1994 Fiscal Year Final Research Report Summary
Enzymatic Glycosylation and Phosphatidylation in Organic Solvent Systems.
| Project/Area Number |
05660095
|
|---|
| Research Category |
Grant-in-Aid for General Scientific Research (C)
|
| Allocation Type | Single-year Grants |
|---|
| Research Field |
応用微生物学・応用生物化学
|
|---|
| Research Institution | Research Institute for Bioresources, Okayama University |
|---|
Principal Investigator |
SUZUKI Yukio Okayama University Research Institute for Bioresources, Professor, 資源生物科学研究所, 教授 (80033108)
|
|---|
| Co-Investigator(Kenkyū-buntansha) |
SUGIMOTO Manabu Okayama University Research Institute for Bioresources, Research Associate, 資源生物科学研究所, 助手 (20216336)
|
|---|
| Project Period (FY) |
1993 – 1994
|
| Keywords | Enzymatic synthesis in organic solvents / Enzymatic glycosylation / Enzymatic phosphatidylation / Transphosphatidylation reaction / Phosphatidylation of water-soluble vitamins / Enzymatic glycosylation of terpenoids / Enzymatic glucosylation of phenolic compounds |
|---|
| Research Abstract |
1.Enzymatic glycosylation of fat-solubly physiologically active compounds in a hydrophilic organic solvent.
New derivatives of long acyclic terpene alcohols, O-beta-glucosylfarnesol, O-beta-galactosylfarnesol and O-beta-galactosylgeranylgeraniol, were found to be formed, when the mixture containing these terpene alcohols and cellobiose (or lactose) in 50 % acetonitrile was incubated with almond beta-glucosidase (or Aspergillus oryzae beta-galactosidase). These glycosylated derivatives were isolated and identified.
Glucosylation of phenolic compounds-A high transglucosylation reaction to hydroxy residue of aromatic compounds.
The synthesis of pheny1-alpha-glucoside and 0-alpha-glucosylcatechol via transglucosylation reaction by Bacillus stearothermophilus cyclomaltodextrin glucanotransferase was found. These glucosides were isolated in crystalline form and identified. These glucosides were much more stable than the aglycones in a peroxidase-hydrogen peroxide-oxidizing system.
3.Enzymatic phosphatidylation of water-soluble vitamins in organic solvents.
Streptomyces sp. phospholipase D was found to be catalyze the transfer reaction of the dipalmitoylphosphatidyl residue from 1,2-dipalmitoy1-3-sn-phosphatidy1-choline (DPPC) to water-soluble vitamins (thiamin, pantothenic acid, and these related compounds) in a biphasic system, to afford novel fat-soluble derivatives of the vitamins (DPP-thiamin, DPP-pantothenic acid, DPP-thiamin-propyldisulfide, DPP-fursulthiamin, and DPP-pantothenyl ethyl ether), respectively. These novel derivatives were isolated and identified.
|
Research Products
(8 results)
