Instituto de Biotecnología, Facultad de Bioquímica Química y Farmacia, Universidad Nacional de Tucumán, Tucumán, Argentina.
Curr Microbiol. 2009 Dec;59(6):646-50. doi: 10.1007/s00284-009-9489-5. Epub 2009 Sep 1.
Antifungal proteins produced by Bacillus sp. IBA 33 were purified by ammonium sulfate precipitation and DEAE-Sephacel column chromatography. The two purified proteins inhibited the growth of Geotrichum candidum, the sour rot disease agent in lemon. The proteins were stable at 20 (3 months), 40, 60 and 100 degrees C (30 min) and remained active after sterilization at 121 degrees C for 15 min. Their hydrophobic nature was proved and when were developed with ninhydrin they did not show any free amino groups. The infrared spectrum showed vibrational modes corresponding to peptide, ester or ketone links and saturated CH links corresponding to long chain fatty acids. UV scan spectroscopy showed tyrosine and or tryptophan amino acids in their composition. The remarkable thermo-resistance of proteins may be a good feature to be used in the development of a new biocontrol method of Geotrichum candidum.
由芽孢杆菌 IBA 33 产生的抗真菌蛋白通过硫酸铵沉淀和 DEAE-葡聚糖凝胶柱层析进行纯化。这两种纯化的蛋白抑制了柠檬中导致酸腐病的念珠菌的生长。这些蛋白在 20°C（3 个月）、40°C、60°C 和 100°C（30 分钟）下稳定，并且在 121°C 下灭菌 15 分钟后仍然保持活性。它们的疏水性得到了证明，并且在用茚三酮显色时，它们没有显示任何游离氨基。红外光谱显示与肽、酯或酮键以及对应长链脂肪酸的饱和 CH 键相对应的振动模式。紫外扫描光谱显示其组成中含有酪氨酸和/或色氨酸氨基酸。蛋白的显著耐热性可能是开发针对念珠菌的新型生物防治方法的一个很好的特征。
