Sorapukdee, Supaluk
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Preferred name
Sorapukdee, Supaluk
Alternative Name
Sorapukdee, S.
Main Affiliation
Email
supaluk.so@kmitl.ac.th
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Item type:Publication, Hydrolytic properties of crude protease from Bacillus subtilis subsp. Subtilis M13(2019-01-01); 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 50°C and pH 6.0 with citrate buffer. Furthermore, this enzyme was preferable to hydrolyze insoluble collagen, and followed by elastin at 37°C and pH 6.0. Maximum hydrolysis for collagen was showed by the highest release of amino acid at 998 μg/ml after incubation for 24 h, and elastin at 656 μg/ml after incubation for 12 h. However, the hydrolytic activity against myofibrillar protein extracted from meat was relatively lower than 3.3 μg/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. - Some of the metrics are blocked by yourconsent settings
Item type:Publication, Optimization of microbial collagenolytic enzyme production by Bacillus subtilis subsp. Subtilis S13 using Plackett-Burman and response surface methodology(2019-01-01); Bacillus subtilis subsp. subtilis S13, a new isolate from soil is found to be the collagenase producing bacteria. The results showed that gelatin concentration, initial pH, and incubation time were accounted for significant factors from PB design and then applied for a central composite design (CCD) under response surface methodology (RSM) for optimization of significant factors were performed. The optimum parameters for the enhancing gelatinase production through CCD and response surface methodology were 19 g/l of pork gelatin, initial pH 6.16 for culture medium, and 59 h of incubation time, which provided the predicted maximum collatinolytic activity of 65.36 U/ml. This condition allowed approximately increasing 4-folds as compared to un-optimized condition (15 U/ml). The obtained optimal activity of this enzyme might be expressed the potential collagenase for several applications including meat tenderizing enzyme.