Purification and characterization of heat-stable alkaline proteinase from bigeye snapper (Priacanthus macracanthus) muscle.

@article{Benjakul2003PurificationAC,
  title={Purification and characterization of heat-stable alkaline proteinase from bigeye snapper (Priacanthus macracanthus) muscle.},
  author={Soottawat Benjakul and Wonnop Visessanguan and Kittima Leelapongwattana},
  journal={Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology},
  year={2003},
  volume={134 4},
  pages={
          579-91
        }
}
Heat-stable alkaline proteinase was purified from bigeye snapper (Priacanthus macracanthus) ordinary muscle by heat-treatment and a series of chromatographies including Phenyl-Sepharose 6 Fast Flow, Source 15Q and Superose 12 HR 10/30. It was purified to 5180-fold with a yield of 0.8%. The molecular weight of purified proteinase was estimated to be 72 kDa by gel filtration. The proteinase appeared as two proteinase activity bands with molecular weights of 66 and 13.7 kDa on non-reducing SDS… CONTINUE READING