Institute of Life Sciences, Jiangsu University, #301 Xuefu Road, Zhenjiang, Jiangsu, People's Republic of China.
Curr Microbiol. 2011 Aug;63(2):198-205. doi: 10.1007/s00284-011-9967-4. Epub 2011 Jun 12.
Natural wild-type strains of Bacillus subtilis spore is regarded as a non-pathogenic for both human and animal, and has been classified as a novel food which is currently being used as probiotics added in the consumption. To identify B. subtilis spore proteins, we have accomplished a preliminary proteomic analysis of B. subtilis spore, with a combination of two-dimensional electrophoretic separations and matrix-assisted laser desorption ionization tandem time of flight mass spectrometry (MALDI-TOF-MS). In this article, we presented a reference map of 158 B. subtilis spore proteins with an isoelectric point (pI) between 4 and 7. Followed by mass spectrometry (MS) analysis, we identified 71 B. subtilis spore proteins with high level of confidence. Database searches, combined with hydropathy analysis and GO analysis revealed that most of the B. subtilis spore proteins were hydrophilic proteins related to catalytic function. These results should accelerate efforts to understand the resistance of spore to harsh conditions.
枯草芽孢杆菌天然野生型孢子被认为对人类和动物均无致病性,已被归类为新型食品,目前作为益生菌添加到消费中。为了鉴定枯草芽孢杆菌孢子蛋白,我们采用二维电泳分离和基质辅助激光解吸电离串联飞行时间质谱(MALDI-TOF-MS)相结合的方法,对枯草芽孢杆菌孢子进行了初步的蛋白质组学分析。在本文中,我们提供了一个参考图谱,图谱上有 158 种等电点(pI)在 4 到 7 之间的枯草芽孢杆菌孢子蛋白。通过质谱(MS)分析,我们鉴定出 71 种枯草芽孢杆菌孢子蛋白,置信度较高。数据库搜索,结合疏水性分析和 GO 分析表明,大多数枯草芽孢杆菌孢子蛋白是与催化功能相关的亲水蛋白。这些结果将加速对孢子抗恶劣条件能力的理解。