Studies on Biologically Active Peptides Produced by Phytoplankton
| Project/Area Number |
01480081
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| Research Category |
Grant-in-Aid for General Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Fisheries chemistry
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| Research Institution | The University of Tokyo |
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Principal Investigator |
YAMAGUCHI Katsumi Univ. Tokyo Fac. Agric. Professor, 農学部, 教授 (50011896)
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| Co-Investigator(Kenkyū-buntansha) |
MURAKAMI Masahiro Univ. Tokyo Fac. Agric. Associate Professor, 農学部, 助教授 (70134517)
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| Project Period (FY) |
1989 – 1990
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| Project Status |
Completed (Fiscal Year 1990)
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| Budget Amount *help |
¥6,800,000 (Direct Cost: ¥6,800,000)
Fiscal Year 1990: ¥2,000,000 (Direct Cost: ¥2,000,000)
Fiscal Year 1989: ¥4,800,000 (Direct Cost: ¥4,800,000)
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| Keywords | Phytoplankton / Cyanophyte / Chlorophyte / Angiotensin-converting enzyme / Protease / Enzyme inhibition / Peptide |
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| Research Abstract |
1. Screening of biologically active peptides
Algal samples of twenty four species and strains were collected and cultured. They were searched for angiotensin-converting enzyme, papain, elastase, trypsin and chymotrypsin inhibitory activities in their water-soluble and fat-soluble fractions. Water-soluble fractions of eleven species and fat-soluble fractions of eight species showed angiotensin-converting enzyme inhibitory activities. Water-soluble fractions of fourteen species and fat-soluble fractions of twenty three species inhibited papain activities. Water-soluble fraction of a species and fat-soluble fractions of two species inhibited elastase activities. Water-soluble fractions of five species and fat-soluble fractions of eleven species inhibited trypsin activities. Water-soluble fractions of five species and fat-soluble fractions of eight species inhibited chymotrypsin activities.
2. Isolation and structural elucidation of angiotensin-converting enzyme inhibitory peptides
Angiotensin-converting enzyme inhibitors were isolated from water-soluble fractions of chlorophytes Dunaliella bardawil and Botryococcus braunii. These inhibitors were suggested to be peptides from the results of the hydrolysates amino acid analyses. They inhibited angiotensin-converting enzyme at 50 mug/ml.
An angiotensin-converting enzyme inhibitor was isolated from the cyanophyte Microcystis aeruginosa by ion exchange and reverse phase chromatography. Its structure was determined as 1 by using amino acid analysis, FABMS and 2D NMR spectrum. The inhibitor includes a novel amino acid, 2-amino-3-hydroxy-8-methylnonanoic acid. It inhibited angiotensin-converting enzyme at 7 mug/ml.
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Report
(3 results)
Research Products
(7 results)
