Isolation of a multi-functional endogenous cellulase gene from mollusc, Ampullaria crossean.

Ji Wang, Ming Ding, Yan-Hong Li, Qing-Xi Chen, Gen-Jun Xu, Fu-Kun Zhao
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Abstract

The cellulase genes of some animals, most coding for endo-beta-1,4-glucanases, were found and cloned. There has been no reports about genes encoding exo-beta-1,4-glucanase or endo- -1,4-xylanase from animal. Here we cloned the cDNA of a cellulase designated as EGX from mollusc, Ampullaria crossean, and expressed it in Pichia pastoris for the first time. The cellulase EGX is a multi-functional beta cellulase with the activities of exo-beta-1,4-glucanase, endo-beta-1,4-glucanase and endo-beta-1,4-xylanase. The opening reading frame of EGX cDNA is 1185 bp and encodes 395 amino acids. The EGX gene can also be amplificated from the genomic DNA by PCR, which verified the endogenous origin of this gene. This EGX gene was the first multi-functional cellulase gene that was directly isolated from animals.

软体动物多功能内源纤维素酶基因的分离。
发现并克隆了一些动物的纤维素酶基因,其中大部分编码内切-1,4-葡聚糖酶。目前还没有从动物中发现编码外-1,4-葡聚糖酶或内-1,4-木聚糖酶基因的报道。本文从软体动物Ampullaria crossean中克隆了一种纤维素酶EGX的cDNA,并首次在毕赤酵母中表达。纤维素酶EGX是一种具有外-1,4-葡聚糖酶、内-1,4-葡聚糖酶和内-1,4-木聚糖酶活性的多功能纤维素酶。EGX cDNA的开放阅读框长1185 bp,编码395个氨基酸。通过PCR还可以从基因组DNA中扩增出EGX基因,验证了该基因的内源起源。该EGX基因是第一个直接从动物中分离得到的多功能纤维素酶基因。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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