Isolation and Identification of Hypocholesterolemic Peptide Derived from Black Soybean Protein

doi:10.7506/spkx1002-6630-201319028

Abstract

Abstract:

Black soybean peptides (BSPs) with strong hypocholesterolemic activity were purified from black soybean
protein hydrolysates by using ultrafiltration (UF) and macroporous adsorption resin (MAR), and further purified using
Sephadex G-25 column, reversed phase high-performance liquid chromatography (RP-HPLC) and size exclusion
chromatography (SEC). The amino acid sequence of the peptide with the strongest hypocholesterolemic activity was
confirmed as Ala-Phe-Pro-Lys-Asp by automated Edman degradation in a protein sequencer, and its relative molecular mass
was determined to be 576 D. In addition, a specific hydrophobic domain in the sequence was observed, and Pro was located
in an important region except the N-terminus.

Key words: black soybean peptides, hypocholesterolemic activity, isolation, structural analysis

CLC Number:

TS201.2.1

LIU En-qi1,2，LI Hua1,*，WU Yong-hua 2，GAO Zhao-jian2，ZHANG Jian-ping2. Isolation and Identification of Hypocholesterolemic Peptide Derived from Black Soybean Protein[J]. FOOD SCIENCE, doi: 10.7506/spkx1002-6630-201319028.

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Isolation and Identification of Hypocholesterolemic Peptide Derived from Black Soybean Protein

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