ISSN:
1750-3841
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
SUMMARY— A proteolyzate obtained by treating an isolated soybean protein preparation with Molsin, a crude preparation of aspergillopeptidase A (APase A), was less bitter and contained larger amounts of free amino acids, especially hydrophobic amino acids. A proteolyzate obtained by treating this protein preparation with crystallized APase A was much more bitter and contained smailer amounts of free amino acids, mainly consisting of hydrophilic amino acids. The latter was richer in peptides than the former, bearing hydrophobic amino acid residues near the C-termini. Difference in N-terminal amino acid composition apparently has not been found between the 2 proteolyzates. These results indicate that Molsin per se contains a certain carboxypeptidase which decomposes the C-terminal structures and, consequently, lessens the bitterness (debittering effect). This carboxypeptidase was found to be identical with aspergillus acid carboxypeptidase (AACPase). Abase A, as well as MO/sin, was effective in removing odor ants, i.e., n-hexanal, n-hexanol and n-heptanol, from the isolated soybean protein preparation Ideodorization effect). AACPase seemed to have no deodorization effect. A method was suggested to prepare a deodorized and debittered proteolyzate by a combination use of APase A and AACPase.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1365-2621.1970.tb00940.x
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