Separation and Determination of Angiotensin Converting Enzyme Inhibitory Peptide from Salt-Soluble Protein Solution Fermented with Lactic Acid Bacteria

doi:10.7506/spkx1002-6630-201609032

Abstract

Abstract:

Sixteen lactic acid bacteria (LAB) strains were cultured for 3 generations in MRS liquid medium, centrifuged,
prepared into LAB suspension with sterilized physiological saline, and then inoculated in salt-soluble protein (SSP) solution
from arabesque greenling. Through determining angiotensin converting enzyme (ACE) inhibitory peptide from metabolites,
Pediococcus acidilactici ID7 and Lactobacillus plantarum 6214 displayed high ACE inhibitory activity, with a percentage
inhibition of 47.6% and 40.6%, respectively. Higher ACE inhibitory activity in SSP solution fermented with Pediococcus
acidilactici ID7 was determined by high performance liquid chromatograph (HPLC). Meanwhile, two peaks after HPLC
purification were achieved, which showed IC50 of 1.21 μg/mL and 1.07 μg/mL, respectively. The peak with higher ACE
inhibitory activity was purified by gel filtration. The obtained ACE inhibitory peptide showed percentage inhibition of
26.67% and molecular weight less than 586.7 D.

Key words: lactic acid bacteria (LAB), angiotensin converting enzyme (ACE), salt-soluble protein (SSP), high performance liquid chromatography (HPLC)

CLC Number:

Q939.99

ZHAO Junliang, LU Haipeng, MANG Lai, JIN Shan. Separation and Determination of Angiotensin Converting Enzyme Inhibitory Peptide from Salt-Soluble Protein Solution Fermented with Lactic Acid Bacteria[J]. FOOD SCIENCE, doi: 10.7506/spkx1002-6630-201609032.

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Separation and Determination of Angiotensin Converting Enzyme Inhibitory Peptide from Salt-Soluble Protein Solution Fermented with Lactic Acid Bacteria

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