Degradation product of total protein

Details Degradation product of total protein Degradation product of total protein

1988-12-14

1991-09-17

Penland, R. B.

Food or edible material: processes, compositions, and products

Fermentation processes

426533, 426623, 426626, 426630, 426650, 426656, 426657, 426807, 2041826, A23K 100

Patent

active

050493973

DESCRIPTION:

BRIEF SUMMARY
The invention relates to a degradation product of total protein that is free of mineral salt, the process for its production and its use as a meat flavor precursor and protein source, especially in animal feed.
The significance of protein matter and its elements, the amino acids, for nutrition and medicine is generally known. But much of natural protein matter is not utilizable since it cannot be digested and is thus unsuited for nutritional purposes. Thus an economical conversion of protein matter of any kind into its amino acid and oligopeptide components is of the greatest interest.
It is known how to convert protein matter hydrolytically or enzymatically into digestible degradation products. Thus, for example keratin proteins, such as chicken feathers, horn or bristles as well as all the protein compounds of entire animal cadavers, by the effect of water or steam at high pressures and temperatures can for the most part be degraded into digestible peptides. Even "toasting" (=treating with superheated steam) of soybean proteins serves to make indigestible constitutents of the soybean protein usable for animal feed.
The drawback here is that degradation occurs nonspecifically and certain thermolabile, essential amino acids such as methionine and cystine are destroyed. While, for example, untreated chicken feathers have a cystine content of 6-7%, "toasted" chicken meal contains only about 1% cystine.
Although the enzymatic method of protein degradation leads, under special conditions, partially up to the amino acids, it is limited to soluble protein matter, such as casein, gelatin, or the like, that are at least largely soluble at the necessarily neutral pH values. Insoluble proteins such as keratin cannot be converted in this way directly into utilizable protein degradation products.
Finally, it is known to hyrolyze any kind of protein by mineral acids and to neutralize the hydrolyzate subsequently by neutralization means, such as sodium hydroxide solution, soda, and the like. Previously such products have been used, for example, as food seasonings, or individual amino acids were isolated from them by methods known in the art such as crystallization or specific precipitation. Amino acids such as glutamic acid, tyrosine, arginine, leucine and cystine are produced in this way.
The drawback in this process is on the one hand the formation of humin, which leads to dark, colloidal solutions that require not only very large amounts of expensive activated carbon for bleaching but that are also responsible for losses in the yield of the amino acids to be isolated.
Another, at least as great a drawback of such hydrolyzates is the high content of inorganic salts that unavoidably precipitate during neutralization. Except for the production of food spices, in which about a 25% common salt content is desired, the salt content requires another purification operation and prohibits further use of hydrolyzate, which itself is of biologically very high quality.
A possibility of reaching a salt-free protein hydrolyzate consists in neutralizing the solution precipitating after the acid hydrolysis by ion exchange chromatography. But this process has the serious drawback that, during the neutralization process, amino acids such as mainly cystine and tyrosine already precipitate and can be fed again to the total hydrolyzate only by complicated, additional process steps. Also, less slightly soluble amino acids remain absorbed on the ion exchange resin and can be isolated again only by economically uninteresting amounts of solvent.
The process of electrolytic neutralization has previously been used only in isolating individual amino acids. Thus DT-PS 1 518 068 describes the production of individual, free amino acids from their acid addition salts by electrolysis using a diaphragm.
But for various reasons it was not to be expected that electrolytic neutralization could be used on a strongly mineral acidic, complex mixture of different amino acids and oligopeptides. Because of the excess mineral acid, here the electrolysis must act

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G. Zaghini et al., "Addition of Amino Acids and Oligopeptides to Piglet Diets, I. Effects on Growth Performance and on the Development of Intestinal Flora", Chem. Ab., Band 92, Nr. 23 (Jun. 1980).
J. Solms et al., "Taste of Amino Acids, Peptides, and Proteins", Chem. Ab., Band 72, Nr. 19, 11 (May 1970).
L. E. Tsupak et al., "Casein Hydrolyzate", Chem. Abs. Band 93, Nr. 13 (sep. 1980).

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