Characterization of L-aspartate-α-decarboxylase from Bacillus subtilis.
- Author:
Siying DENG
;
Junli ZHANG
;
Zhen CAI
;
Yin LI
- Publication Type:Journal Article
- MeSH:
Bacillus subtilis;
enzymology;
Bacterial Proteins;
genetics;
metabolism;
Corynebacterium glutamicum;
enzymology;
Escherichia coli;
enzymology;
Glutamate Decarboxylase;
genetics;
metabolism;
Industrial Microbiology;
Temperature;
beta-Alanine
- From:
Chinese Journal of Biotechnology
2015;31(8):1184-1193
- CountryChina
- Language:Chinese
-
Abstract:
As an important material in pharmaceutical and chemical industry, β-alanine was mainly produced by chemical methods. L-aspartate-α-decarboxylase could catalyze the α-decarboxylation from L-aspartate to β-alanine. Determinations for specific activities of PanDs from Escherichia coli, Corynebacterium glutamicum and Bacillus subtilis were performed in this study (0.98 U/mg, 7.52 U/mg and 8.4 U/mg respectively). The optimal temperature and pH of PanDs from C. glutamicum and B. subtilis were 65 degrees C, pH 6.5 and 60 degrees C, pH 6.5 respectively. According to our research, PanD from B. subtilis could be more appropriate for industrial application because of the higher activity and thermostability when compared to PanDs from E. coli and C. glutamicum which had been the most studied. We also analyzed and discussed the special post-translation self-cleavage phenomenon and the mechanism based inactivation.
