Abstract
We report here a novel keratinase from Bacillus subtilis that has the potential to replace sodium sulfide in the dehairing process of leather industry. The Protease enzyme produced at laboratory condition has been characterized for its rate of enzyme production, and the environmental influencing factors such as pH and temperature on the activity of the enzyme has also been evaluated. The enzyme produced in pilot scale has been subjected to in vitro (spectrophotometrically) as well as in vivo assay (on wet goat skin for hair removal). The organism grown in the Dye's synthetic medium at 5.3mg/ml of cell dry weight produced 548 U/ml of protease. The in vitro enzyme activity increased with temperature within a range of 25°C to 35°C and found maximum at 45°C and at pH 11. An index of dehairing comparable to the use of conventional sodium sulfide method was achieved in 7 h of its application on wet goat skin.
Highlights
Enzymes are vitally important to the existence of life itself
Despite making significant contributions to the economy, the leather industry causes severe environmental pollution owing to the use of various chemicals and the release of a variety of detrimental materials
Tanneries are constantly concerned with the obnoxious odor and the pollution caused by the extremely toxic sodium sulfide used in the dehairing process
Summary
Enzymes are vitally important to the existence of life itself. Civilizations have used enzymes for thousands of years without understanding what they were or how they work. 50% of the enzymes produced is used for industrial process (Pepper et al, 1963). Chloride -5mg; magnesium sulfate- 10mg; boric acidthe use of enzymes in leather manufacturing process 5mg; zinc sulfate- 5mg; Make up to 10 ml with distilled for unhairing has not been accepted by the water.
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