Casein hydrolyzate, process for producing the same and use thereof
a technology of casein hydrolyzate and hydrolyzate, which is applied in the field of casein hydrolyzate, can solve problems such as not known in detail, and achieve the effects of easy and efficient production, excellent in vivo absorbability and various functions
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example 1
Analysis Example 1
Identification of Enzymes
[0088] Among the extracellular enzymes derived from Aspergillus oryzae used in Example 1, enzymes necessary for obtaining the casein hydrolysate of the present invention were analyzed in the following method. Incidentally, all the following operations were performed at 4° C. unless otherwise specified. The reagents used were all guaranteed reagents manufactured by WAKO PURE CHEMICAL INDUSTRIES, LTD. unless otherwise specified.
Impact of Various Inhibitory Agents on Enzymes
[0089] 2000 mg of SUMIZYME FP (registered trademark, manufactured by SHIN NIHON CHEMICAL CO., LTD.) was dissolved in 10 ml of a 50 mM phosphate buffer at pH 7.2, and the insoluble was removed through a cellulose acetate membrane (DISMIC-25cs, pore diameter 0.45 μm, manufactured by ADVANTEC), to obtain a crude enzyme solution.
[0090] This crude enzyme solution was reacted with 1% casein in the same way as in Example 1. When a metalloprotease inhibitor, EDTA (ethylenediami...
example 2
Confirmation of ACE Inhibitory Activity of Casein Hydrolysate by Purified Enzyme Combination
[0108] From Analysis Example 1, it was confirmed that the activity to generate ACE inhibitory components of the fractions adsorbed on the anion exchange resin of the extracellular enzyme derived from Aspergillus oryzae (SUMIZYME FP (registered trademark, manufactured by SHIN NIHON CHEMICAL CO., LTD.)) included four enzymatic activities, i.e., the proteinase activities including those of at least neutral proteases I and II, the aminopeptidase activity including that of leucine aminopeptidase, and the activity to cleave the carboxyl terminal at immediately after proline.
[0109] From the adsorbed fractions (see FIG. 3), Fraction I having high proteinase activity (fractions 1 to 35 in FIG. 3), Fraction II having high activity to cleave the carboxyl terminal at immediately after proline (fractions 36 to 55 in FIG. 3), Fraction III thereafter (fractions 56 to 100 in FIG. 3), and non-adsorbed fract...
example 3
[0113] 15 g of casein derived from cow's milk (manufactured by NIPPON NZMP) was added to 85 g of distilled water at about 80° C. and thoroughly mixed. 1N sodium hydroxide solution was added to the mixture to adjust the pH to 7.0. The temperature was adjusted to 20° C. to prepare a substrate solution.
[0114] To the substrate solution thus obtained, SUMIZYME FP (registered trademark, manufactured by SHIN NIHON CHEMICAL CO., LTD.), which is extracellular enzymes derived from Aspergillus oryzae, was added as the group of enzymes so that the enzyme / casein ratio was 1 / 25 by weight. The mixture was reacted at 50° C. for 20 hours, while the reaction liquid was sampled at intervals to evaluate the ACE inhibitory activity and the average chain length against time in the same way as in Example 1. The results are shown in FIGS. 4 and 5. The enzyme-digested solution taken after 12 hours of reaction, which exhibited the maximum ACE inhibitory activity, was spray-dried to obtain powders of peptide...
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