Increasing of angiotensin converting enzyme inhibitory derived from Indonesian native chicken leg protein using Bacillus cereus protease enzyme

Supadmo, . and Fitriyanto N. A., . and Jamhari, . and Yuliatmo R., . and Bachruddin Z., . and Erwanto Y., . Increasing of angiotensin converting enzyme inhibitory derived from Indonesian native chicken leg protein using Bacillus cereus protease enzyme. pp. 1799-1804. ISSN 2231-7546

Angiotensin converting enzyme (ACE) converts angiotensin I to angiotensin II thereby increasing hypertension. In order to increase ACE inhibition from bioactive peptides in food products native chicken leg protein was hydrolyzed by proteases extracted from three strains of B. cereus (LS2B TD5B and TD5K). The specific activities of LS2B TD5B and TD5K proteases were 303.57 195.96 and 111.14 U/mg respectively. Dissolved proteins in chicken leg hydrolysates were separated by sodium dodecylsulfate-polyacrylamide gel electrophoresis and subjected to ACE inhibition assay. LS2B strain proteases produced the highest dissolved protein content. The IC50 of chicken leg protein hydrolyzed by pepsin trypsin LS2B strain enzymes and LS2B enzymes pepsin trypsin were 2.58 0.072 1.21 0.78 and 1.092 0.01 mg/mL respectively; chicken leg protein hydrolyzed by LS2B enzymes pepsin trypsin purified by Sep-Pak C18 Cartridge showed an IC50 of 0.33 0.02 mg/mL. The results indicate that enzymatic hydrolysis of chicken leg proteins via bacterial enzymes can increase the ACE inhibitory activity of resultant peptides.

Full text available from: Official URL: http://www.ifrj.upm.edu.my/24%20(04)%202017/(58).p...

Abstract

Angiotensin converting enzyme (ACE) converts angiotensin I to angiotensin II thereby increasing hypertension. In order to increase ACE inhibition from bioactive peptides in food products native chicken leg protein was hydrolyzed by proteases extracted from three strains of B. cereus (LS2B TD5B and TD5K). The specific activities of LS2B TD5B and TD5K proteases were 303.57 195.96 and 111.14 U/mg respectively. Dissolved proteins in chicken leg hydrolysates were separated by sodium dodecylsulfate-polyacrylamide gel electrophoresis and subjected to ACE inhibition assay. LS2B strain proteases produced the highest dissolved protein content. The IC50 of chicken leg protein hydrolyzed by pepsin trypsin LS2B strain enzymes and LS2B enzymes pepsin trypsin were 2.58 0.072 1.21 0.78 and 1.092 0.01 mg/mL respectively; chicken leg protein hydrolyzed by LS2B enzymes pepsin trypsin purified by Sep-Pak C18 Cartridge showed an IC50 of 0.33 0.02 mg/mL. The results indicate that enzymatic hydrolysis of chicken leg proteins via bacterial enzymes can increase the ACE inhibitory activity of resultant peptides.

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Item Type:	Article
AGROVOC Term:	Bacillus cereus
AGROVOC Term:	Proteases
AGROVOC Term:	Angiotensin
AGROVOC Term:	Enzyme inhibitors
AGROVOC Term:	Chickens
AGROVOC Term:	Hypertension
AGROVOC Term:	Peptides
AGROVOC Term:	Protein content
AGROVOC Term:	Infrared spectrophotometry
AGROVOC Term:	Isolation
Depositing User:	Ms. Suzila Mohamad Kasim
Last Modified:	24 Apr 2025 06:28
URI:	http://webagris.upm.edu.my/id/eprint/23814

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