JP2005206528A - Angiotensin converting enzyme inhibitor and food containing the same - Google Patents

Abstract

<P>PROBLEM TO BE SOLVED: To provide an ACE(angiotensin converting enzyme) inhibitor easily producible, more safely and easily takable and absorbable in high efficiency, and to provide foods imparted or fortified with ACE inhibitory activity through addition of this inhibitor. <P>SOLUTION: The ACE inhibitor comprises as active ingredient(s) amino acid component(s) selected from the group consisting of L-glutamic acid, L-isoleucine, L-lysine, L-threonine, L-cysteine, L-serine, L-histidine, L-arginine, L-tryptophan, L-methionine, and salts thereof and a mixture thereof. <P>COPYRIGHT: (C)2005,JPO&NCIPI

Description

  The present invention relates to an angiotensin converting enzyme (ACE) inhibitor, beverages to which the ACE inhibitor is added, and foods such as foods for specified insurance.

  Conventionally, it is known that peptides having a specific sequence have various physiological activities. For example, Patent Documents 1 to 3 and Non-Patent Documents 1 to 3 describe that some peptides have ACE inhibitory activity. These peptides have strong ACE inhibitory activity, have been shown to have a strong antihypertensive action in spontaneously hypertensive rats (SHR), and to have an antihypertensive effect on hypertensive patients.

However, ACE inhibitory peptides with specific sequences that have been proposed in the past can be obtained mainly by enzymatic degradation or fermentation, but the yield is extremely low, and there is a concern about safety when chemically synthesized. Is done. Accordingly, there is a need for an ACE inhibitor that can be more easily produced, can be safely and easily ingested, and is absorbed at a high rate.
JP-A-4-28239 JP-A-6-40944 JP-A-6-197786 J. Dairy Sci. 1995, 78: 777-783 J. Dairy Sci. 1995, 78: 1253-1257 Am. J. Clin. Nutr. 1996, 64: 767-771

  The object of the present invention is to provide an ACE inhibitor that can be easily produced, can be safely and easily ingested, and is absorbed at a high rate, and the ACE inhibitor is added to impart or enhance ACE inhibitory activity. Is to provide prepared food.

According to the present invention, L-glutamic acid, L-isoleucine, L-lysine, L-threonine, L-cysteine, L-serine, L-histidine, L-arginine, L-tryptophan, L-methionine, and salts thereof And an angiotensin converting enzyme inhibitor characterized by containing an amino acid component selected from the group consisting of a mixture thereof as an active ingredient.
Moreover, according to this invention, the foodstuff characterized by adding the said angiotensin converting enzyme inhibitor is provided.

  Since the ACE inhibitor of the present invention contains the specific amino acid component as an active ingredient, the ACE inhibitor can be easily produced, and can be safely and easily ingested, and is absorbed at a high rate. As useful. Moreover, since the ACE inhibitor of this invention is added, the foodstuff of this invention is useful as various foodstuffs, such as a drink with which ACE inhibitory activity was assign | provided or strengthened, and food for health and health.

The present invention will be described in detail below.
The ACE inhibitors of the present invention are L-glutamic acid, L-isoleucine, L-lysine, L-threonine, L-cysteine, L-serine, L-histidine, L-arginine, L-tryptophan, L-methionine, their An amino acid component which is a salt or a mixture thereof is contained as an active ingredient. In particular, it preferably contains an amino acid component selected from the group consisting of L-cysteine, L-serine, L-histidine, L-arginine, L-tryptophan, L-methionine, and salts thereof, and mixtures thereof. Furthermore, L-cysteine, L-histidine, a salt thereof, or a mixture thereof is preferable because it has particularly strong ACE inhibitory activity.
Although known ACE-inhibiting peptides have higher ACE-inhibiting activity than these amino acids, these amino acids have abundant dietary experience and are considered to have no adverse effects on the living body even if taken in relatively large amounts. Therefore, ACE inhibitory activity can be safely used by ingesting a large amount.

The content ratio of the specific amino acid in the ACE inhibitor of the present invention can be usually 1 to 100% (w / w).
The form of the ACE inhibitor of the present invention is not particularly limited, and examples thereof include powders, tablets, or liquids dissolved in an appropriate solvent, which are the specific amino acids and mixtures thereof. Further, in addition to the specific amino acid as an active ingredient, it may contain other ACE inhibitors, various nutritional components, various additives for food or medicine, etc. within a range not impairing the effects of the present invention. good.

The subject of administration of the ACE inhibitor of the present invention can be animals such as mammals including humans. The administration route is not particularly limited, but can be preferably administered orally.
The dosage of the ACE inhibitor of the present invention can be appropriately determined according to the type of active ingredient, dosage form, etc., when the active ingredient is only the specific amino acid or when it contains other ACE inhibitors. . For example, when it contains only the specific amino acid as an active ingredient by oral administration, the specific amino acid amount can be 10 mg to 10000 mg, preferably 50 mg to 5000 mg.

  The method for preparing the ACE inhibitor of the present invention is not particularly limited, but specifically, for example, the specific amino acid is obtained by microbial fermentation, enzymatic degradation of protein or peptide, chemical synthesis, etc. It can be prepared by blending with other components.

The food product of the present invention may be any food product obtained by adding the above-described ACE inhibitor of the present invention and imparting ACE inhibitory activity to the food product, or a food product having enhanced ACE inhibitory activity. For example, conventionally, the ACE inhibitory activity can be further enhanced by adding the ACE inhibitor of the present invention to a food for specified health use having an ACE inhibitory activity.
In the food of the present invention, the amount of the ACE inhibitor of the present invention can be appropriately selected according to the type of food, desired effects, and the like.
The kind of the food of the present invention is not particularly limited, and examples thereof include various foods such as beverages and dairy products, and various other special health foods.

EXAMPLES Hereinafter, although this invention is demonstrated in detail with reference to an Example, this invention is not limited to these.
Example 1
The ACE inhibitory activity of various amino acids (L form, purchased from Wako Pure Chemical Industries, Ltd.) was measured by the following procedure.

(a) ACE derived from bovine lung (manufactured by Wako Pure Chemical Industries, Ltd.) was dissolved in pH 8.3, 0.1 M borate buffer so as to be 0.1 U to obtain an ACE solution. On the other hand, 20 types of amino acids dissolved in pH 8.3 and 0.1 M borate buffer were prepared at 10 mg / ml (final concentration of 2.7 mg / ml. Each amino acid solution was added to a test tube in 80 μl. 200 μl of hippuryl histidyl leucine (final concentration 5 mM, containing NaCl 300 mM) was added, and 20 μl of the above ACE solution was further added, and the mixture was reacted for 30 minutes at 37 ° C. Thereafter, 250 μl of 1N hydrochloric acid was added to react. After stirring, 1.7 ml of ethyl acetate was added, and after stirring, 1.4 ml of the ethyl acetate layer was collected in a test tube and evaporated to dryness at 120 ° C. for about 60 minutes. Water was added and the absorbance at 228 nm of hyprilic acid extracted into ethyl acetate was measured.

(b) As a control, (b-1) The same as (a) except that the amino acid solution was not added, (b-2) The same as (a) except that the ACE solution was not added Absorbance was measured for the engineered one and (b-3) the same one as in (a) except that the amino acid solution and the ACE solution were not added.

From the absorbance measured in (a) and (b), ACE inhibitory activity was determined as an inhibition rate (%) by the following formula (1). The results are shown in FIG. In the measurement of this example, the value of A below was 0.35.
Inhibition rate (%) = (A−B) × 100 / A (1)
A: (Absorbance at (b-1))-(Absorbance at (b-3))
B: (Absorbance at (a))-(Absorbance at (b-2))

Example 2
As an amino acid solution, pH 8.3, 0.1 μl borate buffer solution containing L-cysteine at a predetermined concentration (100, 50, 25, 10 and 1.0 μg / ml) or L-histidine at a predetermined concentration (10, 5 0.0, 2.5, 1.0, and 0.5 mg / ml) The ACE inhibitory activity was measured in the same manner as in Example 1 except that the dissolved ones were prepared. From these measurement results, the concentration at which the inhibition rate was 50% was determined as the IC50 value. As a result, the IC50 value of L-cysteine was 33 μM, and the IC50 value of L-histidine was 1030 μM.

2 is a graph showing measurement results of ACE inhibitory activity (inhibition rate) of each amino acid in Example 1. FIG.

Claims (4)

  From L-glutamic acid, L-isoleucine, L-lysine, L-threonine, L-cysteine, L-serine, L-histidine, L-arginine, L-tryptophan, L-methionine, and salts thereof, and mixtures thereof An angiotensin converting enzyme inhibitor characterized by containing an amino acid component selected from the group consisting of as an active ingredient.   2. The amino acid component is selected from the group consisting of L-cysteine, L-serine, L-histidine, L-arginine, L-tryptophan, L-methionine, and salts thereof, and mixtures thereof. Angiotensin converting enzyme inhibitor.   The angiotensin converting enzyme inhibitor according to claim 1, wherein the amino acid component is selected from the group consisting of L-cysteine, L-histidine, and salts thereof, and mixtures thereof.   The foodstuff which added the angiotensin converting enzyme inhibitor of any one of Claims 1-3.

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