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KMID : 1007520020110010055
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Food Science and Biotechnology
2002 Volume.11 No. 1 p.55 ~ p.61
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Amino Acid Substitution of Hypocholesterolemic Peptide Originated from Glycinin Hydrolyzate
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Kwon, Dae Young
Oh, Si Won/Lee, Ji Soo/Yang, Hye Jeong/Lee, Sang Hwa/Lee, Jong Ho/Lee, Yoon Book
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Abstract
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Hypocholesterolemic peptide isolated from glycinin (11 S protein) hydrolyzate by trypsin was identified as tetra-peptide (LPYP). To investigate the effects of polar or non-polar side chains of the peptide on the hypocholesterolemic activity, three peptides were synthesized chemically. Firstly, LPYP was synthesized as a model hypocholesterolemic peptide for comparison, and additional two peptides, LPYPR and SPYPR were synthesized. LPYPR was already reported as a hypocholesterolemic peptide from glycinin hydrolyzates. The SPYPR was chosen based on the genomic data that leucine at Nterminus of LPYPR sometimes substituted by serine. The hypocholesterolemic activities were monitored by assaying bile acid binding capacity or the inhibition of 3-hydroxy3-methylglutaryl CoA reductase (HMG-CoA reductase) in vitro and by the determination of cholesterol content in mice serum. Hypocholesterolemic activity was lost when hydrophobic leucine residue at N-terminus of LPYPR was substituted with polar residues such as serine, and the arginine at C-terminus was not so critical for maintaining hypocholesterolemic activity.
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KEYWORD
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