Tsukagoshi N, Iritani S, Sasaki T, Takemura T, Ihara H, Idota Y, Yamagata H, Udaka S
J Bacteriol. 1985 Dec;164(3):1182-7. doi: 10.1128/jb.164.3.1182-1187.1985.
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.
枯草芽孢杆菌和短短芽孢杆菌47 - 5，携带位于pUB110（pBAM101）上的嗜热脂肪芽孢杆菌α -淀粉酶基因，通过该酶的热稳定性和NH2末端氨基酸序列测定，它们合成的α -淀粉酶与供体菌株相同。无论宿主如何，该酶的34个氨基酸的信号肽在两个丙氨酸残基之间的完全相同位点进行加工。短短芽孢杆菌47 - 5（pBAM101）在所检测的宿主中分泌该酶的效率最高，分别比嗜热脂肪芽孢杆菌、大肠杆菌HB101（pH1301）和枯草芽孢杆菌1A289（pBAM101）高出100倍、15倍和5倍。短短芽孢杆菌47 - 5（pBAM101）中该酶的高效分泌被认为是由于该生物体细胞壁的独特性质。
