Purification and characterization of a carboxymethyl cellulase from Artemia salina

Cited 14 time in scopus
Metadata Downloads
Purification and characterization of a carboxymethyl cellulase from Artemia salina
H W Zin; Kwang Hyun Park; T J Choi
Bibliographic Citation
Biochemical and Biophysical Research Communications, vol. 443, no. 1, pp. 194-199
Publication Year
Brine shrimp (Artemia salina) belong to a group of crustaceans that feed on microalgae and require a cellulase enzyme that can be used in ethanol production from marine algae. Protein with potential cellulase activity was purified and the activity analyzed under different conditions. After initial identification of cellulase activity by CMC cellulase, surface sterilization and PCR using 16s rRNA primers was conducted to confirm that the cellulase activity was not produced from contaminating bacteria. The enzyme was purified by ammonium sulfate fractionation, gel filtration, and ion exchange chromatography. After the final purification, a 70-fold increase in specific enzyme activity was observed. SDS-PAGE results revealed that the cellulase enzyme had a molecular mass of 96. kDa. Temperature, pH, and salinity values were found to be optimal at 55 °C, pH 8.0, and 600. mM NaCl, respectively. Specifically, the enzyme showed a fivefold increase in enzyme activity in seawater compared to 600. mM NaCl in phosphate buffer. Further analysis of the purified enzyme by molecular spectrometry showed no match to known cellulases, indicating this enzyme could be a novel halophilic cellulase that can be used for the production of bioethanol from marine macroalgae.
Appears in Collections:
Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.

Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.