Indian Journal of Science and Technology
Year: 2011, Volume: 4, Issue: 3, Pages: 197-200
S. Subathra1* , Mazher Sultana2 and Gnanamani3
1Dravidian University, Kuppam, AP, India
2Dept. of Advanced Zoology and Animal Biotechnology, Presidency College, Chennai, India
3Scientist, Central Leather Research Institute, Adyar, Chennai
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.
Keywords: Serine protease, collagen, Perionyx excavatus, earthworm, hydroxyproline.
Subscribe now for latest articles and news.