Journal of Pure and Applied MicrobiologyVol. 8 No. 2

Proteomic Analysis of L-isoleucine Production by Corynebacterium glutamicum

Lianghong Yin1,2, Xiaoqing Hu1 and Xiaoyuan Wang1,2*

1State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, China. 2 Key Laboratory of Industrial Biotechnology of Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi 214122, China.

Received on 18 June 2013 and accepted on 09 August 2013

 

ABSTRACT

Corynebacterium glutamicum JHI3-156 is an L-isoleucine producing strain, but its metabolic mechanism is not fully understood. In this work, total proteins extracted from JHI3-156 and the wild type Corynebacterium glutamicum ATCC 13869 were comparatively analyzed by two-dimensional electrophoresis and MALDI-TOF mass spectrometry. About 750 protein spots were visualized on two-dimensional gels from both samples. Compared with the wild type ATCC13869, 82 proteins were up-regulated and 123 proteins were down-regulated in JHI3-156. There were 181 proteins observed only in ATCC13869 and 197 proteins observed only in JHI3-156. 13 protein spots from the ATCC13869 gel and 18 protein spots from the JHI3-156 gel were chosen and further analyzed by MALDI-TOF mass spectrometry. These proteins are involved in cell growth, L-isoleucine biosynthesis and stress response. This study provided some clues to understand the molecular and metabolic mechanisms that lead to the increased L-isoleucine production in Corynebacterium glutamicum.

Keywords : Corynebacterium glutamicum; proteomic analysis; L-isoleucine; two-dimensional electrophoresis.