FRAGMENTATION AND CHARACTERISTICS OF RECOMBINANT ENDOCHITINASE EXPRESSED IN ESCHERICHIA COLI

Authors

Wei-Ming Chen, Department of Food Science, National Taiwan Ocean University, Keelung, Taiwan, R.O.C. Taiwan Agricultural Chemicals and Toxic Substances Research Institute, Taichung, Taiwan, R.O.C.
Gen-Hung Chen, Department of Cosmetic Science, Providence University, Taichung, Taiwan, R.O.C.
Shann-Tzong Jiang, Department of Food Science, National Taiwan Ocean University, Keelung, Taiwan, R.O.C. Department of Food and Nutrition, Providence University, Taichung, Taiwan, R.O.C.Follow

Abstract

A recombinant endochitinase fused with hexahistidine (rEC-H) was expressed and characterized. After Ni affinity chromatography, the recovery, purification-fold and specific activity of rEC-H were 88.8%, 13.4 and 142.1 U/mg, respectively. The purified rEC-H had optimal pH and temperature at pH 7.5 and 60°C, respectively and was stable at pH 4.0-9.0 and

Recommended Citation

Chen, Wei-Ming; Chen, Gen-Hung; and Jiang, Shann-Tzong (2012) "FRAGMENTATION AND CHARACTERISTICS OF RECOMBINANT ENDOCHITINASE EXPRESSED IN ESCHERICHIA COLI," Journal of Marine Science and Technology: Vol. 20: Iss. 4, Article 4.
DOI: 10.6119/JMST-011-0225-1
Available at: https://jmstt.ntou.edu.tw/journal/vol20/iss4/4