Increasing of angiotensin converting enzyme inhibitory derived from Indonesian native chicken leg protein using Bacillus cereus protease enzyme
2017
Supadmo | Fitriyanto, N. A. | Jamhari | Yuliatmo, R. | Bachruddin, Z. | Erwanto Y.
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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