2004 Fiscal Year Final Research Report Summary
Recycle of woody wastes with useful microorganisms
| Project/Area Number |
14360197
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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 |
生物資源科学
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| Research Institution | Chiba University |
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Principal Investigator |
SHINOYAMA Hirofumi Chiba University, Graduate School of Science and Technology, Associate Prof., 大学院・自然科学研究科, 助教授 (40211958)
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| Co-Investigator(Kenkyū-buntansha) |
TSUKAGOSHI Satoru Chiba University, Center for Environmenta, Health and Field Sciences, Research Associate, 助手 (40270863)
MIYAMOTO Hirokuni Japan Eco-science Co., LTD., Company Executive, 代表取締役
SAKAMOTO Kaunori Chiba University, Faculty of Horticulture, Associate Prof., 園芸学部, 助教授 (10225807)
ISHIKAWA Keiko Japan Horticultural Production and Research Institute, Research Manager, 主任研究員 (20212839)
ITO Kenji KANAGAWA Furniture Co., LTD., Company Executive, 代表取締役
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| Project Period (FY) |
2002 – 2004
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| Keywords | sugi leaf surface / PCR-DGGE / sugi resources / analysis of microbial population on leaf surface / xylanase / lacccase / Strobilurus ohshimae / Pestalotiopsis spp. |
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| Research Abstract |
The cultural properties of Pestalotiopsis sp.YK-3 isolated from healthy sugi (Cryptomeria japonica D.Don) leaves were investigated. The fungus grew well as the useful fungus, Aspergillus niger Van Tieghem, in the glucose liqiud medium. It exhibited wider ranges of utilizing abilities for mono-, di-and polysaccharides tested and produced glycan-degrading enzymes. It was grown even on the sugi sawdust or the freeze-dryed sugi leaf medium, and xylanases were produced in each sugi medium. It was also suggested that it had tolerances or utilizing abilities for extractives of sugi leaves when compared with Aspergillus niger Van Tieghem. Pestalotiopsis spp. also utilized insoluble polysaccharides such as xylan, and produced xylan-hydrolyzing enzymes. The xylan-hydrolyzing enzymes also catalyzed degradation of xylan and production of xylosides in solution containing xylan and catechol. It has suggested that xylan-hydrolyzing enzymes with the xylosyl transfer activity has been applied for enzymatic synthesis of various glycosides. A xylanase of Pestalotiopsis sp.ST, a strain isolated from Akita-sugi leaf, was purified successive fractionation on POROS 50HA (Perseptive Biosystems), POROS 50HS and Sephadex G-100. The purified enzyme, 25kDa, was confirmed to be electophretically homogenious on SDS-PAGE (Fig.2). The optimum pH and temperature for this enzyme were 6.0 and 50℃, respectively. This enzyme could not hydrolyze xylobiose and xylotriose.
A novel xylan-degrading enzyme was purified from Trichoderma viride. The purified enzyme had the apparent molecular mass of 73 kDa by gel filtration and SDS-PAGE. The enzyme hardly hydrolyzed xylan in solution containing xylan as a substrate, but catalyzed degradation of xylan and production of xylosides as catechol β-xylobioside in solution containing xylan and catechol. The enzyme had also transxylosyl activity for various phenols as resorcinol, pylogallol, gallic acid, but not for alcohols as methanol.
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