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The Chemistry of the Strength of Wheat Flour

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The Chemistry of the Strength of Wheat Flour THE CHEMISTRY OF THE STRENGTH OF WHEAT FLOUR. BY HERBERT ERNEST WOODMAN, PH.D., D.SC. (From the Animal Nutrition Institute, School of Agriculture, Cambridge University.) IT is well known that different flours vary enormously in respect of the size and shape of loaf they yield on baking. The factor which determines the quality of flour in this connection has been termed " strength" and the latter has been denned as "the capacity of flour for making large well-piled loaves"(l). Many views have been held from time to time regarding the ex- planation of flour strength from the chemical standpoint. The earliest view was that strength was determined by the gluten content of the flour, which by virtue of its tenacity was able to retain in the bread the carbon dioxide produced as a result of the activity of the yeast. Many cases, however, were investigated where flours possessing a high gluten content were not so strong as a flour with a low content of gluten. Furthermore, no accepted regularity has been found to exist between the strength of flours and the water-holding or gas retaining capacity of their glutens. Attention was next directed to the consideration of the individual proteins in the gluten of flour, namely, gliadine and glutenine. It was found that measurements of the absolute amounts of gliadine showed no correlation with strength. Neither was it possible to show any con- sistent relationship between strength and the ratio of gliadine to glutenine in the gluten. It was suggested by Hall (2) that gliadine might not be a definite substance and that the gliadine contained in very strong flours might be different from that in weak flours. Wood (3), however, prepared and examined samples of gliadine from strong and weak flours and concluded, on the grounds of their content of ami'de nitrogen, that the proteins from both sources were identical. Indirect determinations of the amide nitrogen of the glutenines of weak and strong flours led to the conclusion that the glutenine protein in different flours was one and 232 The Chemistry of the Strength of Wheat Flour the same substance. It was therefore not possible, on the available evidence, to explain the difference in the loaf-making qualities of different flours by reference to their protein content. A valuable contribution to the study of the subject was made, when Wood(3) resolved the conception of flour strength into two factors: 1. The factor of strength which determines the shape of the loaf. "• >> >) >> )j size ,, ,, The results obtained by this investigator justified the conclusion that the capacity of a flour for giving off gas when incubated with yeast and water is the factor which in the first instance determines the size of the loaf. The latter depends not so much on the amount of sugar present in the flour as such, but on the diastatic capacity of the flour, which gives rise to continued sugar formation and consequently con- tinued gas evolution in the dough. The same worker also showed that the properties of gluten in regard to coherence and elasticity were subject to considerable modification by the concentration of acid, alkali or salt in the solution with which it was in contact, and he suggested that these properties have an important bearing on the shape of the loaf. A knowledge of the acidity and soluble salt content of a flour should therefore afford a clue to that factor of strength which decides whether the flour will make a good-shaped loaf. The information obtained in the investigation referred to above has been applied with success in several phases of the milling industry. The view has long been held, however, by Professor Wood himself, that in view of the improvement of the methods employed in protein research, the question of the identity or non-identity of the corresponding gluten proteins in weak and strong flours should be re-investigated. It is now recognised that two proteins may be quantitatively identical with regard to their amino-acid content and yet be two distinct proteins, by virtue of differences in the order of linkage of the amino-acids within the protein molecules. Such a case is furnished by the caseinogens pf cow's and sheep's milk. Though it is possible to show that these proteins are distinct substances (4), yet by the ordinary chemical methods of analysis they are indistinguishable. It is clear, then, that any chemical method which is to be employed to decide on the identity or non-identity of related proteins must be such as to take into account the possibility of differences connected with the order in which the constituents of the proteins are linked up within the molecules. Such a method is the Racemisation Method, which has been used recently in the investigation of the corresponding proteins of H. E. WOODMAN • 233 blood serum, colostrum and milk (5). The method depends on the be- haviour of proteins in dilute alkaline solution. When such solutions are kept at 37° C, they suffer a progressive diminution in the value of their optical rotatory power as a result of a keto-enol tautomerism of the = CH — CO — groups in the protein complex. If the specific rotations of the solution be plotted against the time in hours during which the reaction has been allowed to proceed, then the readings fall on a perfectly smooth curve. It is found that the rotation sinks rapidly at first, then more slowly and subsequently after about 250 hours attains a practically constant value. The process thus results in the partial racemisation of the protein, and the graphs thus obtained are referred to as racemisation curves. Since individual proteins display specific behaviour quantitatively when racemised with dilute soda, it follows that the method may be used to test the identity or non-identity of related proteins. Thus, if two proteins are to be pronounced identical, then if racemised under the same conditions, their solutions must show the same initial rotation, the same final rotation and the same rate of diminution of rotation. They must also continue to display identical optical behaviour if the concentration of the alkali or protein in the solution is varied. On the other hand, if two proteins are not identical, this will be revealed by their possessing distinct sets of racemisation curves. In the investigation to be outlined in the present communication, samples of gliadine and glutenine have been isolated from typical strong and weak flours and have been investigated comparatively by means of the racemisation method. The results obtained are very suggestive in relation to their bearing on the existing ideas of flour strength, since it has been shown that whereas the gliadines from weak and strong flours are identical proteins, yet the glutenines prepared from the same sources appear to be two distinct chemical individuals. PREPARATION OF PROTEINS. 1. Gliadine and glutenine from strong flour. The flour used for this purpose was a typically strong flour milled exclusively from Northern Manitoba Wheat. The method used for the isolation of the proteins was in its essentials the same as that described by Osborne(6). The bulk of the starch and soluble constituents was removed by enclosing the flour in a muslin bag and kneading the material in a stream of running water, the process being completed by thoroughly 234 The Chemistry of the Strength of Wheat Flour kneading the gluten under a large volume of distilled water. The re- sultant characteristically sticky gluten was broken up into small pieces and extracted with alcohol, the alcohol added being such as to give, with the water in the gluten, a solvent containing 70 per cent, of alcohol by volume. After standing for 48 hours with frequent shaking, the super- natant alcoholic solution of gliadine was filtered off and the residue was repeatedly extracted with successive portions of 70 per cent, alcohol until the amount of gliadine going into solution was inappreciable. The combined nitrates were then concentrated in vacuo at 50° C, care being taken to keep the gliadine in solution by adding small portions of alcohol from time to time. The concentrated solution was cooled and poured slowly, with constant stirring, into a large volume of ice- cold distilled water containing about 10 grm. salt per litre. A gummy mass separated out which collected on the glass rod. This was repeatedly washed with distilled water, dissolved in 70 per cent, alcohol and the solution filtered until water clear. After concentrating the solution in vacuo at 50° C, the syrupy residue was cooled and poured into absolute alcohol. It was found that complete separation of the gliadine could only be obtained by this method after stirring a little salt into the alcoholic liquid. The addition of ether also enabled the gliadine to separate completely. The process of dissolving the gliadine preparation in 70 per cent, alcohol, filtering, concentrating in vacuo and precipitating by means of absolute alcohol was carried out in all three times, the final precipitation being effected by a mixture of ether and absolute alcohol, this resulting in the gliadine separating in a flocculent condition. The protein was then dried by washing successively with absolute alcohol and anhydrous ether and was finally obtained as a white powder which dissolved completely in 70 per cent, alcohol to give a water clear solution. As a result of the method of preparation, it contained a little salt as impurity. The gluten residue, after extraction of Ihe gliadine with 70 per cent, alcohol, was allowed to dry at room temperature and then powdered. It was then further extracted with alcohol, the gliadine-free residue being shaken with successive portions of ether to remove fat.
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