Autor: |
Yang-Dao, Wei, Ya, Li, Chun, Deng, Shi-Hua, Wu, Cui-Ji, Huang, Yi, Yi |
Rok vydání: |
2017 |
Předmět: |
|
Zdroj: |
The Journal of general and applied microbiology. 63(5) |
ISSN: |
1349-8037 |
Popis: |
A gene (gkdA) (741 bp) encoding a putative protein of 247 amino acids was cloned from the Bacillus licheniformis SR01. The protein was expressed in Escherichia coli BL21 with a molecular mass estimated by SDS-PAGE of approximately 28.03 kDa and showed a calculating isoelectric point (pI) of 6.42. Structure analysis and function identification showed that the enzyme was a multifunctional glycosidase. Its specific activity was 0.013 U/μg. The recombinant glycosidase showed a maximum activity at 50°C and pH 7.0. It was very stable below 90°C and may have heat activation at higher temperatures. The relative residual activity was still more than 80% after 120 min at pH 5.0-10.0. The enzyme activity was inhibited by Cu |
Databáze: |
OpenAIRE |
Externí odkaz: |
|