Time enzymatic

Time Enzymatic protein degradation is a function of time. Lengthy procedures and... 

Ozone-induced oxidation of fibrin-stabilizing factor influences to a considerable extent on its enz5miatic activity. It was shown that enzymatic activity of FXIIIa formed from oxidized FXIII-AjB (Sample 1) was lower compared with non-oxidized FXIIIa (Sample 4) with enzymatic activity of 500 units/ml and was equal to approximately 400 units/ml. At the same time enzymatic activity of FXIIIa obtained from oxidized samples 2 and 3 decreased several times and was equal to -120 and 60 units/ml, respectively. The decline of enz5miatic activity (40 units/ml) took place after oxidation of FXIIIa (Sample 4). These results demonstrate that the reduction of enzymatic activity depends significantly on the stage of the pFXIII conversion into FXIIIa at which oxidation was carried out. 

The signal enhancement produced by liposomal biolabels is instantaneous, eliminating the timed enzymatic incubation step required in ELISA. 

Most commercial products are partially deacety-lated (chitin 10% and chitosan 60%). Complete deacetylation is reached by repeating the - hydrolysis reaction several times. Enzymatic deacetylation yields a less degraded product. 

The conventional electrochemical reduction of carbon dioxide tends to give formic acid as the major product, which can be obtained with a 90% current efficiency using, for example, indium, tin, or mercury cathodes. Being able to convert CO2 initially to formates or formaldehyde is in itself significant. In our direct oxidation liquid feed fuel cell, varied oxygenates such as formaldehyde, formic acid and methyl formate, dimethoxymethane, trimethoxymethane, trioxane, and dimethyl carbonate are all useful fuels. At the same time, they can also be readily reduced further to methyl alcohol by varied chemical or enzymatic processes. 

Km for an enzymatic reaction are of significant interest in the study of cellular chemistry. From equation 13.19 we see that Vmax provides a means for determining the rate constant 2- For enzymes that follow the mechanism shown in reaction 13.15, 2 is equivalent to the enzyme s turnover number, kcat- The turnover number is the maximum number of substrate molecules converted to product by a single active site on the enzyme, per unit time. Thus, the turnover number provides a direct indication of the catalytic efficiency of an enzyme s active site. The Michaelis constant, Km, is significant because it provides an estimate of the substrate s intracellular concentration. 

Process Va.ria.tlons. The conventional techniques for tea manufacture have been replaced in part by newer processing methods adopted for a greater degree of automation and control. These newer methods include withering modification (78), different types of maceration equipment (79), closed systems for fermentation (80), and fluid-bed dryers (81). A thermal process has been described which utilizes decreased time periods for enzymatic reactions but depends on heat treatment at 50—65°C to develop black tea character (82). It is claimed that tannin—protein complex formation is decreased and, therefore, greater tannin extractabiUty is achieved. Tea value is beheved to be increased through use of this process. 

CeUulosic materials, such as farm wastes, can be upgraded for animal feed by simply bringing them into contact with ammonia (qv). The ceUulose sweUs and is made more digestible, and at the same time some ammonia nitrogen, which is a nutrient for mminants, is left behind. Supercritical ammonia improves susceptibiHty to enzymatic hydrolysis (17). 

Germicidal Properties. The germicidal activity of aqueous chlorine is attributed primarily to HOCl. Although the detailed mechanism by which HOCl kills bacteria and other microorganisms has not been estabUshed, sufficient experimental evidence has been obtained to suggest strongly that the mode of action involves penetration of the cell wall followed by reaction with the enzymatic system. The efficiency of destmction is affected by temperature, time of contact, pH, and type and concentration of organisms (177). 

Urea Enzymatic Dialysis Method. This method (16) uses 8 M urea [57-13-6] to gelatinize and facUitate removal of starch and promote extraction of the soluble fiber at mild (50°C) temperatures. EoUowing digestion with heat-stable a-amylase and protease, IDE is isolated by filtration or I DE is obtained after ethanol precipitation. Values for I DE are comparable to those obtained by the methods described eadier, and this method is less time-consuming than are the two AO AC-approved methods. Corrections for protein are required as in the AO AC methods. 

If the inhibitor combines irreversibly with the enzyme—for example, by covalent attachment—the kinetic pattern seen is like that of noncompetitive inhibition, because the net effect is a loss of active enzyme. Usually, this type of inhibition can be distinguished from the noncompetitive, reversible inhibition case since the reaction of I with E (and/or ES) is not instantaneous. Instead, there is a time-dependent decrease in enzymatic activity as E + I El proceeds, and the rate of this inactivation can be followed. Also, unlike reversible inhibitions, dilution or dialysis of the enzyme inhibitor solution does not dissociate the El complex and restore enzyme activity. 

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