Heterologous expression of acyl-ACP desaturase （FAB2） from Chlamydomonas reinhardi in Escherichia coli and its expres- sion features in response to different temperature and salinity stresses
Fatty acid desaturases are enzymes that introduce double bonds into the hydrocarbon chains of fatty acids. The expression of genes for desaturase is very important since it provides the molecular basis for the acclimation of organisms to changing environment. The plastid acyl-ACP desaturase（FAB2） from Chlamydomonas reinhardi is a kind of A9 desaturase, which catalyses the formation of a double bond between the ninth and tenth carbon in the fatty acid chain. In this paper, acyl-ACP desaturase （FAB2） From C. reinhardi was heterologous expressed in Escherichia coli. Homologous annlysis indicated that amino sequence of FAB2 is quite similar to those homologies from plants. The expression levels of FAB2 from C. reinhardi cells which under different temperature and salinity stresses were relatively analysised by using fluorescent quantitative real-time PCR technology. Results showed that the expression quantity of FAB2 during 4℃＋0%NaC1, 25℃ ＋ 1%NaCl were much higer than that of normal situations.
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