Simple jQuery Dropdowns
Please use this identifier to cite or link to this item:
Title: Purification and characterisation of keratinase from a thermotolerant feather-degrading bacterium
Authors: Worapot Suntornsuk
Junthip Tongjun
Poranee Onnim
Hiroshi Oyama
Kanok Ratanakanokchai
Thanit Kusamran
Kohei Oda
King Mongkuts University of Technology Thonburi
Kyoto Institute of Technology
Mahidol University
Keywords: Agricultural and Biological Sciences;Biochemistry, Genetics and Molecular Biology;Immunology and Microbiology
Issue Date: 1-Oct-2005
Citation: World Journal of Microbiology and Biotechnology. Vol.21, No.6-7 (2005), 1111-1117
Abstract: Isolation and identification of a thermotolerant feather-degrading bacterial strain from Thai soil as well as purification and properties of its keratinase were investigated. The thermotolerant bacterium was identified as Bacillus licheniformis. The keratinase was purified to homogeneity by three-step chromatography. The purified enzyme exhibited a high specific activity (218 U mg-1) with 86-fold purification and 25% yield. The enzyme was monomeric and had a molecular mass of 35 kDa. The optimum pH and temperature for the enzyme were 8.5 and 60°C, respectively. The enzyme activity was significantly inhibited by PMSF and partly inhibited by EDTA and iodoacetamide, but was stimulated by metal ions. It hydrolysed soluble proteins with a relative activity of 4-100% and insoluble proteins, including keratins, with a relative activity of 3-35%. Therefore, the enzyme could improve the nutritional value of meat- and poultry-processing wastes containing keratins, collagen and gelatin. © Springer 2005.
ISSN: 09593993
Appears in Collections:Scopus 2001-2005

Files in This Item:
There are no files associated with this item.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.