Cloning, Expression and Enzymatic Characterization of Chitin Deacetylase 4 from Hyphantria Cunea (Drury)
- Xiao-ping YAN, Dan ZHAO, Ya-kun ZHANG, Wei GUO, Kun-li ZHAO, Wei WANG, Yu-jie GAO
- Corresponding Author
- Xiao-ping YAN
Available Online May 2017.
- https://doi.org/10.2991/bbe-17.2017.54How to use a DOI?
- Hyphantria cunea, Chitin deacetylase, Enzymatic activity.
- A novel chitin deacetylase (CDA), HcCDA4, was identified from the American white moth, Hyphantria cunea. The full-length cDNA sequence of HcCDA4 was identified,and the cDNA is 1494bp in length. The HcCDA4 was shown as a 56 kDa protein in E. coli BL21 by SDS-PAGE analysis and the specific antibodies reacting to HcCDA4 were obtained by immunizing rabbits. The insect cells secreting expressed HcCDA4 proteins were used to study enzymatic properties. Results showed that HcCDA4 possessed catalytic activity, and the optimum temperature was 50§C and the optimum pH was 8.0. Under the optimum reaction conditions, the enzyme activities of HcCDA4 protein was 3.44 UúmL-1. The enzyme activity is enhanced in the presence of Zn2+, Mn2+ and Fe2+ ions, but inhibited in the presence of Mg2+and Co2+ ions, Ca 2+ showed a trend of increasing first and then decreasing on HcCDA4 enzymatic activity.
- Open Access
- This is an open access article distributed under the CC BY-NC license.
Cite this article
TY - CONF AU - Xiao-ping YAN AU - Dan ZHAO AU - Ya-kun ZHANG AU - Wei GUO AU - Kun-li ZHAO AU - Wei WANG AU - Yu-jie GAO PY - 2017/05 DA - 2017/05 TI - Cloning, Expression and Enzymatic Characterization of Chitin Deacetylase 4 from Hyphantria Cunea (Drury) BT - 2nd International Conference on Biomedical and Biological Engineering 2017 (BBE 2017) PB - Atlantis Press SN - 2468-5747 UR - https://doi.org/10.2991/bbe-17.2017.54 DO - https://doi.org/10.2991/bbe-17.2017.54 ID - YAN2017/05 ER -