Journal
LETTERS IN APPLIED MICROBIOLOGY
Volume 57, Issue 4, Pages 336-343Publisher
WILEY-BLACKWELL
DOI: 10.1111/lam.12118
Keywords
GH13 family; Industrial application; Pullulanase; Thermococcus kodakarensis KOD1
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Funding
- National Natural Science Foundation of China [31171794, 31201465]
- Natural Science Foundation of Jilin [201101018]
- College Students' Innovative Experiment Project from Jilin University [2012A82219]
- New Teacher Foundation from Ministry of Education [20120061120103]
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In this report, a glycoside hydrolase 13 family pullulanase gene (Tk0977) was cloned from a thermophilic anaerobic archaeon Thermococcus kodakarensis KOD1 (Pul-Tk). Pul-Tk encodes a protein of 765 amino acids including a putative 22-residue signal peptide. The protein has four consensus motives and a catalytic triad of glycoside hydrolase 13 family in the deduced amino acid sequence. The recombinant enzyme was expressed in Escherichiacoli and purified to homogeneity. Pul-Tk can hydrolyse both pullulan and soluble starch. The purified enzyme was optimal at pH55-60 and 100 degrees C and exhibited good stability over a broad pH range (4-8). The V-max and K-m values were 11839176molmg(-1)min(-1) and 037 +/- 002mgml(-1) for pullulan and 5319 +/- 1166molmg(-1)min(-1) and 036 +/- 005mgml(-1) for starch. All these favourable enzymatic properties make it valuable in various industries.
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