Summary
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1.
The hydrolysis of the proteins of Bengal gram has been followed by subjecting the whole meal to peptic, trypsic and pepticcum tryptic digestions. It is shown that pepsin releases predominantly polypeptides with a complexity of about 7.
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2.
Trypsin records a digestibility of 70 per cent, in the case of total proteins and globulins, and only 44 per cent, in the case of whole meal, whereas pepsin records about 70 per cent, in the case of globulins and total proteins, and about 80 per cent, in the case of whole meal. By the successive action of trypsin and pepsin, the total proteins are digested to the extent of nearly 89 per cent., the same being the case with the whole meal.
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3.
A close study of the tables and graphs reveals that as far as peptic digestion is concerned, there is practically no difference in the digestibilities of total proteins and globulins when present in the seed material or after isolation. In the case of tryptic digestion however, the whole meal records a much lower digestibility.
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References
Basu and MukherjeeInd. Jour. Med. Res., 1936,23, 827.
BhagvatJour. Ind. Inst. Sci., 1936,19 A, 67.
Niyogi, Narayana and DesaiInd. Jour. Med. Res., 1931,19, 475.
Ranganathan and SastriProc. Ind. Acad. Sci., 1938,8, 243.
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The author’s thanks are due to Mr. M. Sreenivasaya,b.a., f.i.i.sc., for many helpful suggestions in the course of the work, and also to the Madras Government for the award of a Research Scholarship to one of us (V. R.).
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Ranganathan, V., Sastri, B.N. Digestibilities of the proteins of bengal gramCicer Arietinum Linn. Proc. Indian Acad. Sci. 8, 367–372 (1938). https://doi.org/10.1007/BF03048224
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DOI: https://doi.org/10.1007/BF03048224