Peptides used as angiotensin converting enzyme inhibitor and...

Details Peptides used as angiotensin converting enzyme inhibitor and... Peptides used as angiotensin converting enzyme inhibitor and...

2000-05-17

2004-07-27

Sitton, Jehanne (Department: 1634)

Chemistry: natural resins or derivatives; peptides or proteins;

Peptides of 3 to 100 amino acid residues

C530S331000

Reexamination Certificate

active

06767990

ABSTRACT:

BACKGROUND OF THE INVENTION
Angiotensin converting enzyme (ACE) mainly presents in human vascular endothelial cells, lungs, kidneys and brains. This enzyme may convert inactive angiotensin I to active angiotensin II by cleaving two amino acids (His-Leu) from the C-terminus end so as to cause contraction of blood vessels and increase blood pressure. Meanwhile, ACE may inactivate the bradykinin that exhibits the function of relief of blood vessels. Thus, ACE may increase blood pressure.
The binding of Angiotensin converting enzyme inhibitor (ACEI) to ACE may reduce the formation of angiotensin II and the inactivation of bradykinin. If ACEI is added to foods, it will cause positive effect on decreasing hypertensive symptom. For the present, it is known that many peptides have the effect on the inhibition of ACE. They have different amino acid sequences and lengths. Those peptides having ACE inhibitory activity can be isolated from foods. Those foods include the hydrolysates of animal or plant proteins, such as casein (Maruyama and Suzuki, 1982), corn protein (Miyoshi et al., 1991), sardine meat (Matsui et al., 1993) and bonito (Matsumura et al., 1993); and fermented foods, such as sake and wine residue (Saito et al., 1994), soy bean oil (Kinoshita et al., 1993), cheese (Okamoto et al., 1995) and fermented milk (Nakamura et al., 1995) etc.
Japanese Laid-Open Patent Publication No. 5-87052 and Japanese Laid-Open Patent Publication No. 2-154693 disclose the substances containing oligopeptides. Food Chemical Monthly, 1990, 6:80 also discloses specific oligopeptides which have the improved effect on lipid metabolism, including the reduction of the concentration of triglyceride in blood. These substances containing oligopeptides described in the above patents or references are the mixtures of protein hydrolysates. However, they do no describe the amino acid sequences of the active ingredients of mixtures. The purity of the above-mentioned substances containing peptides is relatively low and can not be used as pharmaceuticals. Further, when those substances are contained in foods, they are very difficult to be quantitatively detected from other peptides contained in foods. This would cause some problems in quality control.
Japanese Laid-open Patent Publication No. 6-298794 discloses a process for the preparation of ACEI from the proteins of animal and plant sources, such as fish meats, pork and chicken. The process utilizes protein hydrolase, such as thermolysin, pepsin or trypsin, in suitable medium and under proper conditions to decompose the starting materials. The hydrolysate is subject to centrifugation, filtration, concentration and resin absorption to obtain the peptides with ACE inhibitory activity. Japanese Laid-open Publication No. 5-331192 discloses the hydrolysis of katsubishi by therolysin to produce the peptides with ACE inhibitory activity. The sequence of the peptide is H-Tyr-Ser-Trp-Ala-OH (SEQ ID NO:3). Japanese Laid-open Publication No. 4-164098 discloses the preparation of the peptides with ACE inhibitory activity from chicken meat containing no fat. The sequence of the peptide is Gln-Lys-Pro-Lys-Arg (SEQ ID NO:4) U.S. Pat. No. 5,854,029 discloses a process for the preparation of the dipeptide Tyr-Pro exhibiting Ace inhibitory actiivity. In the process, lactobacillus is incubated in the peptide and/or protein medium containing Tyr-Pro to obtain an incubation solution containing a large amount of Tyr-Pro.
Among the above-mentioned prior art techniques, most of them utilize different hydrolase, separation and purification method from animal proteins, such as fish meat, chicken or pork to prepare the peptides with ACE inhibitory activity. However, the cost of the starting materials is more expensive.
SUMMARY OF THE INVENTION
The Applicant found that hydrolysis of the wastes produced from the manufacture of chicken essence and further treatment of the waste mixture with hydrolase may obtain the products having strong ACE inhibitory activity. The process is of low cost and may improve the values of chicken essence by-products.
The main object of the invention is to provide novel peptides having ACE inhibitory activity.
Another object of the invention is to provide a process for the preparation of the products having ACE inhibitory activity. The process comprises the treatment of chicken residues with protein hydrolase to obtain the products having ACE inhibitory activity. The products can be used in health foods.


REFERENCES:
patent: 5314807 (1994-05-01), Yoshikawa et al.
patent: 5854029 (1998-12-01), Yamamoto
patent: 64-83096 (1989-03-01), None
patent: 2-62828 (1990-03-01), None
patent: 2-154693 (1990-06-01), None
patent: 02167052 (1990-06-01), None
patent: 04154798 (1992-05-01), None
patent: 4-264098 (1992-09-01), None
patent: 04279597 (1992-10-01), None
patent: 5-87052 (1993-12-01), None
patent: 5-331192 (1993-12-01), None
patent: 6-49096 (1994-02-01), None
patent: 6-298794 (1994-10-01), None
patent: 8-66165 (1996-03-01), None
patent: 08231588 (1996-09-01), None
patent: WO 90/08162 (1990-07-01), None
patent: WO 91/02002 (1991-02-01), None
Kohmura et al., Agric. Biol. Chem. vol. 53, pp 2107-2114, 1989.*
Masanori Kohmura et al.,Agric. Biol. Chem., 1989, 53(8):2107-2114.
Tao Weng et al.,Sci. Bull. Fac. Agric., 1999, 54(1,2):17-24 (along with partial English translation).
Japanese Office Action along with English translation.
Maruyama and Suzuki,Agric. Biol. Chem, 46(5): 1393-1394, 1982.
Miyoshi et al.,Agric. Biol. Chem., 55(5): 1313-1318, 1991.
Matsui et al.,Biosci. Biotech. Biochem., 57(6): 922-925, 1993.
Matsumura et al.,Biosci. Biotech. Biochem., 57(10): 1743-1744, 1993.
Saito et al.,Biosci. Bioech. Biochem., 58(5): 812-816, 1994.
Kinoshita et al.,Biosci. Bioech. Biochem., 57(7):1107-1110, 1993.
Okamoto et al.,Biosci. Bioech. Biochem., 59(6): 1147-1149, 1995.
Nakamura et al.,J. Dairy Sci., 78: 777-783, 1995.
Kyoichi Kagawa,Food Chemical Monthly, 6(2):80-84, 1990.

Affiliated with

Also associated with

Rating

Peptides used as angiotensin converting enzyme inhibitor and... does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Peptides used as angiotensin converting enzyme inhibitor and..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Peptides used as angiotensin converting enzyme inhibitor and... will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-3247339