Design of Lignin-Based Biofunctional Materials and Their Applications
| Project/Area Number |
07660219
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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 |
林産学
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| Research Institution | Mie University |
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Principal Investigator |
FUNAOKA Masamitsu Mie Univ., Fac.Bioresources, Assoc.Prof., 生物資源学部, 助教授 (50093141)
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| Project Period (FY) |
1995 – 1996
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| Project Status |
Completed (Fiscal Year 1996)
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| Budget Amount *help |
¥2,000,000 (Direct Cost: ¥2,000,000)
Fiscal Year 1996: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 1995: ¥1,300,000 (Direct Cost: ¥1,300,000)
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| Keywords | Lignin / Lignophenol derivatives / Phase-separation process / Protein / Enzyme immobilization / Bioreactor / Hydrophobic interaction / Biofunctional materials / フェノール化 / フェノール誘導体 / 相分離 / 吸着 / 機能性高分子 |
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| Research Abstract |
Highly phenolic lignin derivatives (lignophenol derivatives) with different phenolic functionalities were synthesized directly from native lignins, through the phase-separation process using phenol derivatives and concentrated acid. The relationships between the structures of lignophenol derivatives and their functions for proteins were discussed.
Lignophenol derivatives had much higher affinities for proteins, compared with conventional lignins : -10 and -100 times higher in lignomonophenols and lignopolyphenols, respectively. The protein affinity was significantly affected by the substitution pattern of phenolic hydroxyl groups and was decreased by the introduction of hydrophobic alkyl substituents. The protein adsorbing capacities of lignophenol derivatives differed with the species from which they were derived. The maximum protein adsorption was achieved at the isoelectric points of used proteins. The lignophenol derivative-protein complex was rapidly and perfectly separated into lignin and protein moieties in aprotic solvents, although it was very stable at any pH in aqueous solution.
The enzymes immobilized on lignophenol derivatives retained high activity : especially an enzyme on lignocresol comparable to a native one. The activity patterns had good correlations between native and immobilized enzymes.
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Report
(3 results)
Research Products
(27 results)
