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Proteomic investigation of the impact of oxygen on the protein profiles of hyaluronic acid‐producing Streptococcus zooepidemicus
Author(s) -
Wu TingFeng,
Huang WeiChih,
Chen YiChun,
Tsay YeouGuang,
Chang ChunSheng
Publication year - 2009
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200800868
Subject(s) - acetoin , biochemistry , dihydrolipoamide dehydrogenase , fermentation , bacteria , proteome , chemistry , metabolism , dehydrogenase , biology , enzyme , genetics
Abstract Hyaluronic acid (HA) is a linear and negatively charged polysaccharide regularly used in medicine and cosmetics. Recently Streptococcus zooepidemicus has been exploited in the fermentation industry to produce HA. Many studies showed that higher amounts of HA were produced under aerobic condition compared to anaerobic conditions. To explore the effect of oxygen on the HA synthesis in S . zooepidemicus , 2‐DE was used to compare the proteomes of aerobically and anaerobically fermented bacteria to identify proteins, which might be associated with the influence of oxygen on the HA synthesis. Totally nine pairs of 2‐DE gels collected from three batches were compared and nine overexpressed proteins were observed in aerobically fermented bacteria. These proteins were identified by LC/tandem MS as dihydrolipoamide dehydrogenase, UDP‐acetyl‐glucosamine pyrophosphoylase, dihydrolipoamide‐ S ‐acetyltransferase and acetoin dehydrogenase α and β chains, respectively. These upregulated proteins were involved in acetoin dissimilation, the central carbon metabolism and the HA anabolic pathway, implicating that oxygen might augment the expression of genes that are involved in central energy metabolism, acetoin reutilization and HA biosynthesis to enhance the amount of acetyl‐CoA as such that more acetyl‐CoA can be diverged from the central carbon metabolism to replenish acetyl‐CoA for the HA synthesis.