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Sequencing and Expression of Additional Xylanase Genes from the Hyperthermophile Thermotoga maritima FjSS3B.1

机译:嗜热嗜热菌FjSS3B.1的其他木聚糖酶基因的测序和表达

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摘要

Two genes, xynB and xynC, coding for xylanases were isolated from Thermotoga maritima FjSS3B.1 by a genomic-walking–PCR technique. Sequencing of the genes showed that they encode multidomain family 10 xylanases. Only XynB exhibited activity against xylan substrates. The temperature optimum (87°C) and pH optimum (pH 6.5) of XynB are different from the previously reported xylanase, XynA (also a family 10 enzyme), from this organism. The catalytic domain expressed without other domains has a lower temperature optimum, is less thermostable, and has optimal activity at pH 6.5. Despite having a high level of sequence similarity to xynB, xynC appears to be nonfunctional since its encoded protein did not show significant activity on xylan substrates.
机译:通过基因组步行PCR技术从海栖嗜热菌FjSS3B.1中分离出编码木聚糖酶的两个基因xynB和xynC。基因的测序表明它们编码多域家族10木聚糖酶。仅XynB表现出对木聚糖底物的活性。 XynB的最适温度(87°C)和最适pH(pH 6.5)与该生物先前报道的木聚糖酶XynA(也是10族酶)不同。在没有其他结构域的情况下表达的催化结构域具有较低的最佳温度,较低的热稳定性以及在pH 6.5下具有最佳活性。尽管与xynB具有高度的序列相似性,但xynC似乎是无功能的,因为其编码的蛋白质在木聚糖底物上未显示明显的活性。

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