首页> 美国卫生研究院文献>Journal of Bacteriology >Efficient synthesis and secretion of a thermophilic alpha-amylase by protein-producing Bacillus brevis 47 carrying the Bacillus stearothermophilus amylase gene.
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Efficient synthesis and secretion of a thermophilic alpha-amylase by protein-producing Bacillus brevis 47 carrying the Bacillus stearothermophilus amylase gene.

机译:通过携带嗜热脂肪芽孢杆菌淀粉酶基因的产蛋白短芽孢杆菌47高效合成和分泌嗜热α-淀粉酶。

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摘要

Bacillus subtilis and Bacillus brevis 47-5, carrying the Bacillus stearothermophilus alpha-amylase gene on pUB110 (pBAM101), synthesized the same alpha-amylase as the donor strain as determined by the enzyme's thermal stability and NH2-terminal amino acid sequence. Regardless of the host, the 34-amino acid signal peptide of the enzyme was processed at exactly the same site between two alanine residues. B. brevis 47-5(pBAM101) secreted the enzyme most efficiently of the hosts examined, 100, 15, and 5 times more than B. stearothermophilus, Escherichia coli HB101(pH1301), and B. subtilis 1A289(pBAM101), respectively. The efficient secretion of the enzyme in B. brevis 47-5(pBAM101) was suggested to be due to the unique properties of the cell wall of this organism.
机译:枯草芽孢杆菌和短杆菌芽孢杆菌47-5在pUB110(pBAM101)上带有嗜热脂肪芽孢杆菌α-淀粉酶基因,合成了与供体菌株相同的α-淀粉酶,这是通过酶的热稳定性和NH2末端氨基酸序列确定的。无论宿主如何,都在两个丙氨酸残基之间的完全相同位点加工该酶的34个氨基酸的信号肽。短小芽孢杆菌47-5(pBAM101)分泌的酶最有效,分别是嗜热脂肪芽孢杆菌,大肠杆菌HB101(pH1301)和枯草芽孢杆菌1A289(pBAM101)的100、15和5倍。该酶在短小芽孢杆菌47-5(pBAM101)中的有效分泌被认为是由于这种生物的细胞壁的独特特性所致。

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