| Project/Area Number |
14560224
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Zootechnical science/Grassland science
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| Research Institution | University of Miyazaki |
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Principal Investigator |
MUGURUMA Michio University of Miyazaki, Faculty of Agriculture, Department of Applied Biosciences, Professor, 農学部, 教授 (50091369)
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| Co-Investigator(Kenkyū-buntansha) |
KAWAHARA Satoshi University of Miyazaki, Faculty of Agriculture, Department of Applied Biosciences, Lecturer, 農学部, 講師 (30284821)
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| Project Period (FY) |
2002 – 2004
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| Project Status |
Completed (Fiscal Year 2004)
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| Budget Amount *help |
¥3,600,000 (Direct Cost: ¥3,600,000)
Fiscal Year 2004: ¥600,000 (Direct Cost: ¥600,000)
Fiscal Year 2003: ¥800,000 (Direct Cost: ¥800,000)
Fiscal Year 2002: ¥2,200,000 (Direct Cost: ¥2,200,000)
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| Keywords | Elder Person / Collagen / Melting Point / Transglutaminase / Protein / Peptide / Decrease of Blood Pressure / Meat |
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| Research Abstract |
The purpose of this study is to develop protein polymers to improve the ability of rheological properties and biological activity of food
First of all, the clumping of food by using collagen which has a high melting temperature is necessary for geriatric soft food. Microbial transglutaminase(MTG) is used to polymerize collagen through the ε-(y-glutamyl) lysine bond and to change its melting point. The melting temperature increased by increasing the MTG and collagen concentration. Secondly, cross-linking soybean protein and casein or whey protein isolate by MTG provided biopolymers with improved heat stability and emulsifying property. The addition of biopolymers in manufacture of chicken sausages may permit reduction in phosphate content without loss in texture. In order to clarify one of the biological function of meat, we investigated whether a peptide hydrolasate of denatured porcine crude myosin showed inhibitory activity against angiotensin I-converting enzyme(ACE), which contribut
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ed to hypertension. Our results indicated that this hydrolysate showed relatively strong activity. To search for a noble ACE inhibitory peptide, porcine skeletal myosin B was hydrolyzed with pepsin. This hydrolysate also showed ACE inhibitory activity. Analysis using a protein sequencer identified these peptides as 6mer from myosin heavy chain, 8mer from myosin light chain, 9mer from troponin C or 7mer from troponin T. A novel ACE inhibitory peptide (RMLGQTPTK;9mer) from porcine skeletal troponin C was investigated for its inhibitory profile. This peptide was noncompetitive and as hydrophobic as the known ACE inhibitory peptides. Most products derived from 9mer hydrolysis by ACE, aminopeptidase, or carboxypeptidase showed weak but definite ACE inhibitory activities. Thus, 9mer was estimated to be a wholly efficient inhibitor with those fragment peptides.
The results obtained in the present study indicate that biologically active protein polymers can be prepared from meat through chemical modifications, addition of functional peptides and the use of MTG modified collagen. Less
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