Recycle of woody wastes with useful microorganisms

研究了从健康杉木（Cryptomeria japonica d.d ondon）叶片中分离得到的拟盘多毛孢yk -3的培养特性。这种真菌和有用的黑曲霉一样，在葡萄糖液体培养基中生长良好。它对被测的单、双多糖和多糖具有更广泛的利用能力，并产生了多糖降解酶。在杉木木屑和冻干的杉叶培养基上都能生长，每种培养基都能产生木聚糖酶。与黑曲霉（Aspergillus niger Van Tieghem）相比，该菌株对杉叶提取物具有耐受性或利用能力。拟盘多毛孢也利用木聚糖等不溶性多糖，产生木聚糖水解酶。木聚糖水解酶还能在含有木聚糖和儿茶酚的溶液中催化木聚糖的降解和木糖苷的生成。研究表明，具有木糖基转移活性的木聚糖水解酶可用于多种糖苷的酶法合成。利用POROS 50HA （pertive Biosystems）、POROS 50HS和Sephadex G-100对秋田杉木叶片拟盘多毛孢sp.ST的木聚糖酶进行了连续分离纯化。纯化后的酶25kDa在SDS-PAGE上被证实为均质（图2）。该酶的最适pH为6.0℃，最适温度为50℃。该酶不能水解木糖二糖和木糖三糖。从绿色木霉中纯化出一种新的木聚糖降解酶。经凝胶过滤和SDS-PAGE分析，酶的表观分子质量为73 kDa。该酶在以木聚糖为底物的溶液中几乎不水解木聚糖，但在以木聚糖和儿茶酚为底物的溶液中催化木聚糖降解并生成木糖苷为儿茶酚β-木生物苷。该酶对间苯二酚、邻苯二酚、没食子酸等多种酚类也有转木基活性，但对甲醇等醇类没有活性。

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.