Collagenolytic activity of serine protease of Perionyx excavatus

S  Subathra; Mazher Sultana  and Gnanamani

doi:10.17485/ijst/2011/v4i3.25

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Collagenolytic activity of serine protease of Perionyx excavatus

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Indian Journal of Science and Technology

DOI: 10.17485/ijst/2011/v4i3.25

Year: 2011, Volume: 4, Issue: 3, Pages: 197-200

Original Article

Collagenolytic activity of serine protease of Perionyx excavatus

S. Subathra^1* , 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
[email protected]

This work is licensed under a Creative Commons Attribution 4.0 International License.

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.
Keywords: Serine protease, collagen, Perionyx excavatus, earthworm, hydroxyproline.