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  • 1970-1974  (6)
  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 21 (1973), S. 860-863 
    ISSN: 1520-5118
    Source: ACS Legacy Archives
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 19 (1971), S. 1151-1154 
    ISSN: 1520-5118
    Source: ACS Legacy Archives
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 21 (1973), S. 676-680 
    ISSN: 1520-5118
    Source: ACS Legacy Archives
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
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  • 4
    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
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  • 5
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Chemical and organoleptic tests showed that partial digestion of soybean curd and defatted soybean flour by aspergillopeptidase A preparation removed flavor compounds and related fatty materials from these soybean products. Amounts of ether-soluble compounds, total carbonyl compounds and volatile reducing substances released during incubation of soybean curd with the enzyme were higher than those released during incubation without the enzyme. Amounts of volatile flavor compounds, including n-hexanal and n-hexanol, released during the incubation of defatted soybean flour with the enzyme were also higher than those released during incubation without the enzyme. Related compounds, i.e., lipids, pigments, saponins, etc., also were released during the enzymation. The enzymic digestion product from either soybean curd or defatted soybean flour had less odor, taste and color. Stability of the enzymic digestion product from the defatted soybean flour against autoxidation during the preservation, measured by TBA-reaction and organoleptic test, was superior to that of the product treated similarly without the enzyme.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Isolation and characterization of 7 sorts of diffusable bitter peptides in peptic hydrolyzate of soybean protein were presented. One liter of dilute HCI solution containing 25 g of soybean cold-insoluble protein and 250 mg of pepsin was incubated at 37°C for 24 hr. The resulting peptic hydrolyzate was dialyzed against water and the diffusable fraction was, after being concentrated at 40°C, investigated by gel permeation chromatography using Sephadex G-10, ionexchange chromatography of Dowex 50 (w)-X2 (pyridinium) and thin-layer chromatography with silica gel G. Bitterness of the diffusable fraction was attributable to free amino acids having bitter flavor, such as isoleucine, leucine, phenylalanine and valine; also to peptides such as H. Gly-Leu. OH, H. Leu-Phe. OH, H. Ser-Lys-Gly-Leu . OH, H-Leu-Lys . OH, H. Phe-(lle, Leu2)- Gin-Gly-Val . OH, H. Arg-Leu-Leu . OH and H. Arg-Leu . OH. It was characteristic that almost all diffusable bitter peptides investigated here had leucine at the termini. Through carboxypeptidase A treatment on these peptides, the bitterness decreased considerably. Furthermore, applying carboxypeptidase A or Nagane, a bacterial neutral proteinase, to the diffusable fraction of the peptic hydrolyzate was also effective in removing the bitterness somewhat.
    Type of Medium: Electronic Resource
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