A new strain of Bacillus subtilis subsp. subtilis M13 which isolated from meat is
proved to be the collagenase producing bacteria based on high degradation of denatured form of
collagen or gelatin. The molecular weight of the crude enzyme was approximately be 21 kDa
by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Maximum
collagenolytic activity based on gelatin as a substrate was attained at 50C and pH 6.0 with
citrate buffer. Furthermore, this enzyme was preferable to hydrolyze insoluble collagen, and
followed by elastin at 37C and pH 6.0. Maximum hydrolysis for collagen was showed by the
highest release of amino acid at 998 g/ml after incubation for 24 h, and elastin at 656 g/ml
after incubation for 12 h. However, the hydrolytic activity against myofibrillar protein extracted
from meat was relatively lower than 3.3 g/ml at 6 h. There was found either no or slightly
hydrolytic effect after prolonged incubation. The results indicated the potential protease for
using as meat tenderizing enzyme with high degradation of collagen and elastin with low
hydrolysis of meat myofibrillar protein.