Talaromyces emersonii, a thermophilic aerobic fungus, produces a complete xylan-degrading enzyme system when grown on appropriate substrates. In this paper we present the physicochemical and catalytic properties of three enzymes, xylosidase (Xyl) I (M(r) 181,000; pI 8.9), II (M(r) 131,000; pI 5.3) and III (M(r) 54,200; pI 4.2). Xyl I and II appear to be dimeric and Xyl III is a single-subunit protein. All three enzymes catalyse the hydrolysis of aryl beta-D-xylosides and xylo-oligosaccharides. Xyl I is a classic beta-xylosidase (1,4-beta-D-xylan xylohydrolase; EC 3.2.1.37), and Xyl II and III are novel xylanases (endo-1,4-beta-D-xylan xylanohydrolase; EC 3.2.1.8) which we believe have not hitherto been reported. In addition to the above substrates, they also catalyse the extensive hydrolysis of unsubstituted xylans, and may have considerable biotechnological potential. The hydrolysis product profiles and bond-cleavage frequencies with various substrates are presented.

译文

嗜热好氧真菌Talaromyces emersonii在适当的底物上生长时会产生完整的木聚糖降解酶系统。本文介绍了木糖苷酶 (Xyl) I (M(r) 181,000; pI 8.9),II (M(r) 131,000; pI 5.3) 和III (M(r) 54,200; pI 4.2) 三种酶的理化和催化性质。Xyl I和II似乎是二聚体,Xyl III是单亚基蛋白。所有三种酶都催化芳基 β-D-木糖苷和低聚木糖的水解。Xyl I是经典的 β-木糖苷酶 (1,4-β-d-木聚糖木糖水解酶; EC 3.2.1.37),而Xyl II和III是新的木聚糖酶 (endo-1,4-β-d-木聚糖木聚糖水解酶; EC 3.2.1.8),我们认为迄今为止尚未报道。除了上述底物外,它们还催化未取代的木聚糖的广泛水解,并且可能具有相当大的生物技术潜力。介绍了各种底物的水解产物曲线和键裂解频率。

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