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Published on: April 16, 2018
Purification and functional characterization of thermostable 5-aminolevulinic acid synthases
Qinglong Meng1,2, Yanfei Zhang2, Chunling Ma2
1School of Chemical Engineering and Technology, Tianjin University, Tianjin, 300072, People's Republic of China.
Objectives:
As 5-aminolevulinic acid synthase (ALAS), the key enzyme for 5-aminolevulinic acid (ALA) synthesis, is unstable, we have sought to find thermostable ALASs from thermophilic organisms.
Results:
Three ALASs from thermophiles Geobacillus thermoglucosidasius (GT-ALAS), Laceyella sacchari (LS-ALAS) and Pseudomonas alcaliphila (PA-ALAS) were purified and characterized. All enzymes were more stable than two previously studied ALASs from Rhodopseudomonas palustris and Rhodobacter sphaeroides. There was almost no activity change after 60 h at 37 °C for the three thermostable enzymes. This contrasts with the other two enzymes which lost over 90 % activities in just 1 h. Furthermore, the specific activity of LS-ALAS (7.8 U mg(-1)) was also higher than any previously studied ALASs.
Conclusions:
Thermostable ALASs were found in thermophilic organisms and this paves the way for developing cell free processes for enzymatic production of ALA from bulk chemicals succinate and glycine.
