Abstract: The halophilic proteinase showed a maximal activity
at 50°C and pH 9~10, in 20% NaCl and was highly stabilized by
NaCl. It was able to hydrolyse natural actomyosin (NAM), collagen
and anchovy protein. For NAM hydrolysis, the myosin heavy chain
was completely digested by halophilic proteinase as evidenced by the
lowest band intensity remaining, but partially hydrolysed actin. The
SR5-3 proteinase was also capable hydrolyzing two major
components of collagen, β- and α-compounds, effectively. The
degree of hydrolysis (DH) of the halophilic proteinase and
commercial proteinases (Novozyme, Neutrase, chymotrypsin and
Flavourzyme) on the anchovy protein, were compared, and it was
found that the proteinase showed a greater degree of hydrolysis
towards anchovy protein than that from commercial proteinases. DH
of halophilic proteinase was sharply enhanced according to the
increase in the concentration of enzyme from 0.035 U to 0.105 U.
The results warranting that the acceleration of the production of fish
sauce with higher quality, may be achieved by adding of the
halophilic proteinase from this bacterium.