Process for the preparation of angiotensis converting enzyme (ACE) inhibitors and its use

a technology angiotensis, which is applied in the field of process for the preparation of angiotensis converting enzyme (ace) inhibitors, can solve the problems of limiting factors, extensive and expensive protocols, and high potency of synthetic ace inhibitors, and achieves potent ace inhibitory activity

Inactive Publication Date: 2004-09-30
COUNCIL OF SCI & IND RES
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Benefits of technology

0019] The main object of the present invention is to provide a process for the preparation of an enzymatic hydrolysate of a selected soybean storage protein fraction that evidences potent ACE inhibitory activity.

Problems solved by technology

Synthetic ACE inhibitors are very potent and have adverse effects that are generally not considered safe.
However none relate to the use of glycinin as the source of antihypertensive peptides.
Although most peptides that exhibit ACE inhibitory activity are those that are isolated and characterized, it is the extensive and expensive protocols that are limiting factors.

Method used

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  • Process for the preparation of angiotensis converting enzyme (ACE) inhibitors and its use
  • Process for the preparation of angiotensis converting enzyme (ACE) inhibitors and its use

Examples

Experimental program
Comparison scheme
Effect test

example 2

[0058] 500 mg of isolated glycinin was dissolved in 2 mL of Tris-HCl buffer, pH 8.2 and incubated at 37.degree. C. for 10 mins. 10 mg of bovine trypsin (1600 units / mg protein) was added and incubated for 4 h at 37.degree. C. This was followed by the addition of a second aliquot of 10 mg bovine trypsin and further incubated 12 h at 37.degree. C. The reaction was stopped by adding 100% TCA (w / w) to a final concentration of 5%. Centrifuged supernatant is used as peptide source for ACE inhibitory peptides. The IC.sub.50 value for inhibition of porcine kidney ACE was 18.37 .mu.g N.sub.2 equivalence.

example 3

[0059] 500 mg of isolated glycinin was dissolved in 2 mL of Tris-HCl buffer, pH 8.2 and incubated at 37.degree. C. for 10 mins. 10 mg of bovine chymotrypsin (2,168 units / mg protein) was added and incubated for 4 h at 37.degree. C. This was followed by the addition of a second aliquot of 10 mg bovine chymotrypsin and further incubated 12 h at 37.degree. C. The reaction was stopped by adding 100% TCA (w / w) to a final concentration of 5%. Centrifuged supernatant is used as peptide source for ACE inhibitory peptides. The IC.sub.50 value for inhibition of porcine lung ACE was 29.0 .mu.g N.sub.2 equivalence.

example 4

[0060] 500 mg of isolated glycinin was dissolved in 2 mL of sodium phosphate buffer, pH 6.0 and incubated at 50.degree. C. for 10 mins. 220 units of ginger protease was added and incubated for 4 h at 50.degree. C. This was followed by the addition of a second aliquot of 100 units of ginger protease and further incubated 12 h at 50.degree. C. The reaction was stopped by adding TCA to a final concentration of 5%. Centrifuged supernatant is used as peptide source for ACE inhibitory peptides. The IC.sub.50 value for inhibition of porcine kidney ACE was 33.57 .mu.g N.sub.2.

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Abstract

A process for preparing Angiotensin Converting Enzyme (ACE) inhibitors from glycinin of soy flour and its use as ACE inhibitors.

Description

[0001] The present invention relates to a process for the preparation of an enzymatic hydrolysate of a selected soybean storage protein fraction, glycinin that evidences potent Angiotensin Converting Enzyme (ACE) inhibitory activity. The present invention also relates to a use of polypeptides of glycinin as ACE inhibitors.[0002] In recent years, peptides from partial enzymatic hydrolysates of food proteins produced in vivo or in vitro have received greater attention from food scientists than ever before. Many biological peptides with health benefits such as opioid activity, antihypertensive activity, antibacterial activity, mineral-binding activity, anti-thrombotic activity, anti-gastric activity, enhancement of intestinal activity, etc have been identified from food protein hydrolysates. These peptides are hidden in a latent state within the sequence of the parent protein may be released by proteolytic processes during in vivo / in vitro digestion or during food processing. Biologica...

Claims

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Application Information

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Patent Type & Authority Applications(United States)
IPC IPC(8): A23J3/34A61K38/55C07K14/415C12P21/06
CPCA23J3/346A61K38/556C12Y304/15001C12P21/06C07K14/415
Inventor GOWDA, LALITHA RAMAKRISHNARAO APPU RAO, APPU RAO GOPALPRAKASH, VISHWESHWARIAH
Owner COUNCIL OF SCI & IND RES
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