Many organic and inorganic bases were found to be effective in retarding the rate of change of the various properties of the alcohol, but only n-butyl amine and piperidine will be reported at this time.To separate samples of furfuryl alcohol were added, by weight, 0.1,0.3, and 3.0 per cent n-butyl amine and piperidine, respectively. As was the case in the thermal stability study, approximately 40 cc. of each sample were then sealed in Pyrex glass tubes, placed in bombs, and heated in an oven at 150' C .for the indicated period of time.The differences between the physical properties of the stabilized and control samples, prior to heat treatment, are due to the presence of the stabilizer. It is evident from the data that both n-butyl amine and piperidine greatly retard the rate of intermolecular dehydration of furfuryl alcohol, as measured by the amount of water split out. When calculated (as in Figure 2) in terms of per cent furfuryl alcohol transformed to C10H1003, after 10.5 hours a t 150" C. the alcohol alone is transformed to the extent of 33 per cent; in the presence of 0.1 per cent of the stabilizers, this value is only 0.4 per cent with n-butyl amineThe results obtained are given in Table 11. and 1.1 per cent with piperidine. There is no advantage in employing these stabilizers in concentrations higher than 0.1 per cent of the furfuryl aleohol, and there is the disadvantage of discoloring the latter to a greater extent.In hydrogenating furfuryl alcohol to tetrahydrofurfuryl alcohol, a considerable amount of high-boiling residue is obtained. We believe that a sizable proportion of this residue results from the formation of furfuryl alcohol condensation products such as have been described. Use of stabilizers in the hydrogenation process may therefore lead to higher yields of tetrahydrofurfuryl alcohol. Literature CitedAssoc. Official Agr.The adhesive strength, hydrolytic cleavage with sodium hydroxide, and dispersion characteristics of soybean protein are interrelated. Undenatured soybean protein gives low adhesive values when dispersed in alkaline salts but high adhesive values when dispersed in sodium hydroxide. A mild hydrolytic treatment of soybean protein with sodium hydroxide will change the dispersibility of soybean protein so that it will have good adhesive strength when dispersed in alkaline salts but not so good as the undenatured protein dispersed in sodium hydroxide. The dithionite salts (NaZStOd and ZnSSO4) are the best agents so far discovered for bleaching soybean protein. Coated paper has been prepared in the laboratory which shows the undenatured soybean protein to have higher adhesive strength and a lighter color than a good grade of commercial casein.
The reaction between formaldehyde and proteins is of paramount importance in the development of protein plastics (2), coatings, sizes, adhesives, and fibers. It has been used in these industries as a so-called hardening process for many years.In processes that employ protein dispersions it has not oeen found possible to combine the formaldehyde with the protein before use, because they react with each other at a rather rapid rate to cause the formation of a precipitate. Therefore the formaldehyde treatment must be a separate step in the process where it is used. Attempts have been made to simplify such processes by using certain compounds in the protein dispersion that give a delayed formaldehyde reaction, but as yet they have not attained any marked success.In the early literature on the protein-formaldehyde combination, which has been reviewed by Gortner (5), it has been postulated to be a reaction between the formaldehyde and the free amino groups of the protein.Many studies have been made on the analogous reaction between formaldehyde and amino acids (6), but even for these simpler systems there has been no general agreement on the structure of the compounds formed.Recently attempts to define the protein-formaldehyde linkage by means of x-ray diffraction studies have been made (4), but up to the present time they have yielded no characteristic pattern.Because of the desire for obtaining greater water resistance in the abovementioned protein products and because the formaldehyde reaction appears to be the most promising means of accomplishing this result, a
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