Functional Properties of Peptides Produced by Bacterial Enzymes from Traditional Fermented Foods
| Project/Area Number |
18300250
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Eating habits, studies on eating habits
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| Research Institution | Gifu University |
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Principal Investigator |
NAGANO Hiroko Gifu University, Faculty of Education, Professor (40074984)
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| Co-Investigator(Kenkyū-buntansha) |
KASUYA Shiro Gifu University, Faculty of Regional Studies, Professor (20021438)
SUZUKI Tohru Gifu University, The United Graduate School of Agricultural Science, Professor (20235972)
SHIMOYAMADA Makoto Miyagi University, School of Food Agricultural and Environmental Sciences, Associate Professor (60235695)
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| Project Period (FY) |
2006 – 2007
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| Project Status |
Completed (Fiscal Year 2007)
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| Budget Amount *help |
¥16,280,000 (Direct Cost: ¥14,900,000、Indirect Cost: ¥1,380,000)
Fiscal Year 2007: ¥5,980,000 (Direct Cost: ¥4,600,000、Indirect Cost: ¥1,380,000)
Fiscal Year 2006: ¥10,300,000 (Direct Cost: ¥10,300,000)
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| Keywords | fermented food / microorganism / enzyme / protein / peptide / functionary |
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| Research Abstract |
For many thousands of years, people have prepared foods by traditional and natural fermentation. Naturally occurring microorganisms such as bacteria, yeast and moulds produce the proteolytic enzymes for making foods. A variety of Bacillus sp. have been involved in traditional fermented cereal and legume foods. This study aimed to collect microorganisms from fermented foods and characterize proteolytic potentials and functional properties of bacterial enzymes. Memorandum of Understanding (MOU) of collaboratory based on the Convention on Biological Diversity was decided with Thailand, Vietnam, China and Cambodia, the data from this research could therefore be publicly distributed. The isolated bacteria were identified by 16S rDNA and phylogenetic-tree analysis was also performed. The molecular mass and N-terminal amino acid sequence of purified enzyme were 33 kDa and AQSVPYGISQIKAPA, respectively. However, this was the first report in which it was isolated from traditional fermented wheat flour food. The purified protease digested acid casein into fragments with hydrophilic and hydrophobic amino acids at C-terminal, in particular Arg, Glu, Val and Ile.
The concentrated crude enzyme of B. subtilis DB and SR could reduce allergenicity of gliadin (wheat allergen) by hydrolyzing the allergenic gliadin fragments detected by immunoblotting. Furthermore, the concentrated crude enzyme of B. subtilis DB could also digest β-lactoglobulin (milk allergen) into small fragments within 1 h and these fragments were disappeared after 3-h incubation. The fragments were then analyzed for N-terminal amino acid sequence ; it was found that this enzyme could hydrolyze the major allergenic epitope of β-lactoglobulin at Gln^<35>-Ser^<36> position. Therefore these enzymes can be applied for the production of hypoallergenic wheat flour or milk food products.
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Report
(3 results)
Research Products
(29 results)
