Collagenolytic Activity of Serine Protease of Perionyx excavatus
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| Title | Collagenolytic Activity of Serine Protease of Perionyx excavatus |
| Authors | |
| Abstract | A serine collagenolytic protease was purified from the earthworm Perionyx excavates by DEAE-Sephadex A-50 and DEAE-Sephadex A-50 column. The molecular mass of the earthworm serine protease was estimated to be 35 kDa. The purified serine protease was optimally active at pH 6.8-7.8 and 55°C. In vitro studies on collagenolytic activity of this enzyme was also carried out using type I collagen. Hydrolysis of collagen using serine protease was characterized by the collagenolytic activity. The amount of hydroxyproline released (μg/ml) on untanned and tanned leather was monitored. Zymographic analysis was carried out using Collagen as substrate. |
| Publisher | Indian Society for Education and Environment (ISEE) |
| Date | 2011-03-01 |
| Source | Indian Journal of Science and Technology Volume 4, Issue 3, March 2011 |