Neutral detergent residue

To obtain the in vitro true digestibility, the residue from the first buffered rumen liquor stage of the Tilley and Terry (1963) procedure is digested with neutral detergent solution. The ordinary true digestibility is found by... 

The % indigestible cell wall in DM is the residual DM after digestion in rumen liquor (48 h) followed by the neutral detergent procedure and expressed as % sample DM. 

Turn off the heat and immediately filter through the same filter tube previously used for the fat extraction. Wash the residue thoroughly with at least 3 X 20 ml hot distilled water, as it is essential to remove all the neutral detergent solution. Moisten a Suba-Seal and carefully push it into the bottom end of the filter tube as far as the sinter disc. Use dispensers to add 25 ml of... 

Nonionic and even anionic surfactants have also been added in small amounts to DHTDMAC to boost a product s softening efficacy. For example, it was shown in the late 1970s that the performance of a 6% DHTDMAC composition is matched by a mixture of 4.4% DHTDMAC and 0.6% anionic [56] 1.6% DHTDMAC could then be replaced by 0.6% anionic, which is less expensive. That was quite unexpected, as it was generally accepted that fabric softeners must be introduced in the last rinse of the laundering process to avoid their neutralization by the anionic detergent residues on the fabric, which causes the formation of insoluble species. 

The soluble dietary fiber is not measured in the proximate analysis because crude fiber is the residue obtained after the food sample is subjected to sequential hydrolyses with acid and alkali. The crude fiber clearly underestimates values when compared with other methods of analysis such as dietary fiber and detergent fiber. The acid and neutral detergent fiber analyses were developed to estimate hemicellulose, cellulose, and lignin of forages. 

In summary, mild sulfonation of detergent range 10 in a falling film reactor followed by direct neutralization and hydrolysis leads to an IOS system rich in sodium p-hydroxysulfonates and having low concentrations of residual sul-tones, inorganic sulfate, and free oil. 

Found that the anionic form of the Coomassie dye reacts primarily with arginine residues within the macro molecular protein. Coomassie dye reacts to a lesser extent with other basic amino acid residues (His, Lys) and aromatic residues (Try, Tyr, Phe) present in macromolecularproteins, but not with the free amino acids. Dye binding is attributed to van der Waals forces and hydrophobic interactions. The interference seen with bases, detergents, and other compounds can be explained by their effects upon the equilibrium between the three dye forms (cationic, neutral, anionic). 

The structure of the HA2 N-terminal fusion peptide has been probed by a combination of NMR and electron paramagnetic resonance (EPR) in detergent micelles that mimic the lipid bilayer, at both acid and neutral pHs (Han et al, 2001). At both acidic and neutral pH the structure is predominantly helical with a kink where it rises most prominently to the presumptive membrane surface. At lower pH the kink is stronger, there is additional 3io helix, and two charged residues are rotated out of the membrane plane. The stronger kink likely allows the peptide to become more deeply immersed, perhaps disrupting the membrane and facilitating fusion. 

Of particular interest in this connection is the controlled fragmentation of the y-globulin fraction from serum which at neutral pH is surprisingly stable to enzymatic attack. Preliminary results show a highly destructive effect of NBS even at 0°C and pH 5 for only 20 min in the absence of urea or detergent after only one-fifth of the tryptophan residues reacted (Porter, 1960). 

---