Rath J, Messner R, Kosma P, Altmann F, März L, Kubicek C P
Zentrallabor für Molekularbiologie, Institut für Zoologie, Universität Wien, Althanstrasse 14, A-1090 Wien, Austria.
Arch Microbiol. 1995 Dec;164(6):414-9.
A heteroglycan responsible for the binding of the enzyme beta-1,4-D-glucosidase (EC 3.2.1.21) to fungal cell walls was isolated from cell walls of the filamentous fungus Trichoderma reesei. The heteroglycan, composed of mannose, galactose, glucose, and glucuronic acid, also activated beta-1,4-D-glucosidase, beta-1,4-D-xylosidase and N-acetyl-beta-1,4-D-glucosaminidase activity in vitro. The structural backbone of this heteroglycan was prepared by acid hydrolysis and gel filtration. The molecular structure of the core of the heteroglycan was determined by NMR studies as a linear alpha-1,6-D-mannan. The mannan core obtained by acid degradation stimulated the beta-glucosidase activity by 90%. Several glycosidases from Aspergillus niger were also activated by the T. reesei heteroglycan. The beta-glucosidase of Trichoderma was activated by mannan from Saccharomyces cerevisiae to a comparable extent.
从丝状真菌里氏木霉的细胞壁中分离出一种杂聚糖，它负责将β-1,4-D-葡萄糖苷酶（EC 3.2.1.21）结合到真菌细胞壁上。这种由甘露糖、半乳糖、葡萄糖和葡萄糖醛酸组成的杂聚糖，在体外也能激活β-1,4-D-葡萄糖苷酶、β-1,4-D-木糖苷酶和N-乙酰-β-1,4-D-葡萄糖苷酶的活性。该杂聚糖的结构主链通过酸水解和凝胶过滤制备。通过核磁共振研究确定，该杂聚糖核心的分子结构为线性α-1,6-D-甘露聚糖。经酸降解得到的甘露聚糖核心使β-葡萄糖苷酶活性提高了90%。黑曲霉的几种糖苷酶也被里氏木霉杂聚糖激活。里氏木霉的β-葡萄糖苷酶被酿酒酵母的甘露聚糖激活到类似程度。
