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