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Asian-Australas J Anim Sci > Volume 14(12); 2001 > Article
Animal Products
Asian-Australasian Journal of Animal Sciences 2001;14(12): 1769-1774.
DOI: https://doi.org/10.5713/ajas.2001.1769    Published online December 1, 2001.
Comparison of Two Feather-Degrading Bacillus Licheniformis Strains
Xiang Lin, Soo-Won Lee, Hee Dong Bae, Jim A. Shelford, Kuo-Joan Cheng
Abstract
Bacillus licheniformis strains L-25 and PWD-1 are two thermophilic feather-degrading bacteria. Despite isolated from different environmental conditions, they were both capable of breaking down chicken feathers and growing in a medium in which feather was the only source of carbon and nitrogen. A 1.46-kb keratinase gene (ker B) was isolated from strain L-25 by a polymerase chain reaction (PCR) using L-25 genomic DNA as templates. Sequencing results reveal that ker B shares great sequence identity with a previously published keratinase gene of B. licheniformis PWD-1 (ker A). Only two amino acids differences were found in the deduced amino acid sequence between the keratinases from L-25 and PWD-1. However several nucleotide changes were found upstream of the putative promoter region. Protease inhibition studies indicated that neutral protease activity accounted for approximate 25 to 30% of total extracellular proteolytic activity produced by strain L-25 in the feather medium. In contrast, no measurable neutral protease activity was produced by strain PWD-1 in the feather medium. When glucose (1%), a common catabolic repressor, was added into the feather medium, L-25 was still able to grow and produce keratinase. Strain PWD-1 produced no neutral protease activity and its growth was severely inhibited in the feather medium containing glucose. L-25 produced an enhanced level of keratinase in the feather medium in comparison with PWD-1.
Keywords: Bacillus; Protease; Feather and Keratinase
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