the coenzyme biotin, which is bonded to the lysine residue of acetyl GoA carboxylase and acts as a carrier of GO2. Biotin first reacts with bicarbonate ion to give A -carboxybiotin, which then reacts with the enolate ion of acetyl GoA and transfers the CO2 group. Thus, biotin acts as a carrier of GO2, binding it in one step and releasing it in another. [Pg.1140]

Figure 5.5 The CM-C-25 Sephadex resin before and after loading reaction mixture. Figure 5.5 The CM-C-25 Sephadex resin before and after loading reaction mixture.
A proper choice of the reaction medium for the metal loading reaction is very important, especially when nonporous resins are used as polymer supports. Thus, a solvent must be chosen that can solubilize the metal precursor, but which is also capable of swelling the nonporous resin to an appreciable extent swelling is needed to guarantee accessibility of the reactants to most of the functional groups. [Pg.312]

Fig. 3. Generic reaction sequence for the FASs. ACP, acyl carrier protein AT, acetyltransferase MT, malonyl transferase KS, P-ketoacyl synthase KR, P-ketoacyl reductase DH, dehydrase ER, enoyl reductase TE, thioesterase FT, palmitoyl transferase. In the animal FAS the acetyl and malonyl loading reactions are catalyzed by the same acyl transferase and the chain-termination reaction is catalyzed by a thioesterase. In the fungal FAS, the malonyl loading and palmitoyl unloading reactions are catalyzed by the same acyl transferase. Stereochemical analyses in the laboratories of Comforth and Hammes established that in both animal and fungal FASs the KS-catalyzed condensation reaction proceeds with inversion of configuration at the malonyl C2 position, followed by KR-catalyzed reduction of the 3-keto moiety to the 3R alcohol by transfer of the pro-4S hydride from NADPH, and DH-catalyzed dehydration to a trans-enoyl moiety by the syn elimination of the 2S hydrogen and the 3/f hydroxyl as water. However, the stereochemistry of the final reduction reaction catalyzed by ER domain proceeds with different stereochemistry. The animal FAS transfers the pro-4R hydride of NADPH to the pro-3/f position with simultaneous addition of a solvent proton to the pro-2S position, whereas the fungal FAS takes the pro-4S hydride of NADPH into the pro-3S position and the solvent proton is incorporated at the pro-25 position. Fig. 3. Generic reaction sequence for the FASs. ACP, acyl carrier protein AT, acetyltransferase MT, malonyl transferase KS, P-ketoacyl synthase KR, P-ketoacyl reductase DH, dehydrase ER, enoyl reductase TE, thioesterase FT, palmitoyl transferase. In the animal FAS the acetyl and malonyl loading reactions are catalyzed by the same acyl transferase and the chain-termination reaction is catalyzed by a thioesterase. In the fungal FAS, the malonyl loading and palmitoyl unloading reactions are catalyzed by the same acyl transferase. Stereochemical analyses in the laboratories of Comforth and Hammes established that in both animal and fungal FASs the KS-catalyzed condensation reaction proceeds with inversion of configuration at the malonyl C2 position, followed by KR-catalyzed reduction of the 3-keto moiety to the 3R alcohol by transfer of the pro-4S hydride from NADPH, and DH-catalyzed dehydration to a trans-enoyl moiety by the syn elimination of the 2S hydrogen and the 3/f hydroxyl as water. However, the stereochemistry of the final reduction reaction catalyzed by ER domain proceeds with different stereochemistry. The animal FAS transfers the pro-4R hydride of NADPH to the pro-3/f position with simultaneous addition of a solvent proton to the pro-2S position, whereas the fungal FAS takes the pro-4S hydride of NADPH into the pro-3S position and the solvent proton is incorporated at the pro-25 position.
Designed, fabricated, and installed a generic fuel processor and test stand to study the heat transfer characteristics of monolith loaded reaction zones. [Pg.309]

Prep. Washing Au loading Reaction Conversion method (wt%) temp. (K) %)... [Pg.461]

C = diameter at gasket load reaction, in. go = thickness of hub at small end, in. gi = thickness of hub at back of flange, in. H = hydrostatic end force, lb Hn = hydrostatic end force on area inside of flange, lb... [Pg.37]

Thickness required in skirt at compression plate or ring due to maximum holt load reaction. [Pg.199]


See other pages where Loading reactions is mentioned: [Pg.1140]    [Pg.79]    [Pg.87]    [Pg.308]    [Pg.205]    [Pg.155]    [Pg.231]    [Pg.123]    [Pg.225]    [Pg.226]    [Pg.232]    [Pg.300]    [Pg.320]    [Pg.321]    [Pg.377]    [Pg.23]    [Pg.92]    [Pg.723]    [Pg.166]    [Pg.167]    [Pg.238]    [Pg.258]    [Pg.259]    [Pg.311]    [Pg.17]    [Pg.162]    [Pg.79]    [Pg.87]    [Pg.364]    [Pg.366]    [Pg.32]    [Pg.33]    [Pg.257]    [Pg.299]    [Pg.489]    [Pg.59]    [Pg.654]    [Pg.118]    [Pg.142]   
See also in sourсe #XX -- [ Pg.87 ]

See also in sourсe #XX -- [ Pg.87 ]




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