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Updated: Feb 5, 2026

Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella
Published on: November 30, 2018
N-Terminal Domain Truncation and Domain Insertion-Based Engineering of a Novel Thermostable Type I Pullulanase from
Lingmeng Li1, Fengying Dong1, Lin Lin2,3
1State Key Laboratory of Bioreactor Engineering, Newworld Institute of Biotechnology , East China University of Science and Technology , Shanghai 200237 , People's Republic of China.
Abstract:
A novel thermostable type I pullulanase gene ( pul GT) from Geobacillus thermocatenulatus DSMZ730 was cloned. It has an open reading frame of 2154 bp encoding 718 amino acids. G. thermocatenulatus pullulanase (PulGT) was found to be optimally active at pH 6.5 and 70 °C. It exhibited stable activity in the pH range of 5.5-7.0. PulGT lacked three domains (CBM41 domain, X25 domain, and X45 domain) compared with the pullulanase from Bacillus acidopullulyticus ( 2WAN ). Different N-terminally domain truncated (730T) or spliced (730T-U1 and 730T-U2) mutants were constructed. Truncating the N-terminal 85 amino acids decreased the Km value and did not change its optimum pH, an advantageous biochemical property in some applications. Compared with 2WAN , PulGT can be used directly for maize starch saccharification without adjusting the pH, which reduces cost and improves efficiency.
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