Wang Ji, Ding Ming, Li Yan-Hong, Chen Qing-Xi, Xu Gen-Jun, Zhao Fu-Kun
Key Laboratory of Proteomics, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, the Chinese Academy of Sciences, Shanghai 200031, China.
Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 2003 Oct;35(10):941-6.
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.
已发现并克隆了一些动物的纤维素酶基因,其中大多数编码内切β-1,4-葡聚糖酶。目前尚无关于动物来源的外切β-1,4-葡聚糖酶或内切β-1,4-木聚糖酶基因的报道。在此,我们首次从软体动物福寿螺中克隆了一种名为EGX的纤维素酶的cDNA,并在毕赤酵母中进行了表达。纤维素酶EGX是一种多功能β-纤维素酶,具有外切β-1,4-葡聚糖酶、内切β-1,4-葡聚糖酶和内切β-1,4-木聚糖酶的活性。EGX cDNA的开放阅读框为1185 bp,编码395个氨基酸。通过PCR也可从基因组DNA中扩增出EGX基因,这证实了该基因的内源起源。该EGX基因是首个直接从动物中分离得到的多功能纤维素酶基因。