Prospecting, production and thermodynamic profiling of feather degrading keratinolytic protease from Bacillus subtilis GH2

Abstract

Please read abstract in the article. HIGHLIGHTS • Dialysis and ammonium sulfate purification gave a purification yield of 1.99%. • Kinetic properties showed that the keratinase can bind to its substrate. • Thermodynamic parameters suggest that the enzyme is relatively thermostable.

Description

DATA AVAILABILITY : Data will be made available on request.

Keywords

Bacillus subtilis, Keratinase, Kinetics, Purification, Thermal-denaturation

Sustainable Development Goals

SDG-12: Responsible consumption and production

Citation

Alamnie, G., Bekele, T., Girma, A. & Malgas, S. 2026, 'Prospecting, production and thermodynamic profiling of feather degrading keratinolytic protease from Bacillus subtilis GH2', Biocatalysis and Agricultural Biotechnology, vol. 73, art. 103979, pp. 1-12, doi : 10.1016/j.bcab.2026.103979.